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Article

High-speed depolymerization at actin filament ends jointly catalysed by Twinfilin and Srv2/CAP.

Nature cell biology - 1 Nov 2015

Johnston Adam B, Collins Agnieszka, Goode Bruce L

Abstract excerpt

Purified actin filaments depolymerize slowly, and cytosolic conditions strongly favour actin assembly over disassembly, which has left our understanding of how actin filaments are rapidly turned over in vivo incomplete. One mechanism for driving filament disassembly is severing by factors such as Cofilin. However, even after severing, pointed-end depolymerization remains slow and unable to fully account for...

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Identifiers

PMID: 26458246
DOI: 10.1038/ncb3252
PMCID: PMC4808055

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High-speed depolymerization at actin filament ends jointly catalysed by Twinfilin and Srv2/CAP.PMID 26458246Read ↗

Srv2/cyclase-associated protein forms hexameric shurikens that directly catalyze actin filament severing by cofilin.Semantic proximity Read ↗

Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks.Semantic proximity Read ↗

A high-affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclase-associated protein.Semantic proximity Read ↗

The actin-severing activity of cofilin is exerted by the interplay of three distinct sites on cofilin and essential for cell viability.Semantic proximity Read ↗

Cofilin cross-bridges adjacent actin protomers and replaces part of the longitudinal F-actin interface.Semantic proximity Read ↗

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