Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membrane Platform That Coordinates Cytoskeletal and Signaling Components for Cytokinesis
| Autor: | Melanie D. Ohi, Scott E. Collier, Lauren P. Jackson, Alaina H. Willet, Nathan A. McDonald, Chloe E. Snider, Kathleen L. Gould, Mintu Chandra |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Cell Cycle Proteins macromolecular substances General Biochemistry Genetics and Molecular Biology SH3 domain 03 medical and health sciences 0302 clinical medicine GTP-Binding Proteins Schizosaccharomyces Myosin Humans BAR domain Cytoskeleton Actin Cytokinesis biology Chemistry biology.organism_classification 030104 developmental biology Formins Schizosaccharomyces pombe biology.protein Biophysics Schizosaccharomyces pombe Proteins 030217 neurology & neurosurgery |
| Zdroj: | Cell Reports. 33:108526 |
| ISSN: | 2211-1247 |
| DOI: | 10.1016/j.celrep.2020.108526 |
| Popis: | Many eukaryotes assemble an actin- and myosin-based cytokinetic ring (CR) on the plasma membrane (PM) for cell division, but how it is anchored there remains unclear. In Schizosaccharomyces pombe, the F-BAR protein Cdc15 links the PM via its F-BAR domain to proteins in the CR's interior via its SH3 domain. However, Cdc15's F-BAR domain also directly binds formin Cdc12, suggesting that Cdc15 may polymerize a protein network directly adjacent to the membrane. Here, we determine that the F-BAR domain binds Cdc12 using residues on the face opposite its membrane-binding surface. These residues also bind paxillin-like Pxl1, promoting its recruitment with calcineurin to the CR. Mutation of these F-BAR domain residues results in a shallower CR, with components localizing ∼35% closer to the PM than in wild type, and aberrant CR constriction. Thus, F-BAR domains serve as oligomeric membrane-bound platforms that can modulate the architecture of an entire actin structure. |
| Databáze: | OpenAIRE |
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