Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex

Jorge Chevesich, Andrew J. Kreuz, Craig Montell

Research output: Contribution to journalArticlepeer-review

Abstract

In Drosophila, the store-operated Ca2+ channel, TRP, is required in photoreceptor cells for a sustained response to light. Here, we show that TRP forms a complex with phospholipase C-β (NORPA), rhodopsin (RH1), calmodulin, and the PDZ domain containing protein INAD. Proteins with PDZ domains have previously been shown to cluster ion channels in vitro. We show that in InaD mutant flies, TRP is no longer spatially restricted to its normal subcellular compartment, the rhabdomere. These results provide evidence that a PDZ domain protein is required, in vivo, for anchoring of an ion channel to a signaling complex. Furthermore, disruption of this interaction results in retinal degeneration. We propose that the TRP channel is linked to NORPA and RH1 to facilitate feedback regulation of these upstream signaling molecules.

Original languageEnglish (US)
Pages (from-to)95-105
Number of pages11
JournalNeuron
Volume18
Issue number1
DOIs
StatePublished - Jan 1997

ASJC Scopus subject areas

  • Neuroscience(all)

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