Document Detail


RDJ2 (DNAJA2) chaperones neural G protein signaling pathways.
MedLine Citation:
PMID:  18595009     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A number of structurally divergent proteins with J domains, called J proteins, interact with and activate the ATPase of Hsp70s, thereby harnessing the ATPase activity for conformational work on target proteins. The precise role of most mammalian J proteins remains undefined. In this paper, we demonstrate that transient expression of the J protein, Rdj2, in HEK 293 cells increased cellular cyclic adenosine monophosphate (cAMP) levels in the presence of the beta-adrenergic agonist isoproterenol. In CNS-derived catecholaminergic neuronal cell line (CAD) neuroblastoma cells, expression of Rdj2 increased isoproterenol-stimulated phosphorylation of cAMP response element binding protein (CREB). Moreover, we have characterized the binding properties of Rdj2 and observed a direct interaction between Rdj2 and receptor-coupled trimeric GTP-binding proteins (G proteins). We further show that the composition of the Rdj2-chaperone complex and the cysteine string protein (CSPalpha)-chaperone complex, another J protein, is distinct. Our data demonstrate that Rdj2 modulates G protein signaling and further suggest that chaperoning G proteins is an emerging theme of the J protein network.
Authors:
Alma Rosales-Hernandez; Katy E Beck; Xiaoxi Zhao; Andrew P Braun; Janice E A Braun
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-07-02
Journal Detail:
Title:  Cell stress & chaperones     Volume:  14     ISSN:  1355-8145     ISO Abbreviation:  Cell Stress Chaperones     Publication Date:  2009 Jan 
Date Detail:
Created Date:  2008-11-26     Completed Date:  2009-06-25     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  9610925     Medline TA:  Cell Stress Chaperones     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  71-82     Citation Subset:  IM    
Affiliation:
Hotchkiss Brain Institute, Department of Physiology and Biophysics, University of Calgary, Calgary, AB, Canada T2N 4N1.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Brain / drug effects,  metabolism
Cell Line
Cyclic AMP / metabolism
Cyclic AMP Response Element-Binding Protein / metabolism
Escherichia coli / metabolism
Estrogens / pharmacology
GTP-Binding Proteins / metabolism*
HSC70 Heat-Shock Proteins / metabolism
HSP110 Heat-Shock Proteins / metabolism
HSP40 Heat-Shock Proteins / chemistry,  metabolism*
HSP90 Heat-Shock Proteins / metabolism
Mice
Molecular Chaperones / chemistry,  metabolism*
Molecular Sequence Data
Nervous System / drug effects,  metabolism*
Neuroblastoma / metabolism
Phosphorylation / drug effects
Protein Binding / drug effects
Rats
Signal Transduction* / drug effects
Chemical
Reg. No./Substance:
0/Cyclic AMP Response Element-Binding Protein; 0/Estrogens; 0/HSC70 Heat-Shock Proteins; 0/HSP110 Heat-Shock Proteins; 0/HSP40 Heat-Shock Proteins; 0/HSP90 Heat-Shock Proteins; 0/Molecular Chaperones; 60-92-4/Cyclic AMP; EC 3.6.1.-/GTP-Binding Proteins
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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