New light on TRP and TRPL

Craig Montell

Research output: Contribution to journalArticle

Abstract

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 vive 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 n 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.

Original languageEnglish (US)
Pages (from-to)755-763
Number of pages9
JournalMolecular Pharmacology
Volume52
Issue number5
StatePublished - Nov 1997

ASJC Scopus subject areas

  • Pharmacology

Fingerprint Dive into the research topics of 'New light on TRP and TRPL'. Together they form a unique fingerprint.

  • Cite this

    Montell, C. (1997). New light on TRP and TRPL. Molecular Pharmacology, 52(5), 755-763.