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1.
During Drosophila embryogenesis, timely and orderly asymmetric cell divisions ensure the correct number of each cell type that make up the sensory organs of the larval PNS. We report a role of scraps, Drosophila Anillin, during these divisions. Anillin, a constitutive member of the contractile ring is essential for cytokinesis in Drosophila and vertebrates. During embryogenesis we find that zygotically transcribed scraps is required specifically for the unequal cell divisions, those in which cytokinesis occurs in an “off-centred” manner, of the pIIb and pIIIb neuronal precursor cells, but not the equal cell divisions of the lineage related precursor cells. Complementation and genetic rescue studies demonstrate this effect results from zygotic scraps and leads to polyploidy, ectopic mitosis, and loss of the neuronal precursor daughter cells. The net result of which is the formation of incomplete sense organs and embryonic lethality. 相似文献
2.
Karine G. Bourdages Benjamin Lacroix Jonas F. Dorn Carlos P. Descovich Amy S. Maddox 《PloS one》2014,9(10)
The physical separation of a cell into two daughter cells during cytokinesis requires cell-intrinsic shape changes driven by a contractile ring. However, in vivo, cells interact with their environment, which includes other cells. How cytokinesis occurs in tissues is not well understood. Here, we studied cytokinesis in an intact animal during tissue biogenesis. We used high-resolution microscopy and quantitative analysis to study the three rounds of division of the C. elegans vulval precursor cells (VPCs). The VPCs are cut in half longitudinally with each division. Contractile ring breadth, but not the speed of ring closure, scales with cell length. Furrowing speed instead scales with division plane dimensions, and scaling is consistent between the VPCs and C. elegans blastomeres. We compared our VPC cytokinesis kinetics data with measurements from the C. elegans zygote and HeLa and Drosophila S2 cells. Both the speed dynamics and asymmetry of ring closure are qualitatively conserved among cell types. Unlike in the C. elegans zygote but similar to other epithelial cells, Anillin is required for proper ring closure speed but not asymmetry in the VPCs. We present evidence that tissue organization impacts the dynamics of cytokinesis by comparing our results on the VPCs with the cells of the somatic gonad. In sum, this work establishes somatic lineages in post-embryonic C. elegans development as cell biological models for the study of cytokinesis in situ. 相似文献
3.
David Reboutier Marie-Bérengère Troadec Jean-Yves Cremet Lucie Chauvin Vincent Guen Patrick Salaun Claude Prigent 《The Journal of cell biology》2013,201(3):487-504
During cytokinesis, closure of the actomyosin contractile ring (CR) is coupled to the formation of a midbody ring (MR), through poorly understood mechanisms. Using time-lapse microscopy of Drosophila melanogaster S2 cells, we show that the transition from the CR to the MR proceeds via a previously uncharacterized maturation process that requires opposing mechanisms of removal and retention of the scaffold protein Anillin. The septin cytoskeleton acts on the C terminus of Anillin to locally trim away excess membrane from the late CR/nascent MR via internalization, extrusion, and shedding, whereas the citron kinase Sticky acts on the N terminus of Anillin to retain it at the mature MR. Simultaneous depletion of septins and Sticky not only disrupted MR formation but also caused earlier CR oscillations, uncovering redundant mechanisms of CR stability that can partly explain the essential role of Anillin in this process. Our findings highlight the relatedness of the CR and MR and suggest that membrane removal is coordinated with CR disassembly. 相似文献
4.
Cell cycle‐regulated PLEIADE/AtMAP65‐3 links membrane and microtubule dynamics during plant cytokinesis
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Alexander Steiner Katarzyna Rybak Melina Altmann Heather E. McFarlane Susan Klaeger Ngoc Nguyen Eva Facher Alexander Ivakov Gerhard Wanner Bernhard Kuster Staffan Persson Pascal Braun Marie‐Theres Hauser Farhah F. Assaad 《The Plant journal : for cell and molecular biology》2016,88(4):531-541
Cytokinesis, the partitioning of the cytoplasm following nuclear division, requires extensive coordination between cell cycle cues, membrane trafficking and microtubule dynamics. Plant cytokinesis occurs within a transient membrane compartment known as the cell plate, to which vesicles are delivered by a plant‐specific microtubule array, the phragmoplast. While membrane proteins required for cytokinesis are known, how these are coordinated with microtubule dynamics and regulated by cell cycle cues remains unclear. Here, we document physical and genetic interactions between Transport Protein Particle II (TRAPPII) tethering factors and microtubule‐associated proteins of the PLEIADE/AtMAP65 family. These interactions do not specifically affect the recruitment of either TRAPPII or MAP65 proteins to the cell plate or midzone. Rather, and based on single versus double mutant phenotypes, it appears that they are required to coordinate cytokinesis with the nuclear division cycle. As MAP65 family members are known to be targets of cell cycle‐regulated kinases, our results provide a conceptual framework for how membrane and microtubule dynamics may be coordinated with each other and with the nuclear cycle during plant cytokinesis. 相似文献
5.
