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A Review on Ubiquitination of Neurotrophin Receptors: Facts and Perspectives
Ubiquitination is a reversible post-translational modification involved in a plethora of different physiological functions. Among the substrates that are ubiquitinated, neurotrophin receptors (TrkA, TrkB, TrkC, and p75(NTR)) have been studied recently. TrkA is the most studied receptor in terms of i...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5372643/ https://www.ncbi.nlm.nih.gov/pubmed/28335430 http://dx.doi.org/10.3390/ijms18030630 |
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author | Sánchez-Sánchez, Julia Arévalo, Juan Carlos |
author_facet | Sánchez-Sánchez, Julia Arévalo, Juan Carlos |
author_sort | Sánchez-Sánchez, Julia |
collection | PubMed |
description | Ubiquitination is a reversible post-translational modification involved in a plethora of different physiological functions. Among the substrates that are ubiquitinated, neurotrophin receptors (TrkA, TrkB, TrkC, and p75(NTR)) have been studied recently. TrkA is the most studied receptor in terms of its ubiquitination, and different E3 ubiquitin ligases and deubiquitinases have been implicated in its ubiquitination, whereas not much is known about the other neurotrophin receptors aside from their ubiquitination. Additional studies are needed that focus on the ubiquitination of TrkB, TrkC, and p75(NTR) in order to further understand the role of ubiquitination in their physiological and pathological functions. Here we review what is currently known regarding the ubiquitination of neurotrophin receptors and its physiological and pathological relevance. |
format | Online Article Text |
id | pubmed-5372643 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-53726432017-04-10 A Review on Ubiquitination of Neurotrophin Receptors: Facts and Perspectives Sánchez-Sánchez, Julia Arévalo, Juan Carlos Int J Mol Sci Review Ubiquitination is a reversible post-translational modification involved in a plethora of different physiological functions. Among the substrates that are ubiquitinated, neurotrophin receptors (TrkA, TrkB, TrkC, and p75(NTR)) have been studied recently. TrkA is the most studied receptor in terms of its ubiquitination, and different E3 ubiquitin ligases and deubiquitinases have been implicated in its ubiquitination, whereas not much is known about the other neurotrophin receptors aside from their ubiquitination. Additional studies are needed that focus on the ubiquitination of TrkB, TrkC, and p75(NTR) in order to further understand the role of ubiquitination in their physiological and pathological functions. Here we review what is currently known regarding the ubiquitination of neurotrophin receptors and its physiological and pathological relevance. MDPI 2017-03-14 /pmc/articles/PMC5372643/ /pubmed/28335430 http://dx.doi.org/10.3390/ijms18030630 Text en © 2017 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 (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Sánchez-Sánchez, Julia Arévalo, Juan Carlos A Review on Ubiquitination of Neurotrophin Receptors: Facts and Perspectives |
title | A Review on Ubiquitination of Neurotrophin Receptors: Facts and Perspectives |
title_full | A Review on Ubiquitination of Neurotrophin Receptors: Facts and Perspectives |
title_fullStr | A Review on Ubiquitination of Neurotrophin Receptors: Facts and Perspectives |
title_full_unstemmed | A Review on Ubiquitination of Neurotrophin Receptors: Facts and Perspectives |
title_short | A Review on Ubiquitination of Neurotrophin Receptors: Facts and Perspectives |
title_sort | review on ubiquitination of neurotrophin receptors: facts and perspectives |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5372643/ https://www.ncbi.nlm.nih.gov/pubmed/28335430 http://dx.doi.org/10.3390/ijms18030630 |
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