Phosphoinositide-mediated ring anchoring resists perpendicular forces to promote medial cytokinesis
| Autor: | Kathleen L. Gould, Alaina H. Willet, Chloe E. Snider, Marija Zanic, Goker Arpag, Jun-Song Chen |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Cell division Glycosylphosphatidylinositols Myosin Type V Cell Cycle Proteins macromolecular substances 03 medical and health sciences GTP-Binding Proteins Report Schizosaccharomyces Myosin 1-Phosphatidylinositol 4-Kinase Research Articles Paxillin Actin Cytokinesis Anaphase biology Cell Biology biology.organism_classification Cell biology 030104 developmental biology Schizosaccharomyces pombe biology.protein Schizosaccharomyces pombe Proteins |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | Altering phosphoinositide composition through deletion of efr3, a PI4 kinase scaffold, results in type V myosin-dependent cytokinetic ring sliding in Schizosaccharomyces pombe. Membrane-binding proteins contribute to ring anchoring to resist perpendicular forces and thereby promote medial cytokinesis. Many eukaryotic cells divide by assembling and constricting an actin- and myosin-based contractile ring (CR) that is physically linked to the plasma membrane (PM). In this study, we report that Schizosaccharomyces pombe cells lacking efr3, which encodes a conserved PM scaffold for the phosphatidylinositol-4 kinase Stt4, build CRs that can slide away from the cell middle during anaphase in a myosin V–dependent manner. The Efr3-dependent CR-anchoring mechanism is distinct from previously reported pathways dependent on the Fes/CIP4 homology Bin-Amphiphysin-Rvs167 (F-BAR) protein Cdc15 and paxillin Pxl1. In efr3Δ, the concentrations of several membrane-binding proteins were reduced in the CR and/or on the PM. Our results suggest that proper PM lipid composition is important to stabilize the central position of the CR and resist myosin V–based forces to promote the fidelity of cell division. |
| Databáze: | OpenAIRE |
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