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Cell Adhesion Molecules and Ubiquitination—Functions and Significance

Cell adhesion molecules of the immunoglobulin (Ig) superfamily represent the biggest group of cell adhesion molecules. They have been analyzed since approximately 40 years ago and most of them have been shown to play a role in tumor progression and in the nervous system. All members of the Ig superf...

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Detalles Bibliográficos
Autores principales: Homrich, Mirka, Gotthard, Ingo, Wobst, Hilke, Diestel, Simone
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4810158/
https://www.ncbi.nlm.nih.gov/pubmed/26703751
http://dx.doi.org/10.3390/biology5010001
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author Homrich, Mirka
Gotthard, Ingo
Wobst, Hilke
Diestel, Simone
author_facet Homrich, Mirka
Gotthard, Ingo
Wobst, Hilke
Diestel, Simone
author_sort Homrich, Mirka
collection PubMed
description Cell adhesion molecules of the immunoglobulin (Ig) superfamily represent the biggest group of cell adhesion molecules. They have been analyzed since approximately 40 years ago and most of them have been shown to play a role in tumor progression and in the nervous system. All members of the Ig superfamily are intensively posttranslationally modified. However, many aspects of their cellular functions are not yet known. Since a few years ago it is known that some of the Ig superfamily members are modified by ubiquitin. Ubiquitination has classically been described as a proteasomal degradation signal but during the last years it became obvious that it can regulate many other processes including internalization of cell surface molecules and lysosomal sorting. The purpose of this review is to summarize the current knowledge about the ubiquitination of cell adhesion molecules of the Ig superfamily and to discuss its potential physiological roles in tumorigenesis and in the nervous system.
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spelling pubmed-48101582016-04-04 Cell Adhesion Molecules and Ubiquitination—Functions and Significance Homrich, Mirka Gotthard, Ingo Wobst, Hilke Diestel, Simone Biology (Basel) Review Cell adhesion molecules of the immunoglobulin (Ig) superfamily represent the biggest group of cell adhesion molecules. They have been analyzed since approximately 40 years ago and most of them have been shown to play a role in tumor progression and in the nervous system. All members of the Ig superfamily are intensively posttranslationally modified. However, many aspects of their cellular functions are not yet known. Since a few years ago it is known that some of the Ig superfamily members are modified by ubiquitin. Ubiquitination has classically been described as a proteasomal degradation signal but during the last years it became obvious that it can regulate many other processes including internalization of cell surface molecules and lysosomal sorting. The purpose of this review is to summarize the current knowledge about the ubiquitination of cell adhesion molecules of the Ig superfamily and to discuss its potential physiological roles in tumorigenesis and in the nervous system. MDPI 2015-12-23 /pmc/articles/PMC4810158/ /pubmed/26703751 http://dx.doi.org/10.3390/biology5010001 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons by Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Homrich, Mirka
Gotthard, Ingo
Wobst, Hilke
Diestel, Simone
Cell Adhesion Molecules and Ubiquitination—Functions and Significance
title Cell Adhesion Molecules and Ubiquitination—Functions and Significance
title_full Cell Adhesion Molecules and Ubiquitination—Functions and Significance
title_fullStr Cell Adhesion Molecules and Ubiquitination—Functions and Significance
title_full_unstemmed Cell Adhesion Molecules and Ubiquitination—Functions and Significance
title_short Cell Adhesion Molecules and Ubiquitination—Functions and Significance
title_sort cell adhesion molecules and ubiquitination—functions and significance
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4810158/
https://www.ncbi.nlm.nih.gov/pubmed/26703751
http://dx.doi.org/10.3390/biology5010001
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