Source:http://linkedlifedata.com/resource/pubmed/id/16925983
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2006-8-30
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pubmed:abstractText |
Type 1 inositol 1,4,5-trisphosphate receptor (IP(3)R1) is a widely expressed intracellular calcium-release channel found in many cell types. The operation of IP(3)R1 is regulated through phosphorylation by multiple protein kinases. Extracellular signal-regulated kinase (ERK) has been found involved in calcium signaling in distinct cell types, but the underlying mechanisms remain unclear. Here, we present evidence that ERK1/2 and IP(3)R1 bind together through an ERK binding motif in mouse cerebellum in vivo as well as in vitro. ERK-phosphorylating serines (Ser 436) was identified in mouse IP(3)R1 and Ser 436 phosphorylation had a suppressive effect on IP(3) binding to the recombinant N-terminal 604-amino acid residues (N604). Moreover, phosphorylation of Ser 436 in R(224-604) evidently enhance its interaction with the N-terminal "suppressor" region (N223). At last, our data showed that Ser 436 phosphorylation in IP(3)R1 decreased Ca(2+) releasing through IP(3)R1 channels.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Signal-Regulated MAP...,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Serine
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
348
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1319-27
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16925983-Amino Acid Sequence,
pubmed-meshheading:16925983-Animals,
pubmed-meshheading:16925983-Binding Sites,
pubmed-meshheading:16925983-Calcium,
pubmed-meshheading:16925983-Calcium Channels,
pubmed-meshheading:16925983-Extracellular Signal-Regulated MAP Kinases,
pubmed-meshheading:16925983-Inositol 1,4,5-Trisphosphate Receptors,
pubmed-meshheading:16925983-Mice,
pubmed-meshheading:16925983-Microsomes,
pubmed-meshheading:16925983-Molecular Sequence Data,
pubmed-meshheading:16925983-Phosphorylation,
pubmed-meshheading:16925983-Protein Structure, Tertiary,
pubmed-meshheading:16925983-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:16925983-Serine
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pubmed:year |
2006
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pubmed:articleTitle |
Inositol 1,4,5-trisphosphate receptor type 1 phosphorylation and regulation by extracellular signal-regulated kinase.
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pubmed:affiliation |
Laboratory of Molecular and Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100080, PR China. baiguirong@yahoo.com
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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