» Articles » PMID: 9545241

Two Distantly Positioned PDZ Domains Mediate Multivalent INAD-phospholipase C Interactions Essential for G Protein-coupled Signaling

Overview
Journal EMBO J
Date 1998 May 26
PMID 9545241
Citations 32
Authors
Affiliations
Soon will be listed here.
Abstract

Drosophila INAD, which contains five tandem protein interaction PDZ domains, plays an important role in the G protein-coupled visual signal transduction. Mutations in InaD alleles display mislocalization of signaling molecules of phototransduction which include the essential effector, phospholipase C-beta (PLC-beta), which is also known as NORPA. The molecular and biochemical details of this functional link are unknown. We report that INAD directly binds to NORPA via two terminally positioned PDZ1 and PDZ5 domains. PDZ1 binds to the C-terminus of NORPA, while PDZ5 binds to an internal region overlapping with the G box-homology region (a putative G protein-interacting site). The NORPA proteins lacking binding sites, which display normal basal PLC activity, can no longer associate with INAD in vivo. These truncations cause significant reduction of NORPA protein expression in rhabdomeres and severe defects in phototransduction. Thus, the two terminal PDZ domains of INAD, through intermolecular and/or intramolecular interactions, are brought into proximity in vivo. Such domain organization allows for the multivalent INAD-NORPA interactions which are essential for G protein-coupled phototransduction.

Citing Articles

Molecular Mechanism of Oocyte Activation in Mammals: Past, Present, and Future Directions.

Sugita H, Takarabe S, Kageyama A, Kawata Y, Ito J Biomolecules. 2024; 14(3).

PMID: 38540777 PMC: 10968515. DOI: 10.3390/biom14030359.


Neuronal Nitric Oxide Synthase (nNOS) in Neutrophils: An Insight.

Saini R, Azam Z, Sapra L, Srivastava R Rev Physiol Biochem Pharmacol. 2021; 180:49-83.

PMID: 34115206 DOI: 10.1007/112_2021_61.


Phospholipase C.

Bill C, Vines C Adv Exp Med Biol. 2019; 1131:215-242.

PMID: 31646512 PMC: 7790445. DOI: 10.1007/978-3-030-12457-1_9.


An unexpected INAD PDZ tandem-mediated plcβ binding in photo receptors.

Ye F, Huang Y, Li J, Ma Y, Xie C, Liu Z Elife. 2018; 7.

PMID: 30526850 PMC: 6300352. DOI: 10.7554/eLife.41848.


Light-dependent phosphorylation of the Drosophila inactivation no afterpotential D (INAD) scaffolding protein at Thr170 and Ser174 by eye-specific protein kinase C.

Voolstra O, Spat P, Oberegelsbacher C, Claussen B, Pfannstiel J, Huber A PLoS One. 2015; 10(3):e0122039.

PMID: 25799587 PMC: 4370639. DOI: 10.1371/journal.pone.0122039.


References
1.
Kim C, Park D, Rhee S . The role of carboxyl-terminal basic amino acids in Gqalpha-dependent activation, particulate association, and nuclear localization of phospholipase C-beta1. J Biol Chem. 1996; 271(35):21187-92. DOI: 10.1074/jbc.271.35.21187. View

2.
Kavanaugh W, Turck C, Williams L . PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science. 1995; 268(5214):1177-9. DOI: 10.1126/science.7539155. View

3.
McKay R, Chen D, Miller K, Kim S, Stark W, Shortridge R . Phospholipase C rescues visual defect in norpA mutant of Drosophila melanogaster. J Biol Chem. 1995; 270(22):13271-6. DOI: 10.1074/jbc.270.22.13271. View

4.
van der Geer P, Pawson T . The PTB domain: a new protein module implicated in signal transduction. Trends Biochem Sci. 1995; 20(7):277-80. DOI: 10.1016/s0968-0004(00)89043-x. View

5.
Kennedy M . Origin of PDZ (DHR, GLGF) domains. Trends Biochem Sci. 1995; 20(9):350. DOI: 10.1016/s0968-0004(00)89074-x. View