Document Detail


Interaction of alpha1-syntrophin with multiple isoforms of heterotrimeric G protein alpha subunits.
MedLine Citation:
PMID:  18034856     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Syntrophins are components of the dystrophin-glycoprotein complex of the plasma membrane in muscular and neuronal cells, and recruit signaling proteins such as neuronal nitric oxide synthase via their multiple protein-protein interaction motifs. In this study, we found that alpha1-syntrophin binds to various subtypes of guanine nucleotide-binding protein alpha subunits (Galpha). A pull-down analysis using full-length recombinant alpha1-syntrophin and MS analysis showed that alpha1-syntrophin was coprecipitated with several isoforms of Galpha proteins in addition to known binding partners such as dystrobrevin and neuronal nitric oxide synthase. Further analysis using recombinant Galpha isoforms showed that alpha1-syntrophin associates with at least Galphai, Galphao, Galphas and Galphaq subtypes. The region of alpha1-syntrophin required for its interaction with Galphas was determined as the N-terminal half of the first pleckstrin homology domain. In addition, the syntrophin unique domain of alpha1-syntrophin was suggested to contribute to this interaction. In COS-7 cells, downregulation of alpha1-syntrophin by RNAi resulted in enhanced cAMP production and cAMP response element-binding protein phosphorylation induced by isoproterenol treatment. These results suggest that alpha1-syntrophin provides a scaffold for the Galpha family of heterotrimeric G proteins in the brain to regulate the efficiency of signal transduction evoked by G-protein-coupled receptors.
Authors:
Akiko Okumura; Katsuya Nagai; Nobuaki Okumura
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Publication Detail:
Type:  Journal Article     Date:  2007-11-23
Journal Detail:
Title:  The FEBS journal     Volume:  275     ISSN:  1742-464X     ISO Abbreviation:  FEBS J.     Publication Date:  2008 Jan 
Date Detail:
Created Date:  2008-01-04     Completed Date:  2008-04-03     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  England    
Other Details:
Languages:  eng     Pagination:  22-33     Citation Subset:  IM    
Affiliation:
Institute for Protein Research, Osaka University, Japan.
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MeSH Terms
Descriptor/Qualifier:
Animals
Binding Sites
COS Cells
Calcium-Binding Proteins / genetics,  metabolism*
Cercopithecus aethiops
Down-Regulation
GTP-Binding Protein alpha Subunits / metabolism*
Male
Mass Spectrometry
Membrane Proteins / genetics,  metabolism*
Mice
Muscle Proteins / genetics,  metabolism*
Protein Isoforms / metabolism
RNA Interference
Rats
Rats, Wistar
Chemical
Reg. No./Substance:
0/Calcium-Binding Proteins; 0/GTP-Binding Protein alpha Subunits; 0/Membrane Proteins; 0/Muscle Proteins; 0/Protein Isoforms; 0/syntrophin alpha1

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


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