Ubiquitin and Ubiquitin-Like Proteins in Protein Regulation

Author:

Herrmann Joerg1,Lerman Lilach O.1,Lerman Amir1

Affiliation:

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

Abstract

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.

Publisher

Ovid Technologies (Wolters Kluwer Health)

Subject

Cardiology and Cardiovascular Medicine,Physiology

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