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(Circulation Research. 2007;100:1276.)
© 2007 American Heart Association, Inc.

Reviews

Ubiquitin and Ubiquitin-Like Proteins in Protein Regulation

Joerg Herrmann, Lilach O. Lerman, Amir Lerman

From the Division of Cardiovascular Diseases (J.H., A.L.) and the Division of Nephrology and Hypertension (L.O.L), Mayo Clinic, Rochester, Minn.

Correspondence to Amir Lerman, MD, Division of Cardiovascular Diseases, Mayo Clinic Rochester, 200 First St SW, Rochester, MN 55905. E-mail lerman.amir{at}mayo.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

Seven-Transmembrane Receptors and Ubiquitination

Ubiquitin and Ubiquitin-Like Proteins in Protein Regulation
Sudha K. Shenoy Guest Editor

The discovery of the ubiquitin system was awarded with the Nobel Prize in Chemistry in 2004. Labeling of intracellular proteins for degradation by a multienzymatic complex, called the proteasome, was identified as the main function of this system. Subsequently, it was discovered that the attachment of ubiquitin to proteins can modify their function without degradation. Finally, a number of other molecules were recognized to be conjugated to proteins in a manner similar to ubiquitin and were henceforth called ubiquitin-like proteins. This review provides an overview of this class of molecules and its implication for function, subcellular location, and half-life of proteins.

Key Words: cell cycle • inflammation • metabolism • protein • ubiquitinubiquitin-like proteins

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