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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2001-7-12
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pubmed:databankReference |
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pubmed:abstractText |
Ca(2+) is a universal second messenger that is critical for cell growth and is intimately associated with many Ras-dependent cellular processes such as proliferation and differentiation. Ras is a small GTP binding protein that operates as a molecular switch regulating the control of gene expression, cell growth, and differentiation through a pathway from receptors to mitogen-activated protein kinases (MAPKs). A role for intracellular Ca(2+) in the activation of Ras has been previously demonstrated, e.g., via the nonreceptor tyrosine kinase PYK2 and by Ca(2+)/calmodulin-dependent guanine nucleotide exchange factors (GEFs) such as Ras-GRF; however, there is no Ca(2+)-dependent mechanism for direct inactivation. An important advance toward greater understanding of the complex coordination within the Ras-signaling network is the spatio-temporal analysis of signaling events in vivo. Here, we describe the identification of CAPRI (Ca(2+)-promoted Ras inactivator), a Ca(2+)-dependent Ras GTPase-activating protein (GAP) that switches off the Ras-MAPK pathway following a stimulus that elevates intracellular Ca(2+). Analysis of the spatio-temporal dynamics of CAPRI indicates that Ca(2+) regulates the GAP by a fast C2 domain-dependent translocation mechanism.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Serum-Free,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolase Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Histamine,
http://linkedlifedata.com/resource/pubmed/chemical/Ionomycin,
http://linkedlifedata.com/resource/pubmed/chemical/Ionophores,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ras GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ras Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0960-9822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
981-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11448776-Adenosine Triphosphate,
pubmed-meshheading:11448776-Amino Acid Sequence,
pubmed-meshheading:11448776-Animals,
pubmed-meshheading:11448776-Calcium,
pubmed-meshheading:11448776-Cell Line,
pubmed-meshheading:11448776-Culture Media, Serum-Free,
pubmed-meshheading:11448776-GTP Phosphohydrolase Activators,
pubmed-meshheading:11448776-Genes, Reporter,
pubmed-meshheading:11448776-Histamine,
pubmed-meshheading:11448776-Humans,
pubmed-meshheading:11448776-Immunoblotting,
pubmed-meshheading:11448776-Ionomycin,
pubmed-meshheading:11448776-Ionophores,
pubmed-meshheading:11448776-MAP Kinase Signaling System,
pubmed-meshheading:11448776-Molecular Sequence Data,
pubmed-meshheading:11448776-Protein Structure, Tertiary,
pubmed-meshheading:11448776-Recombinant Fusion Proteins,
pubmed-meshheading:11448776-Sequence Alignment,
pubmed-meshheading:11448776-ras GTPase-Activating Proteins,
pubmed-meshheading:11448776-ras Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
CAPRI regulates Ca(2+)-dependent inactivation of the Ras-MAPK pathway.
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pubmed:affiliation |
Department of Biochemistry, School of Medical Sciences, University of Bristol, BS8 1TD, Bristol, United Kingdom. P.J.Lockyer@bristol.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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