6.
Mutations in sticky lead to defective organization of the contractile ring during cytokinesis and are enhanced by Rho and suppressed by Rac 总被引:1,自引:0,他引:1
The contractile ring is a highly dynamic structure, but how this dynamism is accomplished remains unclear. Here, we report the identification and analysis of a novel Drosophila gene, sticky (sti), essential for cytokinesis in all fly proliferating tissues. sti encodes the Drosophila orthologue of the mammalian Citron kinase. RNA interference-mediated silencing of sti in cultured cells causes them to become multinucleate. Components of the contractile ring and central spindle are recruited normally in such STICKY-depleted cells that nevertheless display asymmetric furrowing and aberrant blebbing. Together with an unusual distribution of F-actin and Anillin, these phenotypes are consistent with defective organization of the contractile ring. sti shows opposite genetic interactions with Rho and Rac genes suggesting that these GTPases antagonistically regulate STICKY functions. Similar genetic evidence indicates that RacGAP50C inhibits Rac during cytokinesis. We discuss that antagonism between Rho and Rac pathways may control contractile ring dynamics during cytokinesis. 相似文献
7.
Tetsuya Takeda Iain M. Robinson Matthew M. Savoian John R. Griffiths Anthony D. Whetton Harvey T. McMahon David M. Glover 《Open biology》2013,3(8)
Cytokinesis is a highly ordered cellular process driven by interactions between central spindle microtubules and the actomyosin contractile ring linked to the dynamic remodelling of the plasma membrane. The mechanisms responsible for reorganizing the plasma membrane at the cell equator and its coupling to the contractile ring in cytokinesis are poorly understood. We report here that Syndapin, a protein containing an F-BAR domain required for membrane curvature, contributes to the remodelling of the plasma membrane around the contractile ring for cytokinesis. Syndapin colocalizes with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) at the cleavage furrow, where it directly interacts with a contractile ring component, Anillin. Accordingly, Anillin is mislocalized during cytokinesis in Syndapin mutants. Elevated or diminished expression of Syndapin leads to cytokinesis defects with abnormal cortical dynamics. The minimal segment of Syndapin, which is able to localize to the cleavage furrow and induce cytokinesis defects, is the F-BAR domain and its immediate C-terminal sequences. Phosphorylation of this region prevents this functional interaction, resulting in reduced ability of Syndapin to bind to and deform membranes. Thus, the dephosphorylated form of Syndapin mediates both remodelling of the plasma membrane and its proper coupling to the cytokinetic machinery. 相似文献
8.
Cell division requires a direct link between microtubule-bound RacGAP and Anillin in the contractile ring 总被引:3,自引:0,他引:3
Gregory SL Ebrahimi S Milverton J Jones WM Bejsovec A Saint R 《Current biology : CB》2008,18(1):25-29
The mitotic microtubule array plays two primary roles in cell division. It acts as a scaffold for the congression and separation of chromosomes, and it specifies and maintains the contractile-ring position. The current model for initiation of Drosophila and mammalian cytokinesis [1-5] postulates that equatorial localization of a RhoGEF (Pbl/Ect2) by a microtubule-associated motor protein complex creates a band of activated RhoA [6], which subsequently recruits contractile-ring components such as actin, myosin, and Anillin [1-3]. Equatorial microtubules are essential for continued constriction, but how they interact with the contractile apparatus is unknown. Here, we report the first direct molecular link between the microtubule spindle and the actomyosin contractile ring. We find that the spindle-associated component, RacGAP50C, which specifies the site of cleavage [1-5], interacts directly with Anillin, an actin and myosin binding protein found in the contractile ring [7-10]. Both proteins depend on this interaction for their localization. In the absence of Anillin, the spindle-associated RacGAP loses its association with the equatorial cortex, and cytokinesis fails. These results account for the long-observed dependence of cytokinesis on the continual presence of microtubules at the cortex. 相似文献
9.
