Table of Contents
International Scholarly Research Notices
Volume 2014, Article ID 637295, 23 pages
Review Article

The Membrane Associated RING-CH Proteins: A Family of E3 Ligases with Diverse Roles through the Cell

1Department of Immunology, University of Connecticut Health Center, L3056, Mc1319, 263 Farmington Avenue, Farmington, CT 06030, USA
2Department of Cellular and Molecular Physiology, Yale School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA
3Department of Pathology, Yale School of Medicine, LH315B, 310 Cedar Street, New Haven, CT 06524, USA

Received 1 July 2014; Accepted 22 August 2014; Published 29 October 2014

Academic Editor: Jerome Moreaux

Copyright © 2014 Tasleem Samji et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Since the discovery that conjugation of ubiquitin to proteins can drive proteolytic degradation, ubiquitination has been shown to perform a diverse range of functions in the cell. It plays an important role in endocytosis, signal transduction, trafficking of vesicles inside the cell, and even DNA repair. The process of ubiquitination-mediated control has turned out to be remarkably complex, involving a diverse array of proteins and many levels of control. This review focuses on a family of structurally related E3 ligases termed the membrane-associated RING-CH (MARCH) ubiquitin ligases, which were originally discovered as structural homologs to the virals E3s, K3, and K5 from Kaposi’s sarcoma-associated herpesvirus (KSHV). These proteins contain a catalytic RING-CH finger and are typically membrane-bound, with some having up to 14 putative transmembrane domains. Despite several lines of evidence showing that the MARCH proteins play a complex and essential role in several cellular processes, this family remains understudied.