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The reticulons: a family of proteins with diverse functions
The reticulon family is a large and diverse group of membrane-associated proteins found throughout the eukaryotic kingdom. All of its members contain a carboxy-terminal reticulon homology domain that consists of two hydrophobic regions flanking a hydrophilic loop of 60-70 amino acids, but reticulon...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2007
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2246256/ https://www.ncbi.nlm.nih.gov/pubmed/18177508 http://dx.doi.org/10.1186/gb-2007-8-12-234 |
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author | Yang, Yvonne S Strittmatter, Stephen M |
author_facet | Yang, Yvonne S Strittmatter, Stephen M |
author_sort | Yang, Yvonne S |
collection | PubMed |
description | The reticulon family is a large and diverse group of membrane-associated proteins found throughout the eukaryotic kingdom. All of its members contain a carboxy-terminal reticulon homology domain that consists of two hydrophobic regions flanking a hydrophilic loop of 60-70 amino acids, but reticulon amino-terminal domains display little or no similarity to each other. Reticulons principally localize to the endoplasmic reticulum, and there is evidence that they influence endoplasmic reticulum-Golgi trafficking, vesicle formation and membrane morphogenesis. However, mammalian reticulons have also been found on the cell surface and mammalian reticulon 4 expressed on the surface of oligodendrocytes is an inhibitor of axon growth both in culture and in vivo. There is also growing evidence that reticulons may be important in neurodegenerative diseases such as Alzheimer's disease and amyotrophic lateral sclerosis. The diversity of structure, topology, localization and expression patterns of reticulons is reflected in their multiple, diverse functions in the cell. |
format | Text |
id | pubmed-2246256 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-22462562008-02-20 The reticulons: a family of proteins with diverse functions Yang, Yvonne S Strittmatter, Stephen M Genome Biol Protein Family Review The reticulon family is a large and diverse group of membrane-associated proteins found throughout the eukaryotic kingdom. All of its members contain a carboxy-terminal reticulon homology domain that consists of two hydrophobic regions flanking a hydrophilic loop of 60-70 amino acids, but reticulon amino-terminal domains display little or no similarity to each other. Reticulons principally localize to the endoplasmic reticulum, and there is evidence that they influence endoplasmic reticulum-Golgi trafficking, vesicle formation and membrane morphogenesis. However, mammalian reticulons have also been found on the cell surface and mammalian reticulon 4 expressed on the surface of oligodendrocytes is an inhibitor of axon growth both in culture and in vivo. There is also growing evidence that reticulons may be important in neurodegenerative diseases such as Alzheimer's disease and amyotrophic lateral sclerosis. The diversity of structure, topology, localization and expression patterns of reticulons is reflected in their multiple, diverse functions in the cell. BioMed Central 2007 2007-12-28 /pmc/articles/PMC2246256/ /pubmed/18177508 http://dx.doi.org/10.1186/gb-2007-8-12-234 Text en Copyright © 2007 BioMed Central Ltd |
spellingShingle | Protein Family Review Yang, Yvonne S Strittmatter, Stephen M The reticulons: a family of proteins with diverse functions |
title | The reticulons: a family of proteins with diverse functions |
title_full | The reticulons: a family of proteins with diverse functions |
title_fullStr | The reticulons: a family of proteins with diverse functions |
title_full_unstemmed | The reticulons: a family of proteins with diverse functions |
title_short | The reticulons: a family of proteins with diverse functions |
title_sort | reticulons: a family of proteins with diverse functions |
topic | Protein Family Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2246256/ https://www.ncbi.nlm.nih.gov/pubmed/18177508 http://dx.doi.org/10.1186/gb-2007-8-12-234 |
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