Premium
Transient increase in vimentin phosphorylation and vimentin‐HSC70 association in 9L rat brain tumor cells experiencing heat‐shock
Author(s) -
Cheng TingJen,
Lai YiuKay
Publication year - 1994
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240540111
Subject(s) - vimentin , phosphorylation , intermediate filament , shock (circulatory) , heat shock protein , heat shock , in vitro , microbiology and biotechnology , biology , chemistry , biochemistry , cytoskeleton , immunohistochemistry , medicine , gene , immunology , cell
Characteristic changes in vimentin were studied in 9L rat brain tumor cells treated at 45°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 protein70 (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.