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The Journal of Neuroscience, October 8, 2008, 28(41):10443-10449; doi:10.1523/JNEUROSCI.3282-08.2008

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 Previous Article

Brief Communications
Targeting of RGS7/Gβ5 to the Dendritic Tips of ON-Bipolar Cells Is Independent of Its Association with Membrane Anchor R7BP

Yan Cao,1 Hongman Song,2 Haruhisa Okawa,4 Alapakkam P. Sampath,4,5,6 Maxim Sokolov,2,3 and Kirill A. Martemyanov1

1Department of Pharmacology, University of Minnesota, Minneapolis, Minnesota 55455, Departments of 2Biochemistry and 3Ophthalmology, West Virginia University Eye Institute, West Virginia University School of Medicine, Morgantown, West Virginia 26506, and 4Neuroscience Graduate Program, 5Zilkha Neurogenetic Institute, and 6Department of Physiology and Biophysics, University of Southern California, Los Angeles, California 90089

Correspondence should be addressed to Dr. Kirill Martemyanov, Department of Pharmacology, University of Minnesota, 6-120 Jackson Hall, 321 Church Street SE, Minneapolis, MN 55455. Email: martemyanov{at}umn.edu

Complexes of regulator of G-protein signaling (RGS) proteins with G-protein β5 (Gβ5) subunits are essential components of signaling pathways that regulate the temporal characteristics of light-evoked responses in vertebrate retinal photoreceptors and ON-bipolar cells. Recent studies have found that RGS/Gβ5 complexes bind to a new family of adapter proteins, R9AP (RGS9 anchor protein) and R7 family binding protein (R7BP), that in case of the RGS9/Gβ5 complex were shown to determine its precise subcellular targeting to either the outer segment of photoreceptors or postsynaptic structures of striatal neurons, respectively. In this study, we establish that another trimeric complex consisting of RGS7, Gβ5, and R7BP subunits is specifically targeted to the dendritic tips of retinal bipolar cells. However, examination of the mechanisms of complex targeting in vivo surprisingly revealed that the delivery of RGS7/Gβ5 to the dendrites of ON-bipolar cells occurs independently of its association with R7BP. These findings provide a new mechanism for adapter-independent targeting of RGS/Gβ5 complexes.

Key words: G-protein; signal transduction; RGS proteins; retina; intracellular targeting; knock-out mice

Received July 10, 2008; revised Aug. 31, 2008; accepted Sept. 11, 2008.

Correspondence should be addressed to Dr. Kirill Martemyanov, Department of Pharmacology, University of Minnesota, 6-120 Jackson Hall, 321 Church Street SE, Minneapolis, MN 55455. Email: martemyanov{at}umn.edu






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