4XH3

Mechanistic insights into anchorage of the contractile ring from yeast to humans

4XH3 の概要

• エントリーDOI: 10.2210/pdb4xh3/pdb
• 関連するPDBエントリー: 4XOH 4XOI
• 分子名称: Actin-binding protein anillin (2 entities in total)
• 機能のキーワード: c2, cell cycle
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Nucleus: Q9NQW6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46765.29

構造登録者

Sun, L.F.,Guan, R.F.,Chen, Z.C. (登録日: 2015-01-04, 公開日: 2015-07-15, 最終更新日: 2024-05-29)

主引用文献

Sun, L.,Guan, R.,Lee, I.J.,Liu, Y.,Chen, M.,Wang, J.,Wu, J.Q.,Chen, Z.
Mechanistic insights into the anchorage of the contractile ring by anillin and mid1
Dev.Cell, 33:413-426, 2015

PubMed Abstract: Anillins and Mid1 are scaffold proteins that play key roles in anchorage of the contractile ring at the cell equator during cytokinesis in animals and fungi, respectively. Here, we report crystal structures and functional analysis of human anillin and S. pombe Mid1. The combined data show anillin contains a cryptic C2 domain and a Rho-binding domain. Together with the tethering PH domain, three membrane-associating elements synergistically bind to RhoA and phospholipids to anchor anillin at the cleavage furrow. Surprisingly, Mid1 also binds to the membrane through a cryptic C2 domain. Dimerization of Mid1 leads to high affinity and preference for PI(4,5)P2, which stably anchors Mid1 at the division plane, bypassing the requirement for Rho GTPase. These findings uncover the unexpected general machinery and the divergent regulatory logics for the anchorage of the contractile ring through the anillin/Mid1 family proteins from yeast to humans.

PubMed: 25959226
DOI: 10.1016/j.devcel.2015.03.003

実験手法

X-RAY DIFFRACTION (2.1 Å)