5C1F

Structure of the Imp2 F-BAR domain

Summary for 5C1F

• Entry DOI: 10.2210/pdb5c1f/pdb
• Descriptor: Septation protein imp2, FORMIC ACID (3 entities in total)
• Functional Keywords: imp2 f-bar membrane binding, cell cycle
• Biological source: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
• Total number of polymer chains: 2
• Total formula weight: 71960.66

Authors

Vander Kooi, C.W. (deposition date: 2015-06-13, release date: 2016-01-27, Last modification date: 2024-10-30)

Primary citation

McDonald, N.A.,Takizawa, Y.,Feoktistova, A.,Xu, P.,Ohi, M.D.,Vander Kooi, C.W.,Gould, K.L.
The Tubulation Activity of a Fission Yeast F-BAR Protein Is Dispensable for Its Function in Cytokinesis.
Cell Rep, 14:534-546, 2016

PubMed Abstract: 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.

PubMed: 26776521
DOI: 10.1016/j.celrep.2015.12.062

Experimental method

X-RAY DIFFRACTION (2.3551 Å)