Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 28 June 2005
Vol. 2005, Issue 290, p. pe32
[DOI: 10.1126/stke.2902005pe32]


Wrestling with SUMO in a New Arena

Van G. Wilson* and Germán Rosas-Acosta

Department of Medical Microbiology and Immunology, College of Medicine, Texas A&M University System Health Science Center, College Station, TX 77843–1114, USA.

Abstract: Sumoylation is a widespread posttranslational modification thought to affect primarily nuclear proteins, especially transcription factors for which sumoylation usually results in repression of their transactivational function. Recent proteomics studies have greatly expanded the cadre of known SUMO substrates, and an increasing number of cytoplasmic proteins have been identified as SUMO targets. However, very few of these cytosolic proteins have been evaluated for the functional consequences of sumoylation. Rajan et al. now demonstrate that the activity of an integral cytoplasmic membrane channel-forming protein, K2P1, is completely abrogated by sumoylation at a single lysine residue on the cytoplasmic tail. This is the first report of a plasma membrane protein as a SUMO substrate and explains the long-standing inability to demonstrate functionality of K2P1. Apparently, K2P1 is stoichiometrically sumoylated under most cellular conditions, so it is constitutively inactive until desumoylated. These observations raise several intriguing questions, including: How and where does K2P1 become sumoylated? Why, unlike most known substrates, is K2P1 so efficiently sumoylated? and, What are the signals and SUMO proteases that trigger K2P1 desumoylation? But most importantly, the report by Rajan et al. expands the functional roles attributed to sumoylation into the new arena of membrane protein functional regulation and suggests that similar mechanisms may regulate the function of other pore proteins.

*To whom correspondence should be addressed. E-mail, wilson{at}

Citation: V. G. Wilson, G. Rosas-Acosta, Wrestling with SUMO in a New Arena. Sci. STKE 2005, pe32 (2005).

Read the Full Text

Interaction between Geminivirus Replication Protein and the SUMO-Conjugating Enzyme Is Required for Viral Infection.
M. A. Sanchez-Duran, M. B. Dallas, J. T. Ascencio-Ibanez, M. I. Reyes, M. Arroyo-Mateos, J. Ruiz-Albert, L. Hanley-Bowdoin, and E. R. Bejarano (2011)
J. Virol. 85, 9789-9800
   Abstract »    Full Text »    PDF »
Potassium Channel Silencing by Constitutive Endocytosis and Intracellular Sequestration.
S. Feliciangeli, M. P. Tardy, G. Sandoz, F. C. Chatelain, R. Warth, J. Barhanin, S. Bendahhou, and F. Lesage (2010)
J. Biol. Chem. 285, 4798-4805
   Abstract »    Full Text »    PDF »
Human Ubc9 Contributes to Production of Fully Infectious Human Immunodeficiency Virus Type 1 Virions.
T. Jaber, C. R. Bohl, G. L. Lewis, C. Wood, J. T. West Jr., and R. A. Weldon Jr. (2009)
J. Virol. 83, 10448-10459
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882