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BMC Cell Biology

, 6:45

First Online: 08 December 2005Received: 02 September 2005Accepted: 08 December 2005

Abstract

BackgroundCysteine-rich protein 1 CRP1 is a LIM domain containing protein localized to the nucleus and the actin cytoskeleton. CRP1 has been demonstrated to bind the actin-bundling protein α-actinin and proposed to modulate the actin cytoskeleton; however, specific regulatory mechanisms have not been identified.

ResultsCRP1 expression increased actin bundling in rat embryonic fibroblasts. Although CRP1 did not affect the bundling activity of α-actinin, CRP1 was found to stabilize the interaction of α-actinin with actin bundles and to directly bundle actin microfilaments. Using confocal and photobleaching fluorescence resonance energy transfer FRET microscopy, we demonstrate that there are two populations of CRP1 localized along actin stress fibers, one associated through interaction with α-actinin and one that appears to bind the actin filaments directly. Consistent with a role in regulating actin filament cross-linking, CRP1 also localized to the membrane ruffles of spreading and PDGF treated fibroblasts.

ConclusionCRP1 regulates actin filament bundling by directly cross-linking actin filaments and stabilizing the interaction of α-actinin with actin filament bundles.

List of abbreviationsRILreversion-induced LIM

FHL3Four and a half LIM domain protein 3

ENHenigma homologue protein

ALPactinin-associated LIM protein

CLIM36kDa carboxyl terminal LIM domain protein

CRPcysteine-rich protein

F-actinfilamentous actin

PDGFplatelet-derived growth factor

CFPcyan fluorescent protein

YFPyellow fluorescent protein

REFsrat embryonic fibroblasts.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2121-6-45 contains supplementary material, which is available to authorized users.

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Autor: Thuan C Tran - CoreyAyne Singleton - Tamara S Fraley - Jeffrey A Greenwood

Fuente: https://link.springer.com/article/10.1186/1471-2121-6-45







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