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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
46
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pubmed:dateCreated |
2010-11-8
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pubmed:abstractText |
The N-terminal ?220-amino acid region of the inositol 1,4,5-trisphosphate (IP(3)) receptor (IP(3)R)/Ca(2+) release channel has been referred to as the suppressor/coupling domain because it is required for both IP(3) binding suppression and IP(3)-induced channel gating. Measurements of IP(3)-induced Ca(2+) fluxes of mutagenized mouse type 1 IP(3)R (IP(3)R1) showed that the residues responsible for IP(3) binding suppression in this domain were not essential for channel opening. On the other hand, a single amino acid substitution of Tyr-167 to alanine completely impaired IP(3)-induced Ca(2+) release without reducing the IP(3) binding activity. The corresponding residue in type 3 IP(3)R (IP(3)R3), Trp-168, was also critical for channel opening. Limited trypsin digestion experiments showed that the trypsin sensitivities of the C-terminal gatekeeper domain differed markedly between the wild-type channel and the Tyr-167 mutant under the optimal conditions for channel opening. These results strongly suggest that the Tyr/Trp residue (Tyr-167 in IP(3)R1 and Trp-168 in IP(3)R3) is critical for the functional coupling between IP(3) binding and channel gating by maintaining the structural integrity of the C-terminal gatekeeper domain at least under activation gating.
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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/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1083-351X
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
12
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pubmed:volume |
285
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
36081-91
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pubmed:dateRevised |
2011-11-14
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pubmed:meshHeading |
pubmed-meshheading:20813840-Amino Acid Sequence,
pubmed-meshheading:20813840-Amino Acid Substitution,
pubmed-meshheading:20813840-Animals,
pubmed-meshheading:20813840-Binding Sites,
pubmed-meshheading:20813840-Blotting, Western,
pubmed-meshheading:20813840-Calcium,
pubmed-meshheading:20813840-Cell Line, Tumor,
pubmed-meshheading:20813840-Inositol 1,4,5-Trisphosphate,
pubmed-meshheading:20813840-Inositol 1,4,5-Trisphosphate Receptors,
pubmed-meshheading:20813840-Ion Channel Gating,
pubmed-meshheading:20813840-Ligands,
pubmed-meshheading:20813840-Mice,
pubmed-meshheading:20813840-Models, Molecular,
pubmed-meshheading:20813840-Molecular Sequence Data,
pubmed-meshheading:20813840-Mutagenesis, Site-Directed,
pubmed-meshheading:20813840-Mutation,
pubmed-meshheading:20813840-Protein Binding,
pubmed-meshheading:20813840-Protein Isoforms,
pubmed-meshheading:20813840-Protein Structure, Tertiary,
pubmed-meshheading:20813840-Sequence Homology, Amino Acid,
pubmed-meshheading:20813840-Trypsin,
pubmed-meshheading:20813840-Tryptophan,
pubmed-meshheading:20813840-Tyrosine
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pubmed:year |
2010
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pubmed:articleTitle |
Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor mediates functional coupling between ligand binding and channel opening.
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pubmed:affiliation |
Laboratory for Developmental Neurobiology, RIKEN Brain Science Institute, Saitama 351-0198, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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