Animal cell cytokinesis proceeds via constriction of an actomyosin-based contractile ring (CR) [1, 2]. Upon reaching a diameter of ~1 μm [3], a midbody ring (MR) forms to stabilize the intercellular bridge until abscission [4-6]. How MR formation is coupled to CR closure and how plasma membrane anchoring is maintained at this key transition is unknown. Time-lapse microscopy of Drosophila S2 cells depleted of the scaffold protein Anillin [7-9] revealed that Anillin is required for complete closure of the CR and formation of the MR. Truncation analysis revealed that Anillin N termini connected with the actomyosin CR and supported formation of stable MR-like structures, but these could not maintain anchoring of the plasma membrane. Conversely, Anillin C termini failed to connect with the CR or MR but recruited the septin Peanut to ectopic structures at the equatorial cortex. Peanut depletion mimicked truncation of the Anillin C terminus, resulting in MR-like structures that failed to anchor the membrane. These data demonstrate that Anillin coordinates the transition from CR to MR and that it does so by linking two distinct cortical cytoskeletal elements. One apparently acts as the core structural template for MR assembly, while the other ensures stable anchoring of the plasma membrane beyond the CR stage. 相似文献
10.
《Gene expression patterns : GEP》2015,18(2):98-106
Anillin is a conserved cytokinetic ring protein implicated in actomyosin cytoskeletal organization and cytoskeletal-membrane linkage. Here we explored anillin localization in the highly asymmetric divisions of the mouse oocyte that lead to the extrusion of two polar bodies. The purposes of polar body extrusion are to reduce the chromosome complement within the egg to haploid, and to retain the majority of the egg cytoplasm for embryonic development. Anillin's proposed roles in cytokinetic ring organization suggest that it plays important roles in achieving this asymmetric division. We report that during meiotic maturation, anillin mRNA is expressed and protein levels steadily rise. In meiosis I, anillin localizes to a cortical cap overlying metaphase I spindles, and a broad ring over anaphase spindles that are perpendicular to the cortex. Anillin is excluded from the cortex of the prospective first polar body, and highly enriched in the cytokinetic ring that severs the polar body from the oocyte. In meiosis II, anillin is enriched in a cortical stripe precisely coincident with and overlying the meiotic spindle midzone. These results suggest a model in which this cortical structure contributes to spindle re-alignment in meiosis II. Thus, localization of anillin as a conserved cytokinetic ring marker illustrates that the geometry of the cytokinetic ring is distinct between the two oogenic meiotic cytokineses in mammals. 相似文献
11.
Lava lamp, a novel peripheral golgi protein, is required for Drosophila melanogaster cellularization
Drosophila cellularization and animal cell cytokinesis rely on the coordinated functions of the microfilament and microtubule cytoskeletal systems. To identify new proteins involved in cellularization and cytokinesis, we have conducted a biochemical screen for microfilament/microtubule-associated proteins (MMAPs). 17 MMAPs were identified; seven have been previously implicated in cellularization and/or cytokinesis, including KLP3A, Anillin, Septins, and Dynamin. We now show that a novel MMAP, Lava Lamp (Lva), is also required for cellularization. Lva is a coiled-coil protein and, unlike other proteins previously implicated in cellularization or cytokinesis, it is Golgi associated. Our functional analysis shows that cellularization is dramatically inhibited upon injecting anti-Lva antibodies (IgG and Fab) into embryos. In addition, we show that brefeldin A, a potent inhibitor of membrane trafficking, also inhibits cellularization. Biochemical analysis demonstrates that Lva physically interacts with the MMAPs Spectrin and CLIP190. We suggest that Lva and Spectrin may form a Golgi-based scaffold that mediates the interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization. Our results are consistent with the idea that animal cell cytokinesis depends on both actomyosin-based contraction and Golgi-derived membrane secretion. 相似文献
12.
Field CM Coughlin M Doberstein S Marty T Sullivan W 《Development (Cambridge, England)》2005,132(12):2849-2860
Anillin is a conserved component of the contractile ring that is essential for cytokinesis, and physically interacts with three conserved cleavage furrow proteins, F-actin, myosin II and septins in biochemical assays. We demonstrate that the Drosophila scraps gene, identified as a gene involved in cellularization, encodes Anillin. We characterize defects in cellularization, pole cell formation and cytokinesis in a series of maternal effect and zygotic anillin alleles. Mutations that result in amino acid changes in the C-terminal PH domain of Anillin cause defects in septin recruitment to the furrow canal and contractile ring. These mutations also strongly perturb cellularization, altering the timing and rate of furrow ingression. They cause dramatic vesiculation of new plasma membranes, and destabilize the stalk of cytoplasm that normally connects gastrulating cells to the yolk mass. A mutation closer to the N terminus blocks separation of pole cells with less effect on cellularization, highlighting mechanistic differences between contractile processes. Cumulatively, our data point to an important role for Anillin in scaffolding cleavage furrow components, directly stabilizing intracellular bridges, and indirectly stabilizing newly deposited plasma membrane during cellularization. 相似文献
13.
