6XJ1

Crystal Structure of CDC15 F-BAR Domain from Schizosaccharomyces pombe

6XJ1 の概要

• エントリーDOI: 10.2210/pdb6xj1/pdb
• 分子名称: Cell division control protein 15 (2 entities in total)
• 機能のキーワード: cell division control protein 15, cytoskeletal protein binding, cytoskeletal protein membrane adaptor, phospholipid binding, cell cycle
• 由来する生物種: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68074.45

構造登録者

Chandra, M.,Jackson, L.P.,Snider, C.E.,Gould, K.L. (登録日: 2020-06-22, 公開日: 2020-12-16, 最終更新日: 2023-10-18)

主引用文献

Snider, C.E.,Chandra, M.,McDonald, N.A.,Willet, A.H.,Collier, S.E.,Ohi, M.D.,Jackson, L.P.,Gould, K.L.
Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membrane Platform That Coordinates Cytoskeletal and Signaling Components for Cytokinesis.
Cell Rep, 33:108526-108526, 2020

PubMed Abstract: Many eukaryotes assemble an actin- and myosin-based cytokinetic ring (CR) on the plasma membrane (PM) for cell division, but how it is anchored there remains unclear. In Schizosaccharomyces pombe, the F-BAR protein Cdc15 links the PM via its F-BAR domain to proteins in the CR's interior via its SH3 domain. However, Cdc15's F-BAR domain also directly binds formin Cdc12, suggesting that Cdc15 may polymerize a protein network directly adjacent to the membrane. Here, we determine that the F-BAR domain binds Cdc12 using residues on the face opposite its membrane-binding surface. These residues also bind paxillin-like Pxl1, promoting its recruitment with calcineurin to the CR. Mutation of these F-BAR domain residues results in a shallower CR, with components localizing ∼35% closer to the PM than in wild type, and aberrant CR constriction. Thus, F-BAR domains serve as oligomeric membrane-bound platforms that can modulate the architecture of an entire actin structure.

PubMed: 33357436
DOI: 10.1016/j.celrep.2020.108526

実験手法

X-RAY DIFFRACTION (3.52 Å)