NDLI: Association of INAD with NORPA is essential for controlled activation and deactivation of Drosophila phototransduction in vivo

Content Provider	PubMed Central
Author	Shieh, Bih-hwa Zhu, Mei-ying Lee, John K. Kelly, Ingrid M. Bahiraei, Frohar
Copyright Year	1997
Abstract	Visual transduction in Drosophila is a G protein-coupled phospholipase C-mediated process that leads to depolarization via activation of the transient receptor potential (TRP) calcium channel. Inactivation-no-afterpotential D (INAD) is an adaptor protein containing PDZ domains known to interact with TRP. Immunoprecipitation studies indicate that INAD also binds to eye-specific protein kinase C and the phospholipase C, no-receptor-potential A (NORPA). By overlay assay and site-directed mutagenesis we have defined the essential elements of the NORPA–INAD association and identified three critical residues in the C-terminal tail of NORPA that are required for the interaction. These residues, Phe-Cys-Ala, constitute a novel binding motif distinct from the sequences recognized by the PDZ domain in INAD. To evaluate the functional significance of the INAD–NORPA association in vivo, we generated transgenic flies expressing a modified NORPA, NORPA C1094S , that lacks the INAD interaction. The transgenic animals display a unique electroretinogram phenotype characterized by slow activation and prolonged deactivation. Double mutant analysis suggests a possible inaccessibility of eye-specific protein kinase C to NORPA C1094S , undermining the observed defective deactivation, and that delayed activation may similarly result from NORPA C1094S being unable to localize in close proximity to the TRP channel. We conclude that INAD acts as a scaffold protein that facilitates NORPA–TRP interactions required for gating of the TRP channel in photoreceptor cells.
Starting Page	12682
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	94
Language	English
Publisher	The National Academy of Sciences of the USA
Publisher Date	1997-11-11
Access Restriction	Open
Rights Holder	The National Academy of Sciences of the USA
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Association of INAD with NORPA is essential for controlled activation and deactivation of Drosophila phototransduction in vivo.

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Association of INAD with NORPA is essential for controlled activation and deactivation of Drosophila phototransduction in vivo.

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