Document Detail


Function of phosducin-like proteins in G protein signaling and chaperone-assisted protein folding.
MedLine Citation:
PMID:  17658730     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Members of the phosducin gene family were initially proposed to act as down-regulators of G protein signaling by binding G protein betagamma dimers (Gbetagamma) and inhibiting their ability to interact with G protein alpha subunits (Galpha) and effectors. However, recent findings have over-turned this hypothesis by showing that most members of the phosducin family act as co-chaperones with the cytosolic chaperonin complex (CCT) to assist in the folding of a variety of proteins from their nascent polypeptides. In fact rather than inhibiting G protein pathways, phosducin-like protein 1 (PhLP1) has been shown to be essential for G protein signaling by catalyzing the folding and assembly of the Gbetagamma dimer. PhLP2 and PhLP3 have no role in G protein signaling, but they appear to assist in the folding of proteins essential in regulating cell cycle progression as well as actin and tubulin. Phosducin itself is the only family member that does not participate with CCT in protein folding, but it is believed to have a specific role in visual signal transduction to chaperone Gbetagamma subunits as they translocate to and from the outer and inner segments of photoreceptor cells during light-adaptation.
Authors:
Barry M Willardson; Alyson C Howlett
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review     Date:  2007-06-28
Journal Detail:
Title:  Cellular signalling     Volume:  19     ISSN:  0898-6568     ISO Abbreviation:  Cell. Signal.     Publication Date:  2007 Dec 
Date Detail:
Created Date:  2007-10-12     Completed Date:  2007-12-20     Revised Date:  2013-06-06    
Medline Journal Info:
Nlm Unique ID:  8904683     Medline TA:  Cell Signal     Country:  England    
Other Details:
Languages:  eng     Pagination:  2417-27     Citation Subset:  IM    
Affiliation:
Department of Chemistry and Biochemistry, C-100 BNSN, Brigham Young University Provo, Utah 84602, USA. bmwillardson@chem.byu.edu
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism
Amino Acid Sequence
Animals
Carrier Proteins / metabolism
Cell Cycle Proteins / metabolism
Chaperonin Containing TCP-1
Chaperonins / metabolism
Eye Proteins / metabolism
GTP-Binding Protein Regulators / chemistry,  metabolism*
GTP-Binding Protein beta Subunits / chemistry,  metabolism*
GTP-Binding Protein gamma Subunits / chemistry,  metabolism*
Humans
Models, Molecular
Molecular Chaperones / metabolism*
Molecular Sequence Data
Nerve Tissue Proteins / metabolism
Phosphoproteins / chemistry,  metabolism*
Protein Conformation
Protein Folding*
Retina / metabolism
Signal Transduction*
Tubulin / metabolism
Vision, Ocular
Grant Support
ID/Acronym/Agency:
EY12278/EY/NEI NIH HHS; R01 EY012287-09/EY/NEI NIH HHS; R01 GM078550-01A1/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Actins; 0/Carrier Proteins; 0/Cell Cycle Proteins; 0/Eye Proteins; 0/G-protein Beta gamma; 0/GTP-Binding Protein Regulators; 0/GTP-Binding Protein beta Subunits; 0/GTP-Binding Protein gamma Subunits; 0/Molecular Chaperones; 0/Nerve Tissue Proteins; 0/PDCL protein, human; 0/PDCL2 protein, human; 0/PDCL3 protein, human; 0/Phosphoproteins; 0/Tubulin; 0/phosducin; EC 3.6.1.-/Chaperonin Containing TCP-1; EC 3.6.1.-/Chaperonins
Comments/Corrections

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


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