Oligomerization but Not Membrane Bending Underlies the Function of Certain F-BAR Proteins in Cell Motility and Cytokinesis.

McDonald NA, Vander Kooi CW, Ohi MD, Gould KL
Dev Cell. 2015 35 (6): 725-36

PMID: 26702831 · PMCID: PMC4691284 · DOI:10.1016/j.devcel.2015.11.023

F-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.

Copyright © 2015 Elsevier Inc. All rights reserved.

MeSH Terms (10)

Actin Cytoskeleton Carrier Proteins Cell Cycle Proteins Cell Membrane Cytokinesis Cytoskeletal Proteins Humans Protein Multimerization Schizosaccharomyces Schizosaccharomyces pombe Proteins

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