Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1997-3-20
|
pubmed:abstractText |
Single-site variants in the calmodulin-binding domain of RC3/neurogranin were heterologously expressed in Xenopus oocytes to examine their effects on serotonin-evoked currents. RC3 variants serine36 -->alanine (Ser36-->Ala), serine36-->glycine (Ser36-->Gly), and phenylalanine37-->tryptophan (Phe37-->Trp), which bind calmodulin but are deficient in protein kinase C (PKC) phosphorylation, display serotonin-evoked Ca(2+)-dependent Cl- currents in oocytes similar to control oocytes. A serine36-->aspartate (Ser36-->Asp) variant, which does not bind calmodulin and mimics the PKC-phosphorylated state of RC3, significantly enhances serotonin-evoked currents in a manner similar to wild-type. The results suggest that RC3 not only regulates the availability of free calmodulin in a dendritic spine but also, when phosphorylated, independently stimulates G-protein coupled second messenger pathways that generate inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) and intracellular Ca2+.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chlorides,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neurogranin,
http://linkedlifedata.com/resource/pubmed/chemical/Serotonin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0304-3940
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
29
|
pubmed:volume |
219
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
183-6
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
pubmed-meshheading:8971810-Amino Acid Sequence,
pubmed-meshheading:8971810-Animals,
pubmed-meshheading:8971810-Calmodulin,
pubmed-meshheading:8971810-Calmodulin-Binding Proteins,
pubmed-meshheading:8971810-Chlorides,
pubmed-meshheading:8971810-Electric Conductivity,
pubmed-meshheading:8971810-Female,
pubmed-meshheading:8971810-Genetic Variation,
pubmed-meshheading:8971810-Molecular Sequence Data,
pubmed-meshheading:8971810-Nerve Tissue Proteins,
pubmed-meshheading:8971810-Neurogranin,
pubmed-meshheading:8971810-Oocytes,
pubmed-meshheading:8971810-Patch-Clamp Techniques,
pubmed-meshheading:8971810-Serotonin,
pubmed-meshheading:8971810-Xenopus laevis
|
pubmed:year |
1996
|
pubmed:articleTitle |
Functional studies of single-site variants in the calmodulin-binding domain of RC3/neurogranin in Xenopus oocytes.
|
pubmed:affiliation |
Mental Retardation Research Center, UCLA School of Medicine 90024-1759, USA. jwatson@npimain.medsch.ucla.edu
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|