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1.
Cotyledons of tomato seedlings that germinated in a 20 µM AlK(SO4)2 solution remained chlorotic while those germinated in an aluminum free medium were normal (green) in color. Previously, we have reported the effect of aluminum toxicity on root proteome in tomato seedlings (Zhou et al.1). Two dimensional DIGE protein analysis demonstrated that Al stress affected three major processes in the chlorotic cotyledons: antioxidant and detoxification metabolism (induced), glyoxylate and glycolytic processes (enhanced), and the photosynthetic and carbon fixation machinery (suppressed).Key words: aluminum, cotyledons, proteome, tomatoDifferent biochemical processes occur depending on the developmental stages of cotyledons. During early seed germination, before the greening of the cotyledons, glyoxysomes enzymes are very active. Fatty acids are converted to glucose via the gluconeogenesis pathway.2,3 In greening cotyledons, chloroplast proteins for photosynthesis and leaf peroxisomal enzymes in the glycolate pathway for photorespiration are metabolized.2–4 Enzymes involved in regulatory mechanisms such as protein kinases, protein phosphatases, and mitochondrial enzymes are highly expressed.3,5,6The chlorotic cotyledons are similar to other chlorotic counterparts in that both contains lower levels of chlorophyll, thus the photosynthetic activities are not as active. In order to understand the impact of Al on tomato cotyledon development, a comparative proteome analysis was performed using 2D-DIGE following the as previously described procedure.1 Some proteins accumulated differentially in Al-treated (chlorotic) and untreated cotyledons (Fig. 1). Mass spectrometry of tryptic digestion fragments of the proteins followed by database search has identified some of the differentially expressed proteins (Open in a separate windowFigure 1Image of protein spots generated by Samspot analysis of Al treated and untreated tomato cotyledons proteomes separated on 2D-DIGE.
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Table 1
Proteins identified from tomato cotyledons of seeds germinating in Al-solutionSpot No. | Fold (treated/ctr) | ANOVA (p value) | Annotation | SGN accession |
1 | 2.34 | 0.001374 | 12S seed storages protein (CRA1) | SGN-U314355 |
2 | 2.13 | 0.003651 | unidentified | |
3 | 2.0 | 0.006353 | lipase class 3 family | SGN-U312972 |
4 | 1.96 | 0.002351 | large subunit of RUBISCO | SGN-U346314 |
5 | 1.95 | 2.66E-05 | arginine-tRNA ligase | SGN-U316216 |
6 | 1.95 | 0.003343 | unidentified | |
7 | 1.78 | 0.009219 | Monodehydroascorbate reductase (NADH) | SGN-U315877 |
8 | 1.78 | 0.000343 | unidentified | |
9 | 1.75 | 4.67E-05 | unidentified | |
12 | 1.70 | 0.002093 | unidentified | |
13 | 1.68 | 0.004522 | unidentified | |
15 | 1.66 | 0.019437 | Glutamate dehydrogenase 1 | SGN-U312368 |
16 | 1.66 | 0.027183 | unidentified | |
17 | 1.62 | 2.01E-08 | Major latex protein-related, pathogenesis-related | SGN-U312368 |
18 | −1.61 | 0.009019 | RUBisCo activase | SGN-U312543 |
19 | 1.61 | 0.003876 | Cupin family protein | SGN-U312537 |
20 | 1.60 | 0.000376 | unidentified | |
22 | 1.59 | 0.037216 | unidentified | |
0.003147 | unidentified | |||
29 | −1.56 | 0.001267 | RUBisCo activase | SGN-U312543 |
35 | 1.52 | 0.001955 | unidentified | |
40 | 1.47 | 0.007025 | unidentified | |
41 | 1.47 | 0.009446 | unidentified | |
45 | 1.45 | 0.001134 | unidentified | |
59 | −1.40 | 5.91E-05 | 12 S seed storage protein | SGN-U314355 |
61 | 1.39 | 1.96E-05 | MD-2-related lipid recognition domain containing protein | SGN-U312452 |
65 | 1.37 | 0.000608 | triosephosphate isomerase, cytosolic | SGN-U312988 |
68 | 1.36 | 0.004225 | unidentified | |
81 | 1.32 | 0.001128 | unidentified | |
82 | −1.31 | 0.001408 | 33 kDa precursor protein of oxygen-evolving complex | SGN-U312530 |
87 | 1.30 | 0.002306 | unidentified | |
89 | −1.3 | 0.000765 | unidentified | |
92 | 1.29 | 0.000125 | superoxide dismutase | SGN-U314405 |
98 | 1.28 | 0.000246 | triosephosphate isomerase, cytosolic | SGN-U312988 |
2.
