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Title: HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain

Abstract

HSP40s are a subfamily of heat shock proteins (HSPs) and play important roles in regulation of cell proliferation, survival and apoptosis by serving as chaperones for HSP70s. Up to date hundreds of HSP40 proteins derived from various species ranging from Escherichia coli to homo sapiens have been identified. Here we report the cloning and characterization of a novel human type C DnaJ homologue, HDJC9, containing a typical N-terminal J domain. HDJC9 is upregulated at both mRNA and protein levels upon various stress and mitogenic stimulations. HDJC9 is mainly localized in cell nuclei under normal culture conditions while it is transported into cytoplasm and plasma membrane upon heat shock stress through a non-classical and lipid-dependent pathway. HDJC9 can interact with HSP70s and activate the ATPase activity of HSP70s, both of which are dependent on the J domain. Our data suggest that HDJC9 is a novel cochaperone for HSP70s.

Authors:
 [1];  [2];  [2];  [2];  [2];  [1];
  1. Institute of Immunology, Tsinghua University, Beijing 100084 (China)
  2. Institute of Immunology and National Key Laboratory of Medical Immunology, Second Military Medical University, 800 Xiangyin Road, Shanghai 200433 (China)
Publication Date:
OSTI Identifier:
20979785
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 353; Journal Issue: 2; Other Information: DOI: 10.1016/j.bbrc.2006.12.013; PII: S0006-291X(06)02647-7; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; APOPTOSIS; BIOLOGICAL STRESS; CELL NUCLEI; CELL PROLIFERATION; CLONING; CYTOPLASM; ESCHERICHIA COLI; GENES; HEAT; HEAT-SHOCK PROTEINS; LIPIDS

Citation Formats

Chaofeng, Han, Institute of Immunology and National Key Laboratory of Medical Immunology, Second Military Medical University, 800 Xiangyin Road, Shanghai 200433, Taoyong, Chen, Nan, Li, Mingjin, Yang, Tao, Wan, Xuetao, Cao, Institute of Immunology and National Key Laboratory of Medical Immunology, Second Military Medical University, 800 Xiangyin Road, Shanghai 200433, and sta net cn, E-mail: caoxt@public3. HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain. United States: N. p., 2007. Web.
Chaofeng, Han, Institute of Immunology and National Key Laboratory of Medical Immunology, Second Military Medical University, 800 Xiangyin Road, Shanghai 200433, Taoyong, Chen, Nan, Li, Mingjin, Yang, Tao, Wan, Xuetao, Cao, Institute of Immunology and National Key Laboratory of Medical Immunology, Second Military Medical University, 800 Xiangyin Road, Shanghai 200433, & sta net cn, E-mail: caoxt@public3. HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain. United States.
Chaofeng, Han, Institute of Immunology and National Key Laboratory of Medical Immunology, Second Military Medical University, 800 Xiangyin Road, Shanghai 200433, Taoyong, Chen, Nan, Li, Mingjin, Yang, Tao, Wan, Xuetao, Cao, Institute of Immunology and National Key Laboratory of Medical Immunology, Second Military Medical University, 800 Xiangyin Road, Shanghai 200433, and sta net cn, E-mail: caoxt@public3. 2007. "HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain". United States.
@article{osti_20979785,
title = {HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain},
author = {Chaofeng, Han and Institute of Immunology and National Key Laboratory of Medical Immunology, Second Military Medical University, 800 Xiangyin Road, Shanghai 200433 and Taoyong, Chen and Nan, Li and Mingjin, Yang and Tao, Wan and Xuetao, Cao and Institute of Immunology and National Key Laboratory of Medical Immunology, Second Military Medical University, 800 Xiangyin Road, Shanghai 200433 and sta net cn, E-mail: caoxt@public3},
abstractNote = {HSP40s are a subfamily of heat shock proteins (HSPs) and play important roles in regulation of cell proliferation, survival and apoptosis by serving as chaperones for HSP70s. Up to date hundreds of HSP40 proteins derived from various species ranging from Escherichia coli to homo sapiens have been identified. Here we report the cloning and characterization of a novel human type C DnaJ homologue, HDJC9, containing a typical N-terminal J domain. HDJC9 is upregulated at both mRNA and protein levels upon various stress and mitogenic stimulations. HDJC9 is mainly localized in cell nuclei under normal culture conditions while it is transported into cytoplasm and plasma membrane upon heat shock stress through a non-classical and lipid-dependent pathway. HDJC9 can interact with HSP70s and activate the ATPase activity of HSP70s, both of which are dependent on the J domain. Our data suggest that HDJC9 is a novel cochaperone for HSP70s.},
doi = {},
url = {https://www.osti.gov/biblio/20979785}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 2,
volume = 353,
place = {United States},
year = {Fri Feb 09 00:00:00 EST 2007},
month = {Fri Feb 09 00:00:00 EST 2007}
}