title: The Membrane Associated RING-CH Proteins: A Family of E3 Ligases with Diverse Roles through the Cell.
abstract: 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.
authors.affiliation: Department of Immunology, University of Connecticut Health Center, L3056, Mc1319, 263 Farmington Avenue, Farmington, CT 06030, USA.
authors.forename: Tasleem
authors.identifier: 0000-0003-1841-8600
authors.initials: T
authors.lastname: Samji
authors.affiliation: Department of Cellular and Molecular Physiology, Yale School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA.
authors.forename: Soonwook
authors.identifier: 0000-0002-1180-0762
authors.initials: S
authors.lastname: Hong
authors.affiliation: Department of Pathology, Yale School of Medicine, LH315B, 310 Cedar Street, New Haven, CT 06524, USA.
authors.forename: Robert E
authors.initials: RE
authors.lastname: Means