Up to 60 different proteins are recruited to the site of clathrin-mediated endocytosis in an ordered sequence. These accessory proteins have roles during all the different stages of clathrin-mediated endocytosis. First, they participate in the initiation of the endocytic event, thereby determining when and where endocytic vesicles are made; later they are involved in the maturation of the clathrin coat, recruitment of specific cargo molecules, bending of the membrane, and finally in scission and uncoating of the nascent vesicle. In addition, many of the accessory components are involved in regulating and coupling the actin cytoskeleton to the endocytic membrane. We will discuss the different accessory components and their various roles. Most of the data comes from studies performed with cultured mammalian cells or yeast cells. The process of endocytosis is well conserved between these different organisms, but there are also many interesting differences that may shed light on the mechanistic principles of endocytosis.Receptor-mediated endocytosis is the process by which eukaryotic cells concentrate and internalize cell surface receptors from the plasma membrane into small (∼50 nm– ∼100 nm diameter) membrane vesicles (Chen et al. 2011; McMahon and Boucrot 2011; Weinberg and Drubin 2012). This mechanism has been studied extensively in mammalian tissue culture cells and in yeast, and despite the evolutionary distance between yeast and mammalian cells the mechanism of receptor-mediated endocytosis in the respective cell types show remarkable similarities. Indeed many of the ∼60 endocytic accessory proteins (EAPs) found in yeast have homologs in mammalian cells, although both cell types also have unique EAPs (McMahon and Boucrot 2011; Weinberg and Drubin 2012).In the following, we briefly describe known yeast and mammalian EAPs (Sigismund et al. 2012; see also Bökel and Brand 2013; Cosker and Segal 2014; Di Fiore and von Zastrow 2014).
Open in a separate windowThe proteins are grouped into functional categories and the homologous proteins are listed on the same line. 相似文献
Table 1.
Key endocytic proteins in mammals and in yeastMammals | Yeast | Function | |
---|---|---|---|
Coat proteins | Clathrin | Chc1, Clc1 | Coat protein |
AP-2 (4 subunits) | AP-2 (4 subunits) | Adaptor protein | |
Epsin | Ent1/2 | Adaptor protein | |
AP180 | Yap1801/2 | Adaptor protein | |
CALM | – | Adaptor protein | |
NECAP | – | Adaptor protein | |
FCHo1/2 | Syp1 | Adaptor protein | |
Eps15 | Ede1 | Scaffold protein | |
Intersectin | Pan1 | Scaffold protein | |
– | Sla1 | Scaffold protein | |
– | End3 | Scaffold protein | |
N-BAR proteins | Amphiphysin | Rvs161/167 | Membrane curvature sensor/generator |
Endophilin | – | Membrane curvature sensor/generator | |
BIN1 | – | Membrane curvature sensor/generator | |
Dynamin | Dynamin1/2 | Vps1 | Mechanoenzyme, GTPase |
Actin cytoskeleton | Actin | Act1 | Actin monomer |
Arp2/3 complex | Arp2/3 complex | Actin filament nucleator | |
ABP1 | Abp1 | Actin-binding protein | |
Cortactin | – | Actin-binding protein | |
Coronin | Crn1 | Actin-binding protein | |
Cofilin | Cof1 | Actin depolymerizing protein | |
Actin regulators | Myosin 1E | Myo3/5 | Actin motor |
Myosin 6 | Actin motor | ||
Hip1R, Hip1 | Sla2 | Actin-membrane coupler | |
Syndapin | Bzz1 | BAR domain protein | |
N-WASP | Las17 | Regulator of actin nucleation | |
WIP/WIRE | Vrp1 | Regulator of actin nucleation | |
SNX9 | – | Regulator of actin nucleation | |
– | Bbc1 | Regulator of actin nucleation | |
Other regulators | AAK1 | Ark1/Prk1 | Protein kinase |
Auxilin, GAK | – | Uncoating factor | |
Synaptojanin | Sjl2 | Lipid phosphatase | |
OCRL1 | – | Lipid phosphatase |
3.
4.
5.
All published records for the 49 species of moth flies known from North Africa are reviewed and discussed: Morocco (27 species), Algeria (33 species), Tunisia (18 species) and Egypt (five species). In addition, records of seven species of Psychodinae new to the fauna of Morocco are added, of which three are new mentions for North Africa (Table (Table1)1) and one is a new record for Egypt. Telmatoscopus
squamifer Tonnoir, 1922 is transferred to the genus Iranotelmatoscopus Ježek, 1987, comb. n. Satchelliella
reghayana Boumezzough & Vaillant, 1987 is transferred to the genus Pneumia Enderlein, 1935, comb. n. Pneumia
aberrans Tonnoir, 1922 is transferred to the subgenus Logima.
Open in a separate windowX***: new species for North Africa; X**: new species for Morocco or Egypt; X*: new species for the Rif Mountains. 相似文献
Table 1.
