4xh3

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

spinqualitylabelsall models 4xh3, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xh3 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ANLN_HUMAN Publication Abstract from PubMed 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. Mechanistic insights into the anchorage of the contractile ring by anillin and mid1.,Sun L, Guan R, Lee IJ, Liu Y, Chen M, Wang J, Wu JQ, Chen Z Dev Cell. 2015 May 26;33(4):413-26. doi: 10.1016/j.devcel.2015.03.003. Epub 2015 , May 7. PMID:25959226 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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