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Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades

Autophagy contributes to cellular homeostasis through the degradation of various intracellular targets such as proteins, organelles and microbes. This relates autophagy to various diseases such as infections, neurodegenerative diseases and cancer. A central component of the autophagy machinery is th...

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Detalles Bibliográficos
Autores principales: Boutouja, Fahd, Brinkmeier, Rebecca, Mastalski, Thomas, El Magraoui, Fouzi, Platta, Harald W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5751144/
https://www.ncbi.nlm.nih.gov/pubmed/29186924
http://dx.doi.org/10.3390/ijms18122541
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author Boutouja, Fahd
Brinkmeier, Rebecca
Mastalski, Thomas
El Magraoui, Fouzi
Platta, Harald W.
author_facet Boutouja, Fahd
Brinkmeier, Rebecca
Mastalski, Thomas
El Magraoui, Fouzi
Platta, Harald W.
author_sort Boutouja, Fahd
collection PubMed
description Autophagy contributes to cellular homeostasis through the degradation of various intracellular targets such as proteins, organelles and microbes. This relates autophagy to various diseases such as infections, neurodegenerative diseases and cancer. A central component of the autophagy machinery is the class III phosphatidylinositol 3-kinase (PI3K-III) complex, which generates the signaling lipid phosphatidylinositol 3-phosphate (PtdIns3P). The catalytic subunit of this complex is the lipid-kinase VPS34, which associates with the membrane-targeting factor VPS15 as well as the multivalent adaptor protein BECLIN 1. A growing list of regulatory proteins binds to BECLIN 1 and modulates the activity of the PI3K-III complex. Here we discuss the regulation of BECLIN 1 by several different types of ubiquitination, resulting in distinct polyubiquitin chain linkages catalyzed by a set of E3 ligases. This contribution is part of the Special Issue “Ubiquitin System”.
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spelling pubmed-57511442018-01-08 Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades Boutouja, Fahd Brinkmeier, Rebecca Mastalski, Thomas El Magraoui, Fouzi Platta, Harald W. Int J Mol Sci Review Autophagy contributes to cellular homeostasis through the degradation of various intracellular targets such as proteins, organelles and microbes. This relates autophagy to various diseases such as infections, neurodegenerative diseases and cancer. A central component of the autophagy machinery is the class III phosphatidylinositol 3-kinase (PI3K-III) complex, which generates the signaling lipid phosphatidylinositol 3-phosphate (PtdIns3P). The catalytic subunit of this complex is the lipid-kinase VPS34, which associates with the membrane-targeting factor VPS15 as well as the multivalent adaptor protein BECLIN 1. A growing list of regulatory proteins binds to BECLIN 1 and modulates the activity of the PI3K-III complex. Here we discuss the regulation of BECLIN 1 by several different types of ubiquitination, resulting in distinct polyubiquitin chain linkages catalyzed by a set of E3 ligases. This contribution is part of the Special Issue “Ubiquitin System”. MDPI 2017-11-27 /pmc/articles/PMC5751144/ /pubmed/29186924 http://dx.doi.org/10.3390/ijms18122541 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
Boutouja, Fahd
Brinkmeier, Rebecca
Mastalski, Thomas
El Magraoui