Species (in alphabetical order) of Psychodinae known from the North African countries. Libya has been omitted because no information exists in the literature from Libya.Morocco | Algeria | Tunisia | Egypt | |
---|---|---|---|---|
Bazarella atra (Vaillant, 1955) | X* | X | ||
Berdeniella lucasii (Satchell, 1955) | X | |||
Clogmia albipunctata (Williston, 1893) | X** | X | X | |
Clytocerus kabylicus Wagner, 1987 | X | |||
Iranotelmatoscopus numidicus (Satchell, 1955) | X | |||
Iranotelmatoscopus squamifer (Tonnoir, 1922) | X | |||
Lepiseodina tristis (Meigen, 1830) | X | |||
Mormia tenebricosa (Vaillant, 1954) | X* | X | X | |
Mormia riparia (Satchell, 1955) | X | |||
Mormia similis Wagner, 1987 | X | |||
Panimerus goetghebueri (Tonnoir, 1919) | X | X | ||
Panimerus thienemanni (Vaillant, 1954) | X | X | X | |
Paramormia ustulata (Walker, 1856) | X* | X | X | |
Pericoma barbarica Vaillant, 1955 | X* | X | X | |
Pericoma blandula Eaton, 1893 | X | X | X | |
Pericoma diversa Tonnoir, 1920 | X* | |||
Pericoma exquisita Eaton, 1893 | X | X | X | |
Pericoma granadica Vaillant, 1978 | X* | |||
Pericoma latina Sarà, 1954 | X* | X | ||
Pericoma maroccana Vaillant, 1955 | X* | |||
Pericoma modesta Tonnoir, 1922 | X | X | ||
Pericoma pseudexquisita Tonnoir, 1940 | X*** | |||
Philosepedon beaucournui Vaillant, 1974 | X | X | ||
Philosepedon humerale (Meigen, 1818) | X** | X | ||
Pneumia nubila (Meigen, 1818) | X*** | |||
Pneumia pilularia (Tonnoir, 1940) | X | X | ||
Pneumia propinqua (Satchell, 1955) | X** | X | ||
Pneumia reghayana (Boumezzough & Vaillant, 1986) | X | |||
Pneumia toubkalensis (Omelková & Ježek 2012) | X* | |||
Psychoda aberrans Tonnoir, 1922 | X | |||
Psychoda (Falsologima) savaiiensis Edwards, 1928 | X | |||
Psychoda (Logima) albipennis Zetterstedt, 1850 | X | X | ||
Psychoda (Logima) erminea Eaton, 1893 | X | |||
Psychoda (Psycha) grisescens Tonnoir, 1922 | X | X | X | |
Psychoda (Psychoda) phalaenoides (Linnaeus, 1758) | X | |||
Psychoda (Psychoda) uniformata Haseman, 1907 | X | |||
Psychoda (Psychodocha) cinerea Banks, 1894 | X** | X | X | |
Psychoda (Psychodocha) gemina (Eaton, 1904) | X*** | |||
Psychoda (Psychomora) trinodulosa Tonnoir, 1922 | X | |||
Psychoda (Tinearia) alternata Say, 1824 | X* | X | X | X** |
Psychoda (Tinearia) efflatouni Tonnoir, 1922 | X | |||
Psychoda (Tinearia) lativentris Berden, 1952 | X | |||
Telmatoscopus advena (Eaton, 1893) | X | |||
Thornburghiella quezeli (Vaillant, 1955) | X | X | ||
Tonnoiriella atlantica (Satchell, 1953) | X | X | ||
Tonnoiriella paveli Ježek, 1999 | X | |||
Tonnoiriella pulchra (Eaton, 1893) | X | X | ||
Vaillantodes fraudulentus (Eaton, 1896) | X | X | ||
Vaillantodes malickyi (Wagner, 1987) | X |
6.
Halyna R Shcherbata 《EMBO reports》2022,23(5)
The Invasion of Ukraine prompts us to support our Ukranian colleagues but also to keep open communication with the Russian scientists who oppose the war. In the eyes of the civilized world, Russia has already lost the war: politically, it is becoming ever more isolated; economically as the sanctions take an enormous toll; militarily as the losses of the Russian army mount. In contrast, the courage of Ukrainian people fighting for their independence has united the Western world that is providing enormous support for those Ukrainians who fight the Russian invasion and those who have fled their war‐torn country. Once this war is over, Ukraine will have to heal the wounds of war, reunite families, restore its economy, reestablish infrastructure, and rebuild science and education. Russia will have to restore its dignity and overcome its self‐inflicted isolation.Europe’s unity in condemning Russia’s war of aggression and showing its solidarity with Ukraine has been impressive. This includes not the least welcoming and accommodating millions of refugees. We, the scientific community in Europe, have a moral obligation to help Ukrainian students and colleagues by providing safe space to study and to continue their research. First, European research organizations and funding agencies should develop strategies to support them in the years to come. Second, efforts by EMBO, research funders, universities, and research institutions to support Ukrainian students and scientists are necessary. As a first priority, dedicated and unbureaucratic short‐term scholarship and grant programs are required to accommodate Ukrainian scientists; such programs have been already initiated by many organizations, for example, by EMBO, Volkswagen Stiftung, Max Planck Society, and the ERC among others. These help Ukrainian scientists to stay connected to research and become integrated into the European research landscape. In the long‐term and after the war, this aid should be complemented by funding for research centers of excellence in Ukraine, to which scientists could then return.Even though the priority must be to help Ukrainians, we must also think of students and colleagues in Russia who oppose the war and are affected by the sanctions. As the Iron Curtain closes again, we have to think differently about our ongoing and future collaborations. Although freezing most, if not all, research collaborations