4XOH: Mechanistic Insights Into Anchorage Of The Contractile Ring From Yeast To Humans

Citation:
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.
PDB ID: 4XOHDownload
MMDB ID: 130934
PDB Deposition Date: 2015/1/16
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Source Organism:
Similar Structures:
Biological Unit for 4XOH: dimeric; determined by author and by software (PISA)
Molecular Components in 4XOH
Label Count Molecule
Proteins (2 molecules)
2
Division MAL Foutue 1 Protein(Gene symbol: mid1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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