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The Journal of Neuroscience, December 19, 2007, 27(51):14117-14127; doi:10.1523/JNEUROSCI.3884-07.2007

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Cellular/Molecular
Expression and Localization of RGS9-2/Gβ5/R7BP Complex In Vivo Is Set by Dynamic Control of Its Constitutive Degradation by Cellular Cysteine Proteases

Garret R. Anderson,¹ Rafael Lujan,² Arthur Semenov,¹ Marco Pravetoni,¹ Ekaterina N. Posokhova,¹ Joseph H. Song,¹ Vladimir Uversky,^3,4 Ching-Kang Chen,⁵ Kevin Wickman,¹ and Kirill A. Martemyanov¹

¹Department of Pharmacology, University of Minnesota, Minneapolis, Minnesota 55455, ²Departamento de Ciencias Médicas, Facultad de Medicina, Universidad de Castilla-La Mancha, 02006 Albacete, Spain, ³Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, ⁴Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, 142290, Russia, and ⁵Department of Biochemistry and Molecular Biology, Virginia Commonwealth University, Richmond, Virginia 23298

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

A member of regulator of G-protein signaling family, RGS9-2, is an essential modulator of signaling through neuronal dopamine and opioid G-protein-coupled receptors. Recent findings indicate that the abundance of RGS9-2 determines sensitivity of signaling in the locomotor and reward systems in the striatum. In this study we report the mechanism that sets the concentration of RGS9-2 in vivo, thus controlling G-protein signaling sensitivity in the region. We found that RGS9-2 possesses specific degradation determinants which target it for constitutive destruction by lysosomal cysteine proteases. Shielding of these determinants by the binding partner R7 binding-protein (R7BP) controls RGS9-2 expression at the posttranslational level. In addition, binding to R7BP in neurons targets RGS9-2 to the specific intracellular compartment, the postsynaptic density. Implementation of this mechanism throughout ontogenetic development ensures expression of RGS9-2/type 5 G-protein β subunit/R7BP complexes at postsynaptic sites in unison with increased signaling demands at mature synapses.

Key words: G-protein; signal transduction; RGS proteins; protein degradation; intracellular targeting; striatum

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Received Aug. 24, 2007; revised Oct. 15, 2007; accepted Nov. 6, 2007.

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

This article has been cited by other articles:

				G. R. Anderson, R. Lujan, and K. A. Martemyanov Changes in Striatal Signaling Induce Remodeling of RGS Complexes Containing G{beta}5 and R7BP Subunits Mol. Cell. Biol., June 1, 2009; 29(11): 3033 - 3044. [Abstract] [Full Text] [PDF]

				K. A. Martemyanov, C. M. Krispel, P. V. Lishko, M. E. Burns, and V. Y. Arshavsky Functional comparison of RGS9 splice isoforms in a living cell PNAS, December 30, 2008; 105(52): 20988 - 20993. [Abstract] [Full Text] [PDF]

				Y. Cao, H. Song, H. Okawa, A. P. Sampath, M. Sokolov, and K. A. Martemyanov Targeting of RGS7/G{beta}5 to the Dendritic Tips of ON-Bipolar Cells Is Independent of Its Association with Membrane Anchor R7BP J. Neurosci., October 8, 2008; 28(41): 10443 - 10449. [Abstract] [Full Text] [PDF]

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