with official Russian organizations is justified, it would be a mistake to extend these sanctions to all scientists and students. There is already an exodus of Russian and Belarusian scholars, which will only accelerate in the next months and years, and accepting scientists who ask for political asylum will be beneficial for Europe.The fraction of Russian society in open opposition to the war is, unfortunately, smaller than that officially in support of it. At the beginning of the war, a number of Russian scientists published an open letter on the internet, in which they condemn this war (https://t‐invariant.org/2022/02/we‐are‐against‐war/). They clearly state that "The responsibility for unleashing a new war in Europe lies entirely with Russia. There is no rational justification for this war”, and “demand an immediate halt to all military operations directed against Ukraine". At the same time, other prominent Russian science and education officials signed the “Statement of the Russian Union of University Rectors (Provosts)”, which expressed unwavering support for Russia, its president and its Army and their goal to “to achieve demilitarization and denazification of Ukraine and thus to defend ourselves from the ever‐growing military threat” (https://www.rsr‐online.ru/news/2022‐god/obrashchenie‐rossiyskogo‐soyuza‐rektorov1/).Inevitably, Russian scientists must decide themselves how to live and continue their scientific work under the increasingly tight surveillance of the Kremlin regime. History is repeating itself. Not long ago, during the Cold War, Soviet scientists were largely isolated from the international research community and worked in government‐controlled research. In some fields, no one knew what they were working on or where. However, even in those dark times, courageous individuals such as Andrei Sakharov spoke out against the regime and tried to educate the next generation about the importance of free will. Many Soviet geneticists had been arrested under Stalin’s regime of terror and as a result of Lysenkoism and were executed or sent to the Gulag or had to emigrate, such as Nikolaj Timofeev‐Resovskij, one of the great geneticists of his time and an opponent of communism. As a result of sending dissident scientists to Siberia, great educational institutions were created in the region, which trained many famous scientists. History tells us that it is impossible to kill free will and the search for truth.The Russian invasion of Ukraine is a major humanitarian tragedy and a tragedy for science at many levels. Our hope is that the European science community, policymakers, and funders will be prepared to continue and expand support for our colleagues from Ukraine and eventually help to rebuild the bridges with Russian science that have been torn down.This commentary has been endorsed and signed by the EMBO Young Investigators and former Young Investigators listed below. All signatories are current and former EMBO Young Investigators and endorse the statements in this article.
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Igor Adameyko | Karolinska Institut, Stockholm, Sweden |
Bungo Akiyoshi | University of Oxford, United Kingdom |
Leila Akkari | Netherlands Cancer Institute, Amsterdam, Netherlands |
Panagiotis Alexiou | Masaryk University, Brno, Czech Republic |
Hilary Ashe | Faculty of Life Sciences, University of Manchester, United Kingdom |
Michalis Averof | Institut de Génomique Fonctionnelle de Lyon (IGFL), France |
Katarzyna Bandyra | University of Warsaw, Poland |
Cyril Barinka | Institute of Biotechnology AS CR, Prague, Czech Republic |
Frédéric Berger | Gregor Mendel Institute of Molecular Plant Biology, Austrian Academy of Sciences, Vienna, Austria |
Vitezslav Bryja | Institute of Experimental Biology, Masaryk University, Brno, Czech Republic |
Janusz Bujnicki | International Institute of Molecular and Cell Biology, Warsaw, Poland |
Björn Burmann | University Gothenburg, Sweden |
Andrew Carter | MRC Laboratory of Molecular Biology, Cambridge, United Kingdom |
Pedro Carvalho | Sir William Dunn School of Pathology University of Oxford, United Kingdom |
Ayse Koca Caydasi | Koç University, Istanbul, Turkey |
Hsu‐Wen Chao | Medical University, Taipei, Taiwan |
Jeffrey Chao | Friedrich Miescher Institute, Basel, Switzerland |
Alan Cheung | University of Bristol, United Kingdom |
Tim Clausen | Research Institute for Molecular Pathology (IMP), Vienna, Austria |
Maria Luisa Cochella | The Johns Hopkins University School of Medicine, USA |
Francisco Cubillos | Santiago de Chile, University, Chile |
Uri Ben‐David | Tel Aviv University, Tel Aviv, Israel |
Sebastian Deindl | Uppsala University, Sweden |
Pierre‐Marc Delaux | Laboratoire de Recherche en Sciences Végétales, Castanet‐Tolosan, France |
Christophe Dessimoz | University, Lausanne, Switzerland |
Maria Dominguez | Institute of Neuroscience, CSIC ‐ University Miguel Hernandez, Alicante, Spain |
Anne Donaldson | Institute of Medical Sciences, University of Aberdeen, United Kingdom |
Peter Draber | BIOCEV, First Faculty of Medicine, Charles University, Vestec, Czech Republic |
Xiaoqi Feng | John Innes Centre, Norwich, United Kingdom |
