| RDJ2 (DNAJA2) chaperones neural G protein signaling pathways. | |
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MedLine Citation:
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PMID: 18595009 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Alma Rosales-Hernandez; Katy E Beck; Xiaoxi Zhao; Andrew P Braun; Janice E A Braun |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-07-02 |
Journal Detail:
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Title: Cell stress & chaperones Volume: 14 ISSN: 1355-8145 ISO Abbreviation: Cell Stress Chaperones Publication Date: 2009 Jan |
Date Detail:
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Created Date: 2008-11-26 Completed Date: 2009-06-25 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 9610925 Medline TA: Cell Stress Chaperones Country: Netherlands |
Other Details:
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Languages: eng Pagination: 71-82 Citation Subset: IM |
Affiliation:
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Hotchkiss Brain Institute, Department of Physiology and Biophysics, University of Calgary, Calgary, AB, Canada T2N 4N1. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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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:
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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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