During cytokinesis, constriction of a cortical contractile ring generates a furrow that partitions one cell into two. The contractile ring contains three filament systems: actin, bipolar myosin II filaments, and septins, GTP-binding hetero-oligomers that polymerize to form a membrane-associated lattice. The contractile ring also contains a potential filament crosslinker, Anillin, that binds all three filament types. Here, we show that the contractile ring possesses an intrinsic symmetry-breaking mechanism that promotes asymmetric furrowing. Asymmetric ingression requires Anillin and the septins, which promote the coalescence of components on one side of the contractile ring, but is insensitive to a 10-fold reduction in myosin II levels. When asymmetry is disrupted, cytokinesis becomes sensitive to partial inhibition of contractility. Thus, asymmetric furrow ingression, a prevalent but previously unexplored feature of cell division in metazoans, is generated by the action of two conserved furrow components and serves a mechanical function that makes cytokinesis robust. 相似文献
14.
The rod-shaped fission yeast Schizosaccharomyces pombe, which undergoes cycles of monopolar-to-bipolar tip growth, is an attractive organism for studying cell-cycle regulation of polarity establishment. While previous research has described factors mediating this process from interphase cell tips, we found that division site signaling also impacts the re-establishment of bipolar cell growth in the ensuing cell cycle. Complete loss or targeted disruption of the non-essential cytokinesis protein Fic1 at the division site, but not at interphase cell tips, resulted in many cells failing to grow at new ends created by cell division. This appeared due to faulty disassembly and abnormal persistence of the cell division machinery at new ends of fic1Δ cells. Moreover, additional mutants defective in the final stages of cytokinesis exhibited analogous growth polarity defects, supporting that robust completion of cell division contributes to new end-growth competency. To test this model, we genetically manipulated S. pombe cells to undergo new end take-off immediately after cell division. Intriguingly, such cells elongated constitutively at new ends unless cytokinesis was perturbed. Thus, cell division imposes constraints that partially override positive controls on growth. We posit that such constraints facilitate invasive fungal growth, as cytokinesis mutants displaying bipolar growth defects formed numerous pseudohyphae. Collectively, these data highlight a role for previous cell cycles in defining a cell''s capacity to polarize at specific sites, and they additionally provide insight into how a unicellular yeast can transition into a quasi-multicellular state. 相似文献
15.
Similar to higher animal cells, ameba cells of the cellular slime mold Dictyostelium discoideum form contractile rings containing filaments of myosin II during mitosis, and it is generally believed that contraction of these rings bisects the cells both on substrates and in suspension. In suspension, mutant cells lacking the single myosin II heavy chain gene cannot carry out cytokinesis, become large and multinucleate, and eventually lyze, supporting the idea that myosin II plays critical roles in cytokinesis. These mutant cells are however viable on substrates. Detailed analyses of these mutant cells on substrates revealed that, in addition to "classic" cytokinesis which depends on myosin II ("cytokinesis A"), Dictyostelium has two distinct, novel methods of cytokinesis, 1) attachment-assisted mitotic cleavage employed by myosin II null cells on substrates ("cytokinesis B"), and 2) cytofission, a cell cycle-independent division of adherent cells ("cytokinesis C"). Cytokinesis A, B, and C lose their function and demand fewer protein factors in this order. Cytokinesis B is of particular importance for future studies. Similar to cytokinesis A, cytokinesis B involves formation of a cleavage furrow in the equatorial region, and it may be a primitive but basic mechanism of efficiently bisecting a cell in a cell cycle-coupled manner. Analysis of large, multinucleate myosin II null cells suggested that interactions between astral microtubules and cortices positively induce polar protrusive activities in telophase. A model is proposed to explain how such polar activities drive cytokinesis B, and how cytokinesis B is coordinated with cytokinesis A in wild type cells. 相似文献
16.
