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Article

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

Molecular biology of the cell - 1 Nov 2004

Mattila Pieta K, Quintero-Monzon Omar, Kugler Jamie, Moseley James B, Almo Steven C, Lappalainen Pekka, Goode Bruce L

Abstract excerpt

Cyclase-associated protein (CAP), also called Srv2 in Saccharomyces cerevisiae, is a conserved actin monomer-binding protein that promotes cofilin-dependent actin turnover in vitro and in vivo. However, little is known about the mechanism underlying this function. Here, we show that S. cerevisiae CAP binds with strong preference to ADP-G-actin (Kd 0.02 microM) compared with ATP-G-actin (Kd 1.9 microM) and...

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Identifiers

PMID: 15356265
DOI: 10.1091/mbc.e04-06-0444
PMCID: PMC524793

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