Membranes 2011, 1(4), 354-393; doi:10.3390/membranes1040354
Review

The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function

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Received: 26 October 2011; in revised form: 24 November 2011 / Accepted: 5 December 2011 / Published: 9 December 2011
(This article belongs to the Special Issue Biological Membrane Morphogenesis)
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.
Abstract: A large number of RING finger (RNF) proteins are present in eukaryotic cells and the majority of them are believed to act as E3 ubiquitin ligases. In humans, 49 RNF proteins are predicted to contain transmembrane domains, several of which are specifically localized to membrane compartments in the secretory and endocytic pathways, as well as to mitochondria and peroxisomes. They are thought to be molecular regulators of the organization and integrity of the functions and dynamic architecture of cellular membrane and membranous organelles. Emerging evidence has suggested that transmembrane RNF proteins control the stability, trafficking and activity of proteins that are involved in many aspects of cellular and physiological processes. This review summarizes the current knowledge of mammalian transmembrane RNF proteins, focusing on their roles and significance.
Keywords: endocytosis; ERAD; immune regulation; membrane trafficking; mitochondrial dynamics; proteasome; quality control; RNF; ubiquitin; ubiquitin ligase
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MDPI and ACS Style

Nakamura, N. The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function. Membranes 2011, 1, 354-393.

AMA Style

Nakamura N. The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function. Membranes. 2011; 1(4):354-393.

Chicago/Turabian Style

Nakamura, Nobuhiro. 2011. "The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function." Membranes 1, no. 4: 354-393.


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