View : 20 Download: 8

Human Fas-associated factor 1 interacts with heat shock protein 70 and negatively regulates chaperone activity

Title
Human Fas-associated factor 1 interacts with heat shock protein 70 and negatively regulates chaperone activity
Authors
Kim H.-J.Eun J.S.Lee Y.-S.Kim E.Lee K.-J.
Ewha Authors
이공주김희정
SCOPUS Author ID
이공주scopus; 김희정scopusscopusscopus
Issue Date
2005
Journal Title
Journal of Biological Chemistry
ISSN
0021-9258JCR Link
Citation
vol. 280, no. 9, pp. 8125 - 8133
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
We examined the cell death-inducing property of human Fas-associated factor 1 (hFAF1) in the heat shock signaling pathway. By employing co-immunoprecipitation and peptide mass fingerprinting using matrix-assisted laser desorption ionization time-of-flight mass spectrometry, we found that hFAF1 binds to the 70-kDa heat shock protein family (Hsc70/Hsp70). Interaction mapping indicated that the 82-180 sequence of hFAF1 directly binds to the N-terminal region containing sequence 1-120 of Hsc70/Hsp70. This binding is very tight regardless of ATP and heat shock treatment. Hsc70/ Hsp70 and hFAF1 co-localized in the cytosol and nucleus and concentrated to the perinuclear region by heat shock treatment. We examined how hFAF1 regulates Hsp70 function, and found that hFAF1 inhibited the Hsp70 chaperone activity of refolding denatured protein substrates, accelerated heat shock-induced SAPK/ JNK activation, and raised heat shock-induced cell death in a binding dependent manner. These results suggest that hFAF1 prevents cells from recovery after stress by binding to and inhibiting the chaperone activity of Hsp70. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
DOI
10.1074/jbc.M406297200
Appears in Collections:
약학대학 > 약학과 > Journal papers
Files in This Item:
001.pdf(518.53 kB)Download
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE