Oligomerization but not membrane bending underlies the function of certain F-BAR proteins in cell motility and cytokinesis
| Autor: | Ohi, Nathan A. McDonald, Vander Kooi Cw, Kathleen L. Gould |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
genetic structures
Medial cortex Cell Cycle Proteins General Biochemistry Genetics and Molecular Biology Article Membrane bending Cell membrane Schizosaccharomyces medicine Humans Cytoskeleton Molecular Biology Cytokinesis biology Cell Membrane Cell Biology Actin cytoskeleton biology.organism_classification Cell biology Actin Cytoskeleton Cytoskeletal Proteins medicine.anatomical_structure Membrane Schizosaccharomyces pombe Proteins Protein Multimerization Carrier Proteins Developmental Biology |
| Popis: | SummaryF-BAR proteins function in diverse cellular processes by linking membranes to the actin cytoskeleton. Through oligomerization, multiple F-BAR domains can bend membranes into tubules, though the physiological importance of F-BAR-to-F-BAR assemblies is not yet known. Here, we investigate the F-BAR domain of the essential cytokinetic scaffold, Schizosaccharomyces pombe Cdc15, during cytokinesis. Challenging a widely held view that membrane deformation is a fundamental property of F-BARs, we report that the Cdc15 F-BAR binds, but does not deform, membranes in vivo or in vitro, and six human F-BAR domains—including those from Fer and RhoGAP4—share this property. Nevertheless, tip-to-tip interactions between F-BAR dimers are critical for Cdc15 oligomerization and high-avidity membrane binding, stabilization of contractile ring components at the medial cortex, and the fidelity of cytokinesis. F-BAR oligomerization is also critical for Fer and RhoGAP4 physiological function, demonstrating its broad importance to F-BAR proteins that function without membrane bending. |
| Databáze: | OpenAIRE |
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