Abstract
In Drosophila photoreceptors, phospholipase C (PLC) and other signalling components form multiprotein structures through the PDZ scaffold protein INAD. Association between PLC and INAD is important for termination of responses to light; the underlying mechanism is, however, unclear. Here we report that the maintenance of large amounts of PLC in the signalling membranes by association with INAD facilitates response terminator, and show that PLC functions as a GTPase-activating protein (GAP). The inactivation of the G protein by its target, the PLC, is crucial for reliable production of single-photon responses and for the high temporal and intensity resolution of the response to light.
| Original language | English |
|---|---|
| Pages (from-to) | 296-301 |
| Number of pages | 6 |
| Journal | Nature Cell Biology |
| Volume | 2 |
| Issue number | 5 |
| DOIs | |
| State | Published - 2000 |
Bibliographical note
Funding Information:ACKNOWLEDGEMENTS We thank. R. D. Shortridge for the anti NORPA antibodies, the T 6 mutant and the norpA+ gene and B.-H. Shieh for discussions and for the norpAC1094S mutant, W. L. Pak and C. S. Zuker for the norpA, Gαq 1 and inaD mutants respectively. We also thank H. Cedar, A. Shalom, M. Treinin and M. Danin for critical reading of the manuscript. The work was supported by grants from the NIH, (EY-03529 to B.M. and Z.S.), the US-Israel Binational Science Foundation (B.M., Z.S. and Z.P.), the Israel Science Foundation (to B.M. Z.S. and Z.P.), the Israel Cancer Fund (Z.P.), the German Israeli Foundation (B.M.) and the Minerva Foundation. Correspondence and requests for materials should be addressed to B.M.