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rdf:type |
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lifeskim:mentions |
umls-concept:C0022702,
umls-concept:C0439799,
umls-concept:C1335879,
umls-concept:C1426088,
umls-concept:C1514562,
umls-concept:C1823405,
umls-concept:C1879547,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2587213
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pubmed:issue |
29
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pubmed:dateCreated |
2009-7-13
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pubmed:abstractText |
STIM1 and STIM2 are dynamic transmembrane endoplasmic reticulum Ca(2+) sensors, coupling directly to activate plasma membrane Orai Ca(2+) entry channels. Despite extensive sequence homology, the STIM proteins are functionally distinct. We reveal that the short variable N-terminal random coil sequences of STIM1 and STIM2 confer profoundly different activation properties. Using Orai1-expressing HEK293 cells, chimeric replacement of the 43-amino-acid STIM1 N terminus with that of STIM2 attenuates Orai1-mediated Ca(2+) entry and drastically slows store-induced Orai1 channel activation. Conversely, the 55-amino-acid STIM2 terminus substituted within STIM1 strikingly enhances both Orai1-mediated Ca(2+) entry and constitutive coupling to activate Orai1 channels. Hence, STIM N termini are powerful coupling modifiers, functioning in STIM2 to "brake" the otherwise constitutive activation of Orai1 channels afforded by its high sensitivity to luminal Ca(2+).
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-10698739,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-11463338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-15866891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-16005298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-16204251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-16582901,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-16645049,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-16733527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-16751269,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-16766533,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-16860747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-16906149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-17020874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-17267286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-17434311,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-17602740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-17702753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-17905723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-18160041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-18166150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-18420579,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-18635545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-18854159,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-19019825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-19182790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-19189966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-19249086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19487696-19376967
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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/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ORAI1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/STIM1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/STIM2 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
19164-8
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pubmed:dateRevised |
2010-9-27
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pubmed:meshHeading |
pubmed-meshheading:19487696-Blotting, Western,
pubmed-meshheading:19487696-Calcium,
pubmed-meshheading:19487696-Calcium Channels,
pubmed-meshheading:19487696-Cell Adhesion Molecules,
pubmed-meshheading:19487696-Cell Line,
pubmed-meshheading:19487696-Humans,
pubmed-meshheading:19487696-Kinetics,
pubmed-meshheading:19487696-Membrane Potentials,
pubmed-meshheading:19487696-Membrane Proteins,
pubmed-meshheading:19487696-Neoplasm Proteins,
pubmed-meshheading:19487696-Patch-Clamp Techniques,
pubmed-meshheading:19487696-Recombinant Fusion Proteins,
pubmed-meshheading:19487696-Transfection
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pubmed:year |
2009
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pubmed:articleTitle |
The short N-terminal domains of STIM1 and STIM2 control the activation kinetics of Orai1 channels.
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pubmed:affiliation |
Department of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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