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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1998-3-12
|
| pubmed:abstractText |
The neuronal protein GAP-43 is concentrated at the growth cone membrane, where it is thought to amplify the signal transduction process. As a model for its neuronal effects, GAP-43 protein injection into Xenopus laevis oocytes strongly augments the calcium-sensitive chloride current evoked by the G protein-coupled receptor stimulation. We have now examined a series of GAP-43 mutants in this system and determined those regions of GAP-43 required for this increase in current flux. As expected, palmitoylation inhibits signal amplification in oocytes by blocking G protein activation. Unexpectedly, a second domain of GAP-43 (residues 35-50) containing a protein kinase C phosphorylation site at residue 41 is also necessary for augmentation of G protein-coupled signals in oocytes. This region is not required for activation of isolated Go but is necessary for GAP-43 binding to isolated calmodulin and to isolated protein kinase C. Substitution of Asp for Ser41 inactivates GAP-43 as a signal facilitator in oocytes. This mutation blocks GAP-43 binding to both protein kinase C and calmodulin. Thus, GAP-43 regulates an oocyte signaling cascade via coordinated, simultaneous G protein activation and interaction with either calmodulin or protein kinase C.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Chloride Channels,
http://linkedlifedata.com/resource/pubmed/chemical/GAP-43 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Serotonin,
http://linkedlifedata.com/resource/pubmed/chemical/Serine
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0022-3042
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
70
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
983-92
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9489717-Amino Acid Substitution,
pubmed-meshheading:9489717-Animals,
pubmed-meshheading:9489717-Aspartic Acid,
pubmed-meshheading:9489717-Calmodulin,
pubmed-meshheading:9489717-Chloride Channels,
pubmed-meshheading:9489717-Electrophysiology,
pubmed-meshheading:9489717-GAP-43 Protein,
pubmed-meshheading:9489717-GTP-Binding Proteins,
pubmed-meshheading:9489717-Mutagenesis, Site-Directed,
pubmed-meshheading:9489717-Oocytes,
pubmed-meshheading:9489717-Palmitic Acid,
pubmed-meshheading:9489717-Phosphorylation,
pubmed-meshheading:9489717-Protein Kinase C,
pubmed-meshheading:9489717-Protein Structure, Tertiary,
pubmed-meshheading:9489717-Receptors, Serotonin,
pubmed-meshheading:9489717-Serine,
pubmed-meshheading:9489717-Signal Transduction,
pubmed-meshheading:9489717-Xenopus laevis
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
GAP-43 augmentation of G protein-mediated signal transduction is regulated by both phosphorylation and palmitoylation.
|
| pubmed:affiliation |
Department of Neurology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|