Luisa Figueiredo | Institute of Molecular Medicine, Lisbon, Portugal |
Reto Gassmann | Institute for Molecular and Cell Biology, Porto, Portugal |
Kinga Kamieniarz‐Gdula | Adam Mickiewicz University in Poznań, Poland |
Roger Geiger | Institute for Research in Biomedicine, Bellinzona, Switzerland |
Niko Geldner | University of Lausanne, Switzerland |
Holger Gerhardt | Max Delbrück Center for Molecular Medicine, Berlin, Germany |
Daniel Wolfram Gerlich | Institute of Molecular Biotechnology (IMBA), Vienna, Austria |
Jesus Gil | MRC Clinical Sciences Centre, Imperial College London, United Kingdom |
Sebastian Glatt | Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland |
Edgar Gomes | Institute of Molecular Medicine, Lisbon, Portugal |
Pierre Gönczy | Swiss Institute for Experimental Cancer Research (ISREC), École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland |
Maria Gorna | University of Warsaw, Poland |
Mina Gouti | Max‐Delbrück‐Centrum, Berlin, Germany |
Jerome Gros | Institut Pasteur, Paris, France |
Anja Groth | Biotech Research and Innovation Centre (BRIC), University of Copenhagen, Denmark |
Annika Guse | Centre for Organismal Studies, Heidelberg, Germany |
Ricardo Henriques | Instituto Gulbenkian de Ciência, Oeiras, Portugal |
Eva Hoffmann | Center for Chromosome Stability, University of Copenhagen, Denmark |
Thorsten Hoppe | CECAD at the Institute for Genetics, University of Cologne, Germany |
Yen‐Ping Hsueh | Academia Sinica, Taipei, Taiwan |
Pablo Huertas | Andalusian Molecular Biology and Regenerative Medicine Centre (CABIMER), Seville, Spain |
Matteo Iannacone | IRCCS San Raffaele Scientific Institute, Milan, Italy |
Alvaro Rada‐Iglesias | Institue of Biomedicine and Biotechnology of Cantabria (IBBTEC) University of Cantabria, Santander, Spain |
Axel Innis | Institut Européen de Chimie et Biologie (IECB), Pessac, France |
Nicola Iovino | MPI für Immunbiologie und Epigenetik, Freiburg, Germany |
Carsten Janke | Institut Curie, France |
Ralf Jansen | Interfaculty Institute for Biochemistry, Eberhard‐Karls‐University Tübingen, Germany |
Sebastian Jessberger | HiFo / Brain Research Institute, University of Zurich, Switzerland |
Martin Jinek | University of Zurich, Switzerland |
Simon Bekker‐Jensen | University, Copenhagen, Denmark |
Nicole Joller | University of Zurich, Switzerland |
Luca Jovine | Department of Biosciences and Nutrition & Center for Biosciences, Karolinska Institutet, Stockholm, Sweden |
Jan Philipp Junker | Max‐Delbrück‐Centrum, Berlin, Germany |
Anna Karnkowska | University, Warsaw, Poland |
Zuzana Keckesova | Institute of Organic Chemistry and Biochemistry AS CR, Prague, Czech Republic |
René Ketting | Institute of Molecular Biology (IMB), Mainz, Germany |
Bruno Klaholz | Institute of Genetics and Molecular and Cellular Biology (IGBMC), University of Strasbourg, Illkirch, France |
Jürgen Knoblich | Institute of Molecular Biotechnology (IMBA), Vienna, Austria |
Taco Kooij | Centre for Molecular Life Sciences, Nijmegen, Netherlands |
Romain Koszul | Institut Pasteur, Paris, France |
Claudine Kraft | Institute for Biochemistry and Molecular Biology, Universität Freiburg, Germany |
Alena Krejci | Faculty of Science, University of South Bohemia, Ceske Budejovice, Czech Republic |
Lumir Krejci | National Centre for Biomolecular Research (NCBR), Masaryk University, Brno, Czech Republic |
Arnold Kristjuhan | Institute of Molecular and Cell Biology, University of Tartu, Estonia |
Yogesh Kulathu | MRC Protein Phosphorylation & Ubiquitylation Unit, University of Dundee, United Kingdom |
Edmund Kunji | MRC Mitochondrial Biology Unit, Cambridge, United Kingdom |
Karim Labib | MRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, United Kingdom |
Thomas Lecuit | Developmental Biology Institute of Marseilles ‐ Luminy (IBDML), France |
Gaëlle Legube | Center for Integrative Biology in Toulouse, Paul Sabatier University, France |
Suewei Lin | Academia Sinica, Taipei, Taiwan |
Ming‐Jung Liu | Academia Sinica, Taipei, Taiwan |
Malcolm Logan | Randall Division of Cell and Molecular Biophysics, King’s College London, United Kingdom |
Massimo Lopes | University of Zurich, Switzerland |
Jan Löwe | Structural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom |
Martijn Luijsterburg | University Medical Centre, Leiden, Netherlands |
Taija Makinen | Uppsala University, Sweden |
Sandrine Etienne‐Manneville | Institut Pasteur, Paris, France |
Miguel Manzanares | Spanish National Center for Cardiovascular Research (CNIC), Madrid, Spain |
Jean‐Christophe Marine | Center for Biology of Disease, Laboratory for Molecular Cancer Biology, VIB & KU Leuven, Belgium |
Sascha Martens | Max F. Perutz Laboratories, University of Vienna, Austria |
Elvira Mass | Universität Bonn, Germany |
Olivier Mathieu | Clermont Université, Aubière, France |
Ivan Matic | Max Planck Institute for Biology of Ageing, Cologne, Germany |
Joao Matos | Max Perutz Laboratories, Vienna, Austria |
Nicholas McGranahan | University College London, United Kingdom |
Hind Medyouf | Georg‐Speyer‐Haus, Frankfurt, Germany |
Patrick Meraldi | University of Geneva, Switzerland |
