RT Journal Article
SR Electronic
T1 New Light on TRP and TRPL
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP 755
OP 763
DO 10.1124/mol.52.5.755
VO 52
IS 5
A1 Craig Montell
YR 1997
UL http://molpharm.aspetjournals.org/content/52/5/755.abstract
AB 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 ofDrosophila 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.