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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2006-10-07
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, Chan Young -- Dolmetsch, Richard -- New York, N.Y. -- Science. 2006 Oct 6;314(5796):64-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17023638" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Calcium/*metabolism ; Calcium Channels/*metabolism ; Calcium Signaling ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Humans ; Phospholipase C gamma/chemistry/*metabolism ; Protein Binding ; Protein Structure, Tertiary ; TRPC Cation Channels/*metabolism ; Transcription Factors, TFII/chemistry/*metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Publikationsdatum: 2010-10-12
    Beschreibung: Voltage- and store-operated calcium (Ca(2+)) channels are the major routes of Ca(2+) entry in mammalian cells, but little is known about how cells coordinate the activity of these channels to generate coherent calcium signals. We found that STIM1 (stromal interaction molecule 1), the main activator of store-operated Ca(2+) channels, directly suppresses depolarization-induced opening of the voltage-gated Ca(2+) channel Ca(V)1.2. STIM1 binds to the C terminus of Ca(V)1.2 through its Ca(2+) release-activated Ca(2+) activation domain, acutely inhibits gating, and causes long-term internalization of the channel from the membrane. This establishes a previously unknown function for STIM1 and provides a molecular mechanism to explain the reciprocal regulation of these two channels in cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, Chan Young -- Shcheglovitov, Aleksandr -- Dolmetsch, Ricardo -- DP1 OD003889/OD/NIH HHS/ -- DP1OD003889/OD/NIH HHS/ -- R01 NS048564/NS/NINDS NIH HHS/ -- R21MH087898/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2010 Oct 1;330(6000):101-5. doi: 10.1126/science.1191027.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929812" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Calcium/metabolism ; Calcium Channels, L-Type/chemistry/genetics/*metabolism ; Calcium Signaling ; Cell Line ; Cell Membrane/*metabolism ; Humans ; Ion Channel Gating ; Jurkat Cells ; Membrane Proteins/chemistry/genetics/*metabolism ; Models, Biological ; Neoplasm Proteins/chemistry/genetics/*metabolism ; Neurons/*metabolism ; Patch-Clamp Techniques ; Protein Binding ; Protein Structure, Tertiary ; Rats ; Rats, Sprague-Dawley ; T-Lymphocytes/*metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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