The F-BAR Domain of Rga7 Relies on a Cooperative Mechanism of Membrane Binding with a Partner Protein during Fission Yeast Cytokinesis.

Liu Y, McDonald NA, Naegele SM, Gould KL, Wu JQ
Cell Rep. 2019 26 (10): 2540-2548.e4

PMID: 30840879 · PMCID: PMC6425953 · DOI:10.1016/j.celrep.2019.01.112

F-BAR proteins bind the plasma membrane (PM) to scaffold and organize the actin cytoskeleton. To understand how F-BAR proteins achieve their PM association, we studied the localization of a Schizosaccharomyces pombe F-BAR protein Rga7, which requires the coiled-coil protein Rng10 for targeting to the division site during cytokinesis. We find that the Rga7 F-BAR domain directly binds a motif in Rng10 simultaneously with the PM, and that an adjacent Rng10 motif independently binds the PM. Together, these multivalent interactions significantly enhance Rga7 F-BAR avidity for membranes at physiological protein concentrations, ensuring the division site localization of Rga7. Moreover, the requirement for the F-BAR domain in Rga7 localization and function in cytokinesis is bypassed by tethering an Rga7 construct lacking its F-BAR to Rng10, indicating that at least some F-BAR domains are necessary but not sufficient for PM targeting and are stably localized to specific cortical positions through adaptor proteins.

Copyright © 2019 The Author(s). Published by Elsevier Inc. All rights reserved.

MeSH Terms (12)

Animals Cell Cycle Proteins Cell Membrane Chlorocebus aethiops COS Cells Cytokinesis GTPase-Activating Proteins Microscopy, Confocal Protein Domains Schizosaccharomyces Schizosaccharomyces pombe Proteins Transfection

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