Marco Milán | ICREA & Institute for Research in Biomedicine (IRB), Barcelona, Spain |
Eric Miska | Wellcome Trust/Cancer Research UK Gurdon Institute, University of Cambridge, United Kingdom |
Nuria Montserrat | Institut de Bioenginyeria de Catalunya (IBEC), Barcelona, Spain |
Nuno Barbosa‐Morais | Institute of Molecular Medicine, Lisbon, Portugal |
Antonin Morillon | Institut Curie, Paris, France |
Rafal Mostowy | Jagiellonian University, Krakow, Poland |
Patrick Müller | University of Konstanz, Konstanz, Germany |
Miratul Muqit | University of Dundee, United Kigdom |
Poul Nissen | Centre for Structural Biology, Aarhus University, Denmark |
Ellen Nollen | European Research Institute for the Biology of Ageing, University of Groningen, Netherlands |
Marcin Nowotny | International Institute of Molecular and Cell Biology, Warsaw, Poland |
John O''Neill | MRC Laboratory of Molecular Biology, Cambridge, United Kigdom |
Tamer Önder | Koc University School of Medicine, Istanbul, Turkey |
Elin Org | University of Tartu, Estonia |
Nurhan Özlü | Koç University, Istanbul, Turkey |
Bjørn Panyella Pedersen | Aarhus University, Denmark |
Vladimir Pena | London, The Institute of Cancer Research, United Kingdom |
Camilo Perez | Biozentrum, University of Basel, Switzerland |
Antoine Peters | Friedrich Miescher Institute for Biomedical Research (FMI), Basel, Switzerland |
Clemens Plaschka | IMP, Vienna, Austria |
Pavel Plevka | CEITEC, Masaryk University, Brno, Czech Republic |
Hendrik Poeck | Technische Universität, München, , Germany |
Sophie Polo | Université Diderot (Paris 7), Paris, France |
Simona Polo | IFOM ‐ The FIRC Institute of Molecular Oncology, Milan, Italy |
Magdalini Polymenidou | University of Zurich, Switzerland |
Freddy Radtke | Swiss Institute for Experimental Cancer Research (ISREC), École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland |
Markus Ralser | Institute of Biochemistry Charité, Berlin, Germany & MRC National Institute for Medical Research, London, United Kingdom |
Jan Rehwinkel | John Radcliffe Hospital, Oxford, United Kingdom |
Maria Rescigno | European Institute of Oncology (IEO), Milan, Italy |
Katerina Rohlenova | Prague, Institute of Biotechnology, Czech Republic |
Guadalupe Sabio | Centro Nacional de Investigaciones Cardiovasculares (CNIC), Madrid, Spain |
Ana Jesus Garcia Saez | University of Cologne, CECAD Research Center, Germany |
Iris Salecker | Institut de Biologie de l''Ecole Normale Supérieure (IBENS), Paris, France |
Peter Sarkies | University of Oxford, United Kingdom |
Frédéric Saudou | Grenoble Institute of Neuroscience, France |
Timothy Saunders | Centre for Mechanochemical Cell Biology, Interdisciplinary Biomedical Research Building, Warwick Medical School, Coventry, United Kingdom |
Orlando D. Schärer | IBS Center for Genomic Integrity, Ulsan, South Korea |
Arp Schnittger | Biozentrum Klein Flottbek, University of Hamburg, Germnay |
Frank Schnorrer | Aix Marseille University, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France |
Maya Schuldiner | Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel |
Schraga Schwartz | Weizmann Institute of Science, Rehovot, Israel |
Martin Schwarzer | Institute of Microbiology, Academy of Sciences of the Czech Republic |
Claus Maria | Instituto de Medicina Molecular Faculdade de Medicina da Universidade de Lisboa, Portugal |
Hayley Sharpe | The Babraham Institute, United Kingdom |
Halyna Shcherbata | Institute of Cell Biochemistry, Hannover Medical School, Hannover, Germany |
Eric So | Department of Haematological Medicine, King''s College London, United Kingdom |
Victor Sourjik | Max Planck Institute for Terrestrial Microbiology, Marburg, Germany |
Anne Spang | Biozentrum, University of Basel, Switzerland |
Irina Stancheva | Institute of Cell Biology, University of Edinburgh, United Kingdom |
Bas van Steensel | Department of Gene Regulation, The Netherlands Cancer Institute, Amsterdam, Netherlands |
Richard Stefl | CEITEC, Masaryk University, Brno, Czech Republic |
Yonatan Stelzer | Weizmann Institute of Science, Rehovot, Israel |
Julian Stingele | Ludwig‐Maximilians‐Universität, München, Germany |
Katja Sträßer | Institute for Biochemistry, University of Giessen, Germany |
Kvido Strisovsky | Institute of Organic Chemistry and Biochemistry ASCR, Prague, Czech Republic |
Joanna Sulkowska | University, Warsaw, Poland |
Grzegorz Sumara | Nencki Institute of Experimental Biology, Warsaw, Poland |
Karolina Szczepanowska | International Institute Molecular Mechanisms & Machines PAS, Warsaw, Poland |
Luca Tamagnone | Institute for Cancer Research and Treatment, University of Torino Medical School, Italy |
Meng How Tan | Singapore, Nanyang Technological University, Singapore |
Nicolas Tapon | Cancer Research UK London Research Institute, United Kingdom |
Nicholas M. I. Taylor | University, Copenhagen, Denmark |
Sven Van Teeffelen | Université de Montréal, Canada |
Maria Teresa Teixeira | Laboratory of Molecular and Cellular Biology of Eukaryotes, IBPC, Paris, France |
Aurelio Teleman | German Cancer Research Center (DKFZ), Heidelberg, Germany |
Pascal Therond | Institute Valrose Biology, University of Nice‐Sophia Antipolis, France |
