rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
6
|
pubmed:dateCreated |
2006-9-22
|
pubmed:abstractText |
G protein-coupled receptors (GPCRs) mediate cellular responses to a variety of stimuli, but how specific responses are regulated has been elusive, as the types of GPCRs vastly outnumber the classes of G protein heterotrimers available to initiate downstream signaling. In our analysis of signaling proteins containing DEP domains ( approximately 90 residue sequence motifs first recognized in fly Dishevelled, worm EGL-10, and mammalian Pleckstrin), we find that DEP domains are responsible for specific recognition of GPCRs. We examined the yeast regulator of G protein signaling (RGS) protein Sst2 and demonstrate that the DEP domains in Sst2 mediate binding to its cognate GPCR (Ste2). DEP-domain-mediated tethering promotes downregulation by placing the RGS protein in proximity to its substrate (receptor-activated Galpha subunit). Sst2 docks to the Ste2 cytosolic tail, but only its unphosphorylated state, allowing for release and recycling of this regulator upon receptor desensitization and internalization. DEP-domain-mediated targeting of effectors and regulators to specific GPCRs provides a means to dictate the nature, duration, and specificity of the response.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Mating Factor,
http://linkedlifedata.com/resource/pubmed/chemical/SST2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/STE2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0092-8674
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
22
|
pubmed:volume |
126
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1079-93
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:16990133-Amino Acid Sequence,
pubmed-meshheading:16990133-Cytosol,
pubmed-meshheading:16990133-Down-Regulation,
pubmed-meshheading:16990133-GTPase-Activating Proteins,
pubmed-meshheading:16990133-Models, Biological,
pubmed-meshheading:16990133-Molecular Sequence Data,
pubmed-meshheading:16990133-Phosphorylation,
pubmed-meshheading:16990133-Protein Binding,
pubmed-meshheading:16990133-Protein Structure, Tertiary,
pubmed-meshheading:16990133-Protein Subunits,
pubmed-meshheading:16990133-Receptors, G-Protein-Coupled,
pubmed-meshheading:16990133-Receptors, Mating Factor,
pubmed-meshheading:16990133-Saccharomyces cerevisiae,
pubmed-meshheading:16990133-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:16990133-Sequence Homology, Amino Acid,
pubmed-meshheading:16990133-Signal Transduction
|
pubmed:year |
2006
|
pubmed:articleTitle |
DEP-domain-mediated regulation of GPCR signaling responses.
|
pubmed:affiliation |
Department of Molecular and Cell Biology, Division of Biochemistry and Molecular Biology, University of California, Berkeley, CA 94720, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|