The Tubulation Activity of a Fission Yeast F-BAR Protein Is Dispensable for Its Function in Cytokinesis

McDonald, Nathan A.; Takizawa, Yoshimasa; Feoktistova, Anna; Xu, Ping; Ohi, Melanie D.; Vander Kooi, Craig W.; Gould, Kathleen L.

doi:10.1016/j.celrep.2015.12.062

Title: The Tubulation Activity of a Fission Yeast F-BAR Protein Is Dispensable for Its Function in Cytokinesis

Journal Article · Thu Jan 14 00:00:00 EST 2016 · Cell Reports

DOI:https://doi.org/10.1016/j.celrep.2015.12.062· OSTI ID:1251216

McDonald, Nathan A. ^[1]; Takizawa, Yoshimasa ^[2]; Feoktistova, Anna ^[1]; Xu, Ping ^[3]; Ohi, Melanie D. ^[1]; Vander Kooi, Craig W. ^[3]; Gould, Kathleen L. ^[1]

Vanderbilt Univ., Nashville, TN (United States)
Vanderbilt Univ., Nashville, TN (United States); Okinawa Inst. of Science and Technology (Japan)
Univ. of Kentucky, Lexington, KY (United States)

F-BAR proteins link cellular membranes to the actin cytoskeleton in many biological processes. Here we investigated the function of the Schizosaccharomyces pombe Imp2 F-BAR domain in cytokinesis and find that it is critical for Imp2’s role in contractile ring constriction and disassembly. To understand mechanistically how the F-BAR domain functions, we determined its structure, elucidated how it interacts with membranes, and identified an interaction between dimers that allows helical oligomerization and membrane tubulation. Using mutations that block either membrane binding or tubulation, we find that membrane binding is required for Imp2’s cytokinetic function but that oligomerization and tubulation, activities often deemed central to F-BAR protein function, are dispensable. Accordingly, F-BARs that do not have the capacity to tubulate membranes functionally substitute for the Imp2 F-BAR, establishing that its major role is as a cell-cycle-regulated bridge between the membrane and Imp2 protein partners, rather than as a driver of membrane curvature.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: National Institutes of Health (NIH)

Grant/Contract Number:: P20GM103486; GM101035

OSTI ID:: 1251216

Journal Information:: Cell Reports, Vol. 14, Issue 3; ISSN 2211-1247

Publisher:: ElsevierCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 23 works

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The intrinsically disordered region of the cytokinetic F-BAR protein Cdc15 performs a unique essential function in maintenance of cytokinetic ring integrity Mangione, MariaSanta C.; Snider, Chloe E.; Gould, Kathleen L. Molecular Biology of the Cell, Vol. 30, Issue 22 https://doi.org/10.1091/mbc.e19-06-0314	journal	October 2019
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