Activation of Trp3 by Inositol 1,4,5-Trisphosphate Receptors through Displacement of Inhibitory Calmodulin from a Common Binding Domain

Mammalian homologues of Drosophila Trp form plasma membrane channels that mediate Ca2+ influx in response to activation of phospholipase C and internal Ca2+ store depletion. Previous studies showed that human Trp3 is activated by inositol 1,4,5-trisphosphate (IP3) receptors (IP3Rs) and identified in...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2001-03, Vol.98 (6), p.3168-3173
Hauptverfasser:	Zhang, Zongming, Tang, Jisen, Tikunova, Svetlana, Johnson, J. David, Chen, Zhangguo, Qin, Ning, Dietrich, Alexander, Stefani, Enrico, Birnbaumer, Lutz, Zhu, Michael Xi
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites Binding, Competitive Biological Sciences Calcium Calcium - metabolism Calcium Channels - genetics Calcium Channels - metabolism Calmodulin - metabolism Cations, Divalent Cell Line Cell lines Cellular biology Drug interactions Fluorescence Goods and services tax HEK293 cells Humans Inhibitory concentration 50 Inositol 1 Inositol 1,4,5-Trisphosphate Receptors Molecular Sequence Data Peptides - metabolism Proteins Radiocarbon Receptors, Cytoplasmic and Nuclear - metabolism Trp3 protein TRPC Cation Channels
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