Reviews |
From the Department of Biology (Y.W.), Saint Louis University, Mo; and Department of Biochemistry and Biophysics (H.G.D.), University of North Carolina at Chapel Hill.
Correspondence to Yuqi Wang, Department of Biology, Saint Louis University, 128 Macelwane Hall, 3507 Laclede Ave, St Louis, MO 63103. E-mail ywang8{at}slu.edu
This Review is part of a thematic series on Ubiquitination, which includes the following articles:
Regulation of G Protein and Mitogen-Activated Protein Kinase Signaling by Ubiquitination: Insights From Model Organisms
Heart Failure and Protein Quality Control
Ubiquitin and Ubiquitin-Like Proteins in Protein Regulation
Seven-Transmembrane Receptors and Ubiquitination
Sudha K. Shenoy Guest Editor
Guanine nucleotide binding proteins (G proteins) and mitogen-activated protein kinases are highly conserved signaling molecules engaged in a wide variety of cellular processes. The strength and duration of signaling mediated by G proteins and mitogen-activated protein kinases are well known to be regulated via phosphorylation of pathway components. Over the past few years, it has become evident that many of the same signaling proteins also undergo ubiquitination, a posttranslational modification that typically leads to protein degradation. Consequently the strength and duration of signaling can also be modulated by regulating the abundance of signaling proteins. This article describes G protein and mitogen-activated protein kinasemediated signaling pathways that are known to be regulated by ubiquitination. The focus is on studies performed in the budding yeast Saccharomyces cerevisiae, as many principles governing this new regulatory mechanism were initially discovered in this model organism. Similar mechanisms uncovered in other model systems are also briefly discussed to illustrate the importance and universality of signaling regulation by ubiquitination.
Key Words: GPCR G proteins MAP kinases ubiquitination yeast
This article has been cited by other articles:
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S. K. Shenoy, A. S. Modi, A. K. Shukla, K. Xiao, M. Berthouze, S. Ahn, K. D. Wilkinson, W. E. Miller, and R. J. Lefkowitz {beta}-Arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2 PNAS, April 21, 2009; 106(16): 6650 - 6655. [Abstract] [Full Text] [PDF] |
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M. P. Torres, M. J. Lee, F. Ding, C. Purbeck, B. Kuhlman, N. V. Dokholyan, and H. G. Dohlman G Protein Mono-ubiquitination by the Rsp5 Ubiquitin Ligase J. Biol. Chem., March 27, 2009; 284(13): 8940 - 8950. [Abstract] [Full Text] [PDF] |
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Y. Wang, M. Zhu, M. Ayalew, and J. A. Ruff Down-regulation of Pkc1-mediated Signaling by the Deubiquitinating Enzyme Ubp3 J. Biol. Chem., January 25, 2008; 283(4): 1954 - 1961. [Abstract] [Full Text] [PDF] |
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