Tara C. Smith Peter C. Fridy Yinyin Li Shruti Basil Sneha Arjun Ryan M. Friesen John Leszyk Brian T. Chait Michael P. Rout Elizabeth J. Luna 《Molecular biology of the cell》2013,24(23):3603-3619
Cytokinesis, the process by which cytoplasm is apportioned between dividing daughter cells, requires coordination of myosin II function, membrane trafficking, and central spindle organization. Most known regulators act during late cytokinesis; a few, including the myosin II–binding proteins anillin and supervillin, act earlier. Anillin''s role in scaffolding the membrane cortex with the central spindle is well established, but the mechanism of supervillin action is relatively uncharacterized. We show here that two regions within supervillin affect cell division: residues 831–1281, which bind central spindle proteins, and residues 1–170, which bind the myosin II heavy chain (MHC) and the long form of myosin light-chain kinase. MHC binding is required to rescue supervillin deficiency, and mutagenesis of this site creates a dominant-negative phenotype. Supervillin concentrates activated and total myosin II at the furrow, and simultaneous knockdown of supervillin and anillin additively increases cell division failure. Knockdown of either protein causes mislocalization of the other, and endogenous anillin increases upon supervillin knockdown. Proteomic identification of interaction partners recovered using a high-affinity green fluorescent protein nanobody suggests that supervillin and anillin regulate the myosin II and actin cortical cytoskeletons through separate pathways. We conclude that supervillin and anillin play complementary roles during vertebrate cytokinesis. 相似文献
17.
Cell division after mitosis is mediated by ingression of an actomyosin-based contractile ring. The active, GTP-bound form of the small GTPase RhoA is a key regulator of contractile-ring formation. RhoA concentrates at the equatorial cell cortex at the site of the nascent cleavage furrow. During cytokinesis, RhoA is activated by its RhoGEF, ECT2. Once activated, RhoA promotes nucleation, elongation, and sliding of actin filaments through the coordinated activation of both formin proteins and myosin II motors (reviewed in [1, 2]). Anillin is a 124 kDa protein that is highly concentrated in the cleavage furrow in numerous animal cells in a pattern that resembles that of RhoA [3-7]. Although anillin contains conserved N-terminal actin and myosin binding domains and a PH domain at the C terminus, its mechanism of action during cytokinesis remains unclear. Here, we show that human anillin contains a conserved C-terminal domain that is essential for its function and localization. This domain shares homology with the RhoA binding protein Rhotekin and directly interacts with RhoA. Further, anillin is required to maintain active myosin in the equatorial plane during cytokinesis, suggesting it functions as a scaffold protein to link RhoA with the ring components actin and myosin. Although furrows can form and initiate ingression in the absence of anillin, furrows cannot form in anillin-depleted cells in which the central spindle is also disrupted, revealing that anillin can also act at an early stage of cytokinesis. 相似文献
18.
Mitch Leslie 《The Journal of cell biology》2009,186(5):633
How cells set the where and when of cytokinesisCompared with the complex choreography required to sort chromosomes during mitosis, cytokinesis might seem fairly simple. But ensuring that the contractile ring of actin and myosin pinches off daughter cells also takes some fancy footwork. Two independent groups (1, 2) offer fresh details about how cells cue cytokinesis at the right time and place.Open in a separate windowFOCAL POINT Top: Asymmetry might set the cytokinesis clock, Dannel McCollum (left) and Juan Carlos García-Cortés (right) determined. The cytokinesis-triggering septum initiation network (indicated by a bright dot on the spindle pole body) turns on only in one side of these yeast cells. Bottom: Eric Griffis (left) and Ron Vale (right), together with James Spudich, reveal that microtubules and the motor protein Kinesin-6 help dictate where cytokinesis occurs. Here, Kinesin-6 (green) has migrated to the equator of a mitotic cell.Cytokinesis can''t begin until the chromosomes have separated, and to forestall multiple divisions it has to end when the daughter cell is independent. García-Cortés and McCollum (1) show that mitotic cells stay on this schedule thanks to a team of proteins that sparks cytokinesis but also initiates its own shutdown.In the fission yeast Schizosaccharomyces pombe, the septum initiation network, or SIN, instigates cytokinesis. The mystery was how cells commit SIN at the right time. The SIN activator Spg1 rides on the spindle pole bodies that anchor the mitotic spindle. Previous work (3) showed that the protein Etd1, which turns on Spg1, amasses at the ends of the cell. García-Cortés and McCollum wondered whether the lengthening of the spindle as chromosomes pull apart might bring Spg1 and Etd1 together, thereby activating SIN. To test that idea, the researchers followed Spg1 activation in cells dosed with a drug that halts spindle elongation. In cells where drug exposure came after the spindle had stretched out, Spg1 turned on as normal. But if the cells entered mitosis after addition of the drug—and thus could not lengthen their spindles—Spg1 remained inactive. The researchers also found that tethering Spg1 to Etd1 prompted cells to divide again and again, further evidence that the rendezvous between the two proteins spurs cytokinesis when chromosome separation is complete.
