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Regulation of TGF-β Superfamily Signaling by SMAD Mono-Ubiquitination
TGF-β(transforming growth factor-β) superfamily signaling mediators are important regulators of diverse physiological and pathological events. TGF-β signals are transduced by transmembrane type I and type II serine/threonine kinase receptors and their downstream effectors, the SMAD (drosophila mothe...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4276910/ https://www.ncbi.nlm.nih.gov/pubmed/25317929 http://dx.doi.org/10.3390/cells3040981 |
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author | Xie, Feng Zhang, Zhengkui van Dam, Hans Zhang, Long Zhou, Fangfang |
author_facet | Xie, Feng Zhang, Zhengkui van Dam, Hans Zhang, Long Zhou, Fangfang |
author_sort | Xie, Feng |
collection | PubMed |
description | TGF-β(transforming growth factor-β) superfamily signaling mediators are important regulators of diverse physiological and pathological events. TGF-β signals are transduced by transmembrane type I and type II serine/threonine kinase receptors and their downstream effectors, the SMAD (drosophila mothers against decapentaplegic protein) proteins. Numerous studies have already demonstrated crucial regulatory roles for modification of TGF-β pathway components by poly-ubiquitination. Recently, several studies also uncovered mono-ubiquitination of SMADs as a mechanism for SMAD activation or inactivation. Mono-ubiquitination and subsequent deubiquitination of SMAD proteins accordingly play important roles in the control of TGF-β superfamily signaling. This review highlights the major pathways regulated by SMAD mono-ubiquitination. |
format | Online Article Text |
id | pubmed-4276910 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-42769102015-01-15 Regulation of TGF-β Superfamily Signaling by SMAD Mono-Ubiquitination Xie, Feng Zhang, Zhengkui van Dam, Hans Zhang, Long Zhou, Fangfang Cells Review TGF-β(transforming growth factor-β) superfamily signaling mediators are important regulators of diverse physiological and pathological events. TGF-β signals are transduced by transmembrane type I and type II serine/threonine kinase receptors and their downstream effectors, the SMAD (drosophila mothers against decapentaplegic protein) proteins. Numerous studies have already demonstrated crucial regulatory roles for modification of TGF-β pathway components by poly-ubiquitination. Recently, several studies also uncovered mono-ubiquitination of SMADs as a mechanism for SMAD activation or inactivation. Mono-ubiquitination and subsequent deubiquitination of SMAD proteins accordingly play important roles in the control of TGF-β superfamily signaling. This review highlights the major pathways regulated by SMAD mono-ubiquitination. MDPI 2014-10-15 /pmc/articles/PMC4276910/ /pubmed/25317929 http://dx.doi.org/10.3390/cells3040981 Text en © 2014 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/4.0/). |
spellingShingle | Review Xie, Feng Zhang, Zhengkui van Dam, Hans Zhang, Long Zhou, Fangfang Regulation of TGF-β Superfamily Signaling by SMAD Mono-Ubiquitination |
title | Regulation of TGF-β Superfamily Signaling by SMAD Mono-Ubiquitination |
title_full | Regulation of TGF-β Superfamily Signaling by SMAD Mono-Ubiquitination |
title_fullStr | Regulation of TGF-β Superfamily Signaling by SMAD Mono-Ubiquitination |
title_full_unstemmed | Regulation of TGF-β Superfamily Signaling by SMAD Mono-Ubiquitination |
title_short | Regulation of TGF-β Superfamily Signaling by SMAD Mono-Ubiquitination |
title_sort | regulation of tgf-β superfamily signaling by smad mono-ubiquitination |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4276910/ https://www.ncbi.nlm.nih.gov/pubmed/25317929 http://dx.doi.org/10.3390/cells3040981 |
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