Document Detail


Nmi interacts with Hsp105β and enhances the Hsp105β-mediated Hsp70 expression.
MedLine Citation:
PMID:  25088258     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The mammalian stress protein Hsp105α is expressed constitutively and is further induced under stress conditions, whereas the alternative spliced form, Hsp105β is only expressed during mild heat shock. We previously reported that Hsp105α is localized mainly in the cytoplasm, whereas Hsp105β is localized in the nucleus. Consistent with the different localization of these proteins, Hsp105β but not Hsp105α induces the expression of the major stress protein Hsp70. We here identified N-myc and Stat interactor (Nmi), as an Hsp105β-binding protein by yeast two-hybrid screening. Immunoprecipitation and pull-down assay showed that Nmi interacts with Hsp105β in vivo and in vitro. Luciferase reporter gene assay and Western blotting showed that Nmi enhances both the Hsp105β-induced phosphorylation of Stat3 and the Hsp105β-induced activation of the hsp70 promoter in a manner that is dependent on the Stat3-binding site, which results in an increase in Hsp70 protein levels. Most importantly, mild heat shock-induced Hsp70 expression, which is dependent on Hsp105β, is suppressed by knockdown of endogenous Nmi. These results suggest that Nmi has a role as a positive regulator of Hsp105β-mediated hsp70 gene expression along the Stat3 signaling pathway.
Authors:
Youhei Saito; Akihisa Yukawa; Masashi Matozaki; Hiroki Mikami; Tomohiro Yamagami; Nobuyuki Yamagishi; Takahisa Kuga; Takumi Hatayama; Yuji Nakayama
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-7-31
Journal Detail:
Title:  Experimental cell research     Volume:  -     ISSN:  1090-2422     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2014 Jul 
Date Detail:
Created Date:  2014-8-4     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2014. Published by Elsevier Inc.
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