“It provides a mechanism for how cells can know when they''ve finished cytokinesis.”A complication to the story—Spg1 and SIN only flip on in half of the cell—might explain how cells determine when to curtail cytokinesis. After the contractile ring has tightened, SIN triggers the elimination of Etd1 in the cell half where Spg1 was turned on. In turn, that leads to the shutdown of Spg1 and then SIN. According to the researchers, asymmetry of SIN signaling might serve as an indicator that the cytoplasm has been divided. “It provides a mechanism for how cells can know when they''ve finished cytokinesis,” says senior author Dannel McCollum. What researchers don''t understand is how the cell chooses which end will activate Spg1 and SIN.Even if a cell''s timing is impeccable, cytokinesis will go awry if the contractile ring assembles at the wrong location. The findings from Vale, Spudich, and Griffis (2) suggest that the molecular motor Kinesin-6 helps designate where the cell will split.Previous studies have shown that the GTPase RhoA (4) is the master regulator of cytokinesis and switches on in the cleavage furrow. Why it activates there isn''t clear. Other studies indicate that certain microtubules dictate the site of the contractile ring (5). Kinesin-6, which hauls RhoA effectors, might connect these two mechanisms.The team used total internal reflection fluorescence microscopy to follow Kinesin-6 and myosin in Drosophila cells that were just entering anaphase. They observed that myosin filaments disappeared from the poles of the fly cells and appeared again at the equator—both changes require Kinesin-6. Contrary to some other studies, the researchers didn''t observe the molecules traveling en masse from one location to the other. Instead, the researchers think that myosin filaments at the poles dissolve and then reform at the equator.Kinesin-6 itself has to concentrate at the cleavage furrow. The researchers found that the molecules first hop on the tips of growing microtubules. Microtubules that reach the cell center stabilize and form bundles. Eventually, all of a cell''s Kinesin-6 accumulates on microtubule tips or in a broad swath around the cell''s midsection. The work suggests that Kinesin-6 helps demarcate the cleavage furrow by delivering RhoA activators that spur the formation of myosin filaments at the cell equator. “Our data suggest that the process of building the contractile ring is largely due to the concentration of positive factors, rather than a directed delivery of negative factors,” says co-author Eric Griffis. What triggers myosin disassembly at the poles and reassembly at the cleavage furrow remains unclear. 相似文献
19.
Kimberly Bellingham-Johnstun Erica Casey Anders John Ravi Christina Bruinsma Caroline Laplante 《The Journal of cell biology》2021,220(3)
The molecular organization of cytokinesis proteins governs contractile ring function. We used single molecule localization microscopy in live cells to elucidate the molecular organization of cytokinesis proteins and relate it to the constriction rate of the contractile ring. Wild-type fission yeast cells assemble contractile rings by the coalescence of cortical proteins complexes called nodes whereas cells without Anillin/Mid1p (Δmid1) lack visible nodes yet assemble contractile rings competent for constriction from the looping of strands. We leveraged the Δmid1 contractile ring assembly mechanism to determine how two distinct molecular organizations, nodes versus strands, can yield functional contractile rings. Contrary to previous interpretations, nodes assemble in Δmid1 cells. Our results suggest that Myo2p heads condense upon interaction with actin filaments and an excess number of Myo2p heads bound to actin filaments hinders constriction thus reducing the constriction rate. Our work establishes a predictive correlation between the molecular organization of nodes and the behavior of the contractile ring. 相似文献
20.
The ultimate goal of all signaling pathways in cytokinesis is to control the mechanical separation of the mother cell into two daughter cells. Because of the intrinsic mechanical nature of cytokinesis, it is essential to understand fully how cell shapes and the material properties of the cell are generated, how these shapes and material properties create force, and how motor proteins such as myosin-II modify the system to achieve successful cytokinesis. In this review (which is part of the Cytokinesis series), we discuss the relevant physical properties of cells, how these properties are measured and the basic models that are used to understand cell mechanics. Finally, we present our current understanding of how cytokinesis mechanics work. 相似文献