Transient increase in vimentin phosphorylation and vimentin-HSC70 association in 9L rat brain tumor cells experiencing heat-shock.

Abstract:

:Characteristic changes in vimentin were studied in 9L rat brain tumor cells treated at 45 degrees C. During heat-shock treatment, vimentin molecules were rapidly phosphorylated and reorganized from a filamentous form into a perinuclear higher-order structure that was less extractable by nonionic detergent. These effects were found to be highly transient, peaked at 30 min after the onset of heat-shock treatment, and subsided thereafter. Simultaneously, the solubility of the constitutively expressed heat-shock protein 70 (HSC70) was also temporarily decreased and the kinetics was identical to that of vimentin. The results indicated that HSC70 and vimentin were co-insolubilized during the heat-shock treatment. We propose that the reorganization of the intermediate filaments resulted from enhanced phosphorylation of vimentin leads to the concurrent association of HSC70 to the intermediate filaments. This process may play an essential role in regulating heat-shock genes.

journal_name

J Cell Biochem

authors

Cheng TJ,Lai YK

doi

10.1002/jcb.240540111

subject

Has Abstract

pub_date

1994-01-01 00:00:00

pages

100-9

issue

1

eissn

0730-2312

issn

1097-4644

journal_volume

54

pub_type

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