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The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function
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 se...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4021871/ https://www.ncbi.nlm.nih.gov/pubmed/24957874 http://dx.doi.org/10.3390/membranes1040354 |
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author | Nakamura, Nobuhiro |
author_facet | Nakamura, Nobuhiro |
author_sort | Nakamura, Nobuhiro |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4021871 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-40218712014-05-27 The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function Nakamura, Nobuhiro Membranes (Basel) Review 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. MDPI 2011-12-09 /pmc/articles/PMC4021871/ /pubmed/24957874 http://dx.doi.org/10.3390/membranes1040354 Text en © 2011 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Nakamura, Nobuhiro The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function |
title | The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function |
title_full | The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function |
title_fullStr | The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function |
title_full_unstemmed | The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function |
title_short | The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function |
title_sort | role of the transmembrane ring finger proteins in cellular and organelle function |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4021871/ https://www.ncbi.nlm.nih.gov/pubmed/24957874 http://dx.doi.org/10.3390/membranes1040354 |
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