The annexins of Dictyostelium |
| |
| Authors: | Marko Marija Prabhu Yogikala Müller Rolf Blau-Wasser Rosemarie Schleicher Michael Noegel Angelika A |
| |
| Affiliation: | 1. Institute for Biochemistry I, Medical Faculty, and Center for Molecular Medicine Cologne, University of Cologne, Joseph-Stelzmann-Str. 52, D-50931 Köln, Germany;2. Institute of Cell Biology, Ludwig-Maximilians-Universität, D-80336 München, Germany;1. Ludwig-Maximilians-Universitaet Muenchen, Institut fuer Zellbiologie (ABI), Schillerstr. 42, D-80336 Muenchen, Germany;2. University of Turin, Department of Clinical and Biological Sciences, I-10043 Orbassano, Italy;1. Department of Molecular Cardiology, Texas Heart Institute, Houston, TX 77030, USA;2. National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA;3. Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA;1. Departments of Pathology and Cell Biology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan;2. Department of Molecular and Cellular Pathology, Kagoshima University Graduate School of Medical and Dental Sciences, Kitakyushu, Japan;3. Bio-information Research Center, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan;4. Department of Urology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan;5. Department of Emergency Medicine, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan;7. Department of Occupational Pneumology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan;11. Department of Molecular Biology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan;6. Department of Cell Pathology, Faculty of Medical and Pharmaceutical Sciences, Graduate School of Medical Sciences, Kumamoto University, Kitakyushu, Japan;12. Laboratory of Cell Signaling, Graduate School of Pharmaceutical Sciences, The University of Tokyo, and Core Research for Evolutional Science and Technology, Tokyo, Japan;1. Department of Ophthalmology and Visual Sciences, University of Louisville, 301 E. Muhammad Ali Blvd., Louisville, KY 40202, USA;2. Department of Biochemistry and Molecular Genetics, University of Louisville, 319 Abraham Flexner Way, Louisville, KY 40202, USA;3. Department of Ophthalmology, Tokyo Medical University, 6-7-1 Nishi Shinjuku, Shinjuku, Tokyo 160-0023, Japan;1. Neuroscience and Mental Health Institute, University of Alberta, Edmonton, Alberta, Canada;2. Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canada;3. Division of Neurology, Department of Medicine, University of Alberta, Edmonton, Alberta, Canada;4. Department of Psychology, University of Alberta, Edmonton, Alberta, Canada;1. UCD School of Medicine and Medical Science, University College Dublin, Ireland;2. Ophthalmology, Mater Misericordiae University Hospital and Conway Institute, University College Dublin, Ireland;3. School of Medicine (Physiology), Trinity Biomedical Sciences Institute, Trinity College Dublin, Ireland;4. Dept. Cell Biology & Anatomy, North Texas Eye Research Institute, U. North Texas, Health Science Center, Ft. Worth, TX, USA |
| |
| Abstract: | Annexins are a highly conserved ubiquitous family of Ca2+- and phospholipid-binding proteins present in nearly all eukaryotic cells. Analysis of the Dictyostelium genome revealed the presence of two annexin genes, the annexin C1 gene (nxnA) giving rise to two isoforms of 47 and 51 kDa (previously synexin), and the annexin C2 gene (nxnB) coding for a 56-kDa protein with 33% sequence identity to annexin C1. Annexin C2 is expressed at very low and constant levels throughout development. Quantification by real-time PCR indicated that it is present in about 35-fold lower amounts compared to annexin C1. We have used a GFP-tagged annexin C2 to study its cellular distribution and dynamics. In cell fractionation studies, annexin C2 cofractionates with annexin C1 and is enriched in the 100,000 g pellet. Like annexin C1, GFP-AnxC2 stains the plasma membrane. In addition it is present in the perinuclear region and overlaps to some degree with the Golgi apparatus, whereas annexin C1 is present on intracellular membranes resembling endosomal membranes and in the nucleus. Annexin C2 is not observed in the nucleus. An annexin C1 mutant (SYN-) which shows a defect during multicellular development can be rescued by full-length annexin C1, whereas overexpression of GFP-AnxC2 did not rescue the developmental defect The data support the concept that annexins, although having a highly conserved structure, participate in different functions in a cell. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect PubMed 等数据库收录！ |
|
