In vivo evaluation of hsp27 as an inhibitor of actin polymerization: hsp27 limits actin stress fiber and focal adhesion formation after heat shock.

Abstract:

:The role of hsp27 as an inhibitor of actin polymerization was considered in the context of the actin cytoskeleton and its relationship with focal adhesion formation. The aim of this study was to evaluate the potential effects of hsp27 on focal adhesion formation as a relevant biological consequence of actin stress fiber formation. When hsp27 was overexpressed in stably transfected cells, cell attachment was delayed and recovery of disrupted stress fibers and focal adhesions was limited. In ROS 17/2.8 cells, heat shock caused the reversible disruption of stress fibers and focal adhesions. The loss of stress fibers and focal adhesions was associated with reduced phosphotyrosine on the focal adhesion kinase (FAK). Microinjection of recombinant 6-His hsp27 and phosphorylated 6-His hsp27 was used to demonstrate that nonphosphorylated hsp27 prevented the recovery of stress fibers and focal adhesions. These results provide in vivo evidence that hsp27 acts as an inhibitor of actin polymerization that can alter cellular interactions with extracellular environments by perturbation of stress fibers, and subsequently focal adhesions.

journal_name

J Cell Physiol

authors

Schneider GB,Hamano H,Cooper LF

doi

10.1002/(SICI)1097-4652(199812)177:4<575::AID-JCP8

keywords:

subject

Has Abstract

pub_date

1998-12-01 00:00:00

pages

575-84

issue

4

eissn

0021-9541

issn

1097-4652

pii

10.1002/(SICI)1097-4652(199812)177:4<575::AID-JCP8

journal_volume

177

pub_type

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