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Mol Pharmacol. 1997 Nov;52(5):755-63.

New light on TRP and TRPL.

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  • Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.


Store-operated Ca2+ entry, a mode of Ca2+ influx activated by depletion of Ca2+ from the internal stores, has been detected in a wide variety of cell types and may be the primary mechanism for Ca2+ entry in nonexcitable cells. Nevertheless, until recently, no candidate store-operated channel (SOC) had been identified molecularly. Through the serendipity of Drosophila genetics, a candidate SOC, referred to as Transient Receptor Potential (TRP), has been identified that is essential for the light-induced cation conductance in photoreceptor cells. A combination of in vitro and in vivo studies has provided strong evidence that TRP is a bona fide SOC. Moreover, TRP forms a supramolecular complex, proposed to be critical for feedback regulation and/or activation, that includes rhodopsin, phospholipase C, protein kinase C, calmodulin, and the PDZ domain-containing protein, INAD. INAD seems to be a scaffolding protein that links TRP with several of these other proteins in the complex. TRP also complexes with a related channel subunit, TRP-like, to form a heteromultimer with conductance characteristics distinct from those of TRP or TRP-like homomultimers. A family of proteins related to TRP is conserved from Caenorhabditis elegans to humans, and recent evidence indicates that at least some of these proteins are SOCs. The human TRP-related proteins may mediate many of the store-operated conductances that have been identified previously in a plethora of human cells.

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