TY - JOUR
T1 - TRPγ, a Drosophila TRP-related subunit, forms a regulated cation channel with TRPL
AU - Xu, X. Z.Shawn
AU - Chien, Fred
AU - Butler, Alice
AU - Salkoff, Larry
AU - Montell, Craig
N1 - Funding Information:
We thank Atish Choudhury, Barbara Zwecker, and Matthew Friese for technical assistance; Todd Laverty for performing the in situ hybridizations to polytene chromosomes; Hong-Sheng Li for valuable discussions; and Denise Montell for comments on the manuscript. We also thank Charles Zuker for the trpl mutant and Roger Hardie for the trpl;trp double mutant flies. This work was supported by a grant from the National Eye Institute (EY10852) to C. M.
PY - 2000
Y1 - 2000
N2 - TRP and TRPL are two light-sensitive cation channel subunits required for the Drosophila photoresponse; however, our understanding of the identities, subunit composition, and function of the light-responsive channels is incomplete. To explain the residual photoresponse that remains in the trp mutant, a third TRP-related subunit has previously been proposed to function with TRPL. Here, we identify such a subunit, TRPγ. We show that TRPγ is highly enriched in photoreceptor cells and preferentially heteromultimerizes with TRPL in vitro and in vivo. The N-terminal domain of TRPγ dominantly suppressed the TRPL-dependent photoresponse, indicating that TRPγ-TRPL heteromultimers contribute to the photoresponse. While TRPL and TRPγ homomultimers are constitutively active, we demonstrate that TRPL-TRPγ heteromultimers form a regulated phospholipase C-(PLC-) stimulated channel.
AB - TRP and TRPL are two light-sensitive cation channel subunits required for the Drosophila photoresponse; however, our understanding of the identities, subunit composition, and function of the light-responsive channels is incomplete. To explain the residual photoresponse that remains in the trp mutant, a third TRP-related subunit has previously been proposed to function with TRPL. Here, we identify such a subunit, TRPγ. We show that TRPγ is highly enriched in photoreceptor cells and preferentially heteromultimerizes with TRPL in vitro and in vivo. The N-terminal domain of TRPγ dominantly suppressed the TRPL-dependent photoresponse, indicating that TRPγ-TRPL heteromultimers contribute to the photoresponse. While TRPL and TRPγ homomultimers are constitutively active, we demonstrate that TRPL-TRPγ heteromultimers form a regulated phospholipase C-(PLC-) stimulated channel.
UR - http://www.scopus.com/inward/record.url?scp=0033623942&partnerID=8YFLogxK
U2 - 10.1016/S0896-6273(00)81201-5
DO - 10.1016/S0896-6273(00)81201-5
M3 - Article
C2 - 10896160
AN - SCOPUS:0033623942
VL - 26
SP - 647
EP - 657
JO - Neuron
JF - Neuron
SN - 0896-6273
IS - 3
ER -