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.
|Number of pages||12|
|State||Published - Dec 21 2015|
Bibliographical noteFunding Information:
The authors thank Anna Feoktistova for outstanding technical assistance with biochemical experiments and Dr. Rachel Roberts-Galbraith and members of the Gould laboratory for critical review of the manuscript. FRAP experiments were performed through the VUMC Cell Imaging Shared Resource. BLI experiments were performed through the VUMC Antibody and Protein Resource. EM and AU facilities receive support from the Vanderbilt Center for Structural Biology. N.A.M. was supported by AHA fellowship 15PRE21780003. This work was supported by NIH grant GM101035 to K.L.G.
© 2015 Elsevier Inc.
ASJC Scopus subject areas
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology (all)
- Developmental Biology
- Cell Biology