Document Detail

Interaction between urokinase receptor and heat shock protein MRJ enhances cell adhesion.
MedLine Citation:
PMID:  20372789     Owner:  NLM     Status:  MEDLINE    
The urokinase-type plasminogen activator receptor (uPAR) has diverse biological functions including roles in proteolysis, cell adhesion and cellular signaling. We identified a heat shock protein MRJ (DNAJB6) as a novel uPAR-interacting protein in a yeast two-hybrid screen and confirmed the interaction and co-localization by GST-pull down assays, and co-immunoprecipitation in cells transfected with MRJ. Endogenous interaction between uPAR and MRJ was also detected in breast cancer MDA-MB-231 cells. Deletion mapping demonstrated that the C-terminal region of MRJ is required to mediate its interaction with uPAR. To understand the biological function of the uPAR-MRJ complex, we determined whether MRJ regulated uPAR mediated adhesion to vitronectin in human embryonic kidney (HEK) 293 cells stably transfected with uPAR. After transfection with full length MRJ, there was a 50% increase in cell adhesion compared to the mock transfected control (p<0.01). This increase in adhesion is dependent on the uPAR/full length MRJ interaction as cells transfected with the mutant construct containing only N-terminal region or C-terminal region of MRJ had no increase in cell adhesion. The observed increase in adhesion to vitronectin by MRJ was also blocked by an anti-uPAR domain I antibody suggesting that the induced adhesion is at least in part contributed by uPAR on the cell surface. These data provide a novel mechanism by which uPAR plays a role in cell adhesion to vitronectin.
Charles Edo De Bock; Zhen Lin; Ahmed H Mekkawy; Jennifer A Byrne; Yao Wang
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  International journal of oncology     Volume:  36     ISSN:  1791-2423     ISO Abbreviation:  Int. J. Oncol.     Publication Date:  2010 May 
Date Detail:
Created Date:  2010-04-07     Completed Date:  2010-11-22     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9306042     Medline TA:  Int J Oncol     Country:  Greece    
Other Details:
Languages:  eng     Pagination:  1155-63     Citation Subset:  IM    
Leukaemia Foundation Research Laboratory, Queensland Institute of Medical Research, Herston, QLD, Australia.
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MeSH Terms
Breast Neoplasms / metabolism*
Cell Adhesion
Cell Line
Cell Line, Tumor
Gene Expression Regulation, Neoplastic*
Glutathione Transferase / metabolism
HSP40 Heat-Shock Proteins / metabolism*
Models, Biological
Molecular Chaperones / metabolism*
Nerve Tissue Proteins / metabolism*
Protein Structure, Tertiary
Receptors, Urokinase Plasminogen Activator / metabolism*
Signal Transduction
Two-Hybrid System Techniques
Vitronectin / metabolism
Reg. No./Substance:
0/DNAJB6 protein, human; 0/HSP40 Heat-Shock Proteins; 0/Molecular Chaperones; 0/Nerve Tissue Proteins; 0/Receptors, Urokinase Plasminogen Activator; 0/Vitronectin; EC Transferase

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