Pavel Tolar | University College London, United Kingdom |
Isheng Jason Tsai | Academia Sinica, Taipei, Taiwan |
Helle Ulrich | Institute of Molecular Biology (IMB), Mainz, Germany |
Stepanka Vanacova | Central European Institute of Technology, Masaryk University, Brno, Czech Republic |
Henrique Veiga‐Fernandes | Champalimaud Center for the Unknown, Lisboa, Portugal |
Marc Veldhoen | Instituto de Medicina Molecular, Lisbon, Portugal |
Louis Vermeulen | Academic Medical Centre, Amsterdam, Netherlands |
Uwe Vinkemeier | University of Nottingham Medical School, United Kingdom |
Helen Walden | MRC Protein Phosphorylation & Ubiquitylation Unit, University of Dundee, United Kingdom |
Michal Wandel | Institute of Biochemistry and Biophysics, PAS, Warsaw, Poland |
Julie Welburn | Wellcome Trust Centre, Edinburgh, United Kingdom |
Ervin Welker | Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, Szeged, Hungary |
Gerhard Wingender | Izmir Biomedicine and Genome Center, Dokuz Eylul University, Izmir, Turkey |
Thomas Wollert | Institute Pasteur, Membrane Biochemistry and Transport, Centre François Jacob, Paris, France |
Hyun Youk | University of Massachusetts Medical School, USA |
Christoph Zechner | MPI für molekulare Zellbiologie und Genetik, Dresden, Germany |
Philip Zegerman | Wellcome Trust / Cancer Research UK Gurdon Institute, University of Cambridge, United Kingdom |
Alena Ziková | Institute of Parasitology, Biology Centre AS CR, Ceske Budejovice, Czech Republic |
Piotr Ziolkowski | Adam Mickiewicz University, Poznan, Poland |
David Zwicker | MPI für Dynamik und Selbstorganisation, Göttingen, Germany |
7.
Genital coevolution between the sexes is expected to be common because of the direct interaction between male and female genitalia during copulation. Here we review the diverse mechanisms of genital coevolution that include natural selection, female mate choice, male–male competition, and how their interactions generate sexual conflict that can lead to sexually antagonistic coevolution. Natural selection on genital morphology will result in size coevolution to allow for copulation to be mechanically possible, even as other features of genitalia may reflect the action of other mechanisms of selection. Genital coevolution is explicitly predicted by at least three mechanisms of genital evolution: lock and key to prevent hybridization, female choice, and sexual conflict. Although some good examples exist in support of each of these mechanisms, more data on quantitative female genital variation and studies of functional morphology during copulation are needed to understand more general patterns. A combination of different approaches is required to continue to advance our understanding of genital coevolution. Knowledge of the ecology and behavior of the studied species combined with functional morphology, quantitative morphological tools, experimental manipulation, and experimental evolution have been provided in the best-studied species, all of which are invertebrates. Therefore, attention to vertebrates in any of these areas is badly needed.Of all the evolutionary interactions between the sexes, the mechanical interaction of genitalia during copulation in species with internal fertilization is perhaps the most direct. For this reason alone, coevolution between genital morphologies of males and females is expected. Morphological and genetic components of male and female genitalia have been shown to covary in many taxa (Sota and Kubota 1998; Ilango and Lane 2000; Arnqvist and Rowe 2002; Brennan et al. 2007; Rönn et al. 2007; Kuntner et al. 2009; Tatarnic and Cassis 2010; Cayetano et al. 2011; Evans et al. 2011, 2013; Simmons and García-González 2011; Yassin and Orgogozo 2013; and see examples in Taxa Male structures Female structures Evidence Likely mechanism References Mollusks Land snails (Xerocrassa) Spermatophore-producing organs Spermatophore-receiving organs Comparative among species SAC or female choice Sauder and Hausdorf 2009 Satsuma Penis length Vagina length Character displacement Lock and key Kameda et al. 2009 Arthropods Arachnids (Nephilid spiders) Multiple Multiple Comparative among species SAC Kuntner et al. 2009 Pholcidae spiders Cheliceral apophysis Epigynal pockets Comparative (no phylogenetic analysis) Female choice Huber 1999 Harvestmen (Opiliones) Hardened penes and loss of nuptial gifts Sclerotized pregenital barriers Comparative among species SAC Burns et al. 2013 Millipedes Parafontaria tonominea Gonopod size Genital segment size Comparative in species complex Mechanical incompatibility resulting from Intersexual selection Sota and Tanabe 2010 Antichiropus variabilis Gonopod shape and size Accesory lobe of the vulva and distal projection Functional copulatory morphology Lock and key Wojcieszek and Simmons 2012 Crustacean Fiddler crabs, Uca Gonopode Vulva, vagina, and spermatheca Two-species comparison, shape correspondence Natural selection against fluid loss, lock and key, and sexual selection Lautenschlager et al. 2010 Hexapodes Odonates Clasping appendages Abdominal shape and sensory hairs Functional morphology, comparative among species Lock and key via female sensory system Robertson and Paterson 1982; McPeek et al. 2009 Insects Coleoptera: seed beetles Spiny aedagus Thickened walls of copulatory duct Comparative among species SAC Rönn et al. 2007 Callosobruchus: Callosobruchus maculatus Damage inflicted Susceptibility to damage Full sib/half sib mating experiments SAC Gay et al. 2011 Reduced spines No correlated response Experimental evolution SAC Cayetano et al. 2011 Carabid beetles (Ohomopterus) Apophysis of the endophallus Vaginal appendix (pocket attached to the vaginal apophysis) Cross-species matings Lock and key Sota and Kubota 1998; Sasabi et al. 2010 Dung beetle: Onthophagus taurus Shape of the parameres in the aedagus Size and location of genital pits Experimental evolution Female choice Simmons and García-González 2011 Diptera: Drosophila santomea and D. yakuba Sclerotized spikes on the aedagus Cavities with sclerotized platelets Cross-species matings SAC Kamimura 2012 Drosophila melanogaster species complex Epandrial posterior lobes
Oviscapt pouches Comparative among species SAC or female choice Yassin and Orgogozo 2013 Phallic spikes Oviscapt furrows Cercal teeth, phallic hook, and spines Uterine, vulval, and vaginal shields D. mauritiana and D. sechelia Posterior lobe of the genital arch Wounding of the female abdomen Mating with introgressed lines SAC Masly and Kamimura 2014 Stalk-eyed flies (Diopsidae) Genital process Common spermathecal duct Comparative among species and morphological Female choice Kotrba et al. 2014 Tse-tse flies: Glossina pallidipes Cercal teeth Female-sensing structures Experimental copulatory function Female choice Briceño and Eberhard 2009a,b Phelebotomine: sand flies Aedagal filaments, aedagal sheaths Spermathecal ducts length, base of the duct Comparative among species None specified Ilango and Lane 2000 Heteroptera: Bed bugs (Cimiciidae) Piercing genitalia Spermalege (thickened exosqueleton) Comparative among species SAC Carayon 1966; Morrow and Arnqvist 2003 Plant bugs (Coridromius) Changes in male genital shape External female paragenitalia Comparative among species SAC Tatarnic and Cassis 2010 Waterstriders (Gerris sp.) Grasping appendages Antigrasping appendages Comparative among species SAC Arnqvist and Rowe 2002 Gerris incognitus Grasping appendages Antigrasping appendages Comparative among populations SAC Perry and Rowe 2012 Bee assassins (Apiomerus) Aedagus Bursa copulatrix Comparative among species None Forero et al. 2013 Cave insects (Psocodea), Neotrogla Male genital chamber Penis-like gynosome Comparative among species Female competition (role reversal), coevolution SAC Yoshizawa et al. 2014 Butterflies (Heliconiinae) Thickness of spermatophore wall Signa: Sclerotized structure to break spermatophores Comparative among species SAC Sánchez and Cordero 2014 Fish Basking shark: Cetorhinus maximus Clasper claw Thick vaginal pads Morphological observation None Matthews 1950 Gambusia Gonopodial tips Genital papillae within openings Comparative among species Strong character displacement Langerhans 2011 Poecilia reticulata Gonopodium tip shape Female gonopore shape Comparative among populations SAC Evans et al. 2011 Reptiles Anoles Hemipene shape Vagina shape Shape correspondence, two species Sexual selection Köhler et al. 2012 Several species Hemipene shape Vagina shape Shape correspondence Lock and key, female choice, and SAC Pope 1941; Böhme and Ziegler 2009; King et al. 2009 Asiatic pit vipers Spininess in hemipenes Thickness of vagina wall Two-species comparison None Pope 1941 Garter snake: Thamnophis sirtalis Basal hempene spine Vaginal muscular control Experimental manipulation SAC Friesen et al. 2014 Birds Waterfowl Penis length Vaginal elaboration Comparative among species SAC Brennan et al. 2007 Tinamous Penis length/presence Vaginal elaboration Comparative among species Female choice/natural selection PLR Brennan, K Zyscowski, and RO Prum, unpubl. Mammals Marsupials Bifid penis Two lateral vaginae Shape correspondence None Renfree 1987 Equidna Bifid penis with four rosettes Single vagina splits into two uteri Shape correspondence None Augee et al. 2006; Johnston et al. 2007 Insectivores: Short-tailed shrew: Blarina brevicauda S-shaped curve of the erect penis Coincident curve in the vagina Shape correspondence None Bedford et al. 2004 Common tenrec: Tenrec caudatus Filiform penis (up to 70% of the male’s body length) Internal circular folds in the vagina Length correspondence None Bedford et al. 2004 Rodents: Cape dune mole: Bathyergus suillus Penis and baculum length Vaginal length Allometric relationships within species None Kinahan et al. 2007 Australian hopping mice (Notomys) Spiny penis Derived distal region in the vagina Morphological observation and two-species comparison Copulatory lock Breed et al. 2013 Pig: Sus domesticus Filiform penis end Cervical ridges Artificial insemination Female choice Bonet et al. 2013 Primates: Macaca arctoides Long and filamentous glans Vestibular colliculus (fleshy fold) that partially obstructs the entrance to the vagina Shape correspondence and comparison with close relatives None Fooden 1967