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Hsp25, a member of the Hsp30 family, promotes inclusion formation in response to stress
Author(s) -
Katoh Yumiko,
Fujimoto Mitsuaki,
Nakamura Kosuke,
Inouye Sachiye,
Sugahara Kazuma,
Izu Hanae,
Nakai Akira
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2003.12.085
Subject(s) - aggresome , heat shock protein , inclusion bodies , hsp70 , microbiology and biotechnology , biology , protein aggregation , hsp27 , hela , proteasome , gene , protein folding , subfamily , cloning (programming) , ubiquitin , chemistry , genetics , cell culture , escherichia coli , computer science , programming language
Protein aggregates are oligomeric complexes of misfolded proteins, and serve as the seeds of inclusion bodies termed aggresomes in the cells. Heat shock proteins (Hsps) prevent misfolding and aggregate formation. Here, we found that only avian Hsp25 dominantly accumulated in the aggresomes induced by proteasome inhibition. Molecular cloning of chicken Hsp25 (cHsp25) revealed that it belongs to the Hsp30 family, which is a subfamily of the α‐crystallin/small Hsp gene family. Unexpectedly, overexpression of cHsp25 into HeLa cells promoted inclusion formation whereas overexpression of mouse Hsp27 and its chicken homologue did not. These results suggest that cHsp25 acts differently from other small Hsps on protein aggregates.