| Literature DB >> 18184564 |
Tao Wang1, Xiaoyue Wang, Qiang Xie, Craig Montell.
Abstract
Phosphoinositide-specific phospholipase C (PLC) isozymes play roles in a diversity of processes including Drosophila phototransduction. In fly photoreceptor cells, the PLCbeta encoded by norpA is critical for activation of TRP channels. Here, we describe a PLCbeta regulator, STOPS, which encodes a SOCS box protein. Mutation of stops resulted in a reduced concentration of NORPA and a defect in stopping signaling following cessation of the light stimulus. NORPA has been proposed to have dual roles as a PLC- and GTPase-activating protein (GAP). We found that the slow termination resulting from expressing low levels of wild-type NORPA was suppressed by addition of normal amounts of an altered NORPA, which had wild-type GAP activity, but no PLC activity. STOPS is the first protein identified that specifically regulates PLCbeta protein concentration. Moreover, this work demonstrates that a PLCbeta derivative that does not promote TRP channel activation, still contributes to signaling in vivo.Entities:
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Year: 2008 PMID: 18184564 PMCID: PMC2253723 DOI: 10.1016/j.neuron.2007.11.020
Source DB: PubMed Journal: Neuron ISSN: 0896-6273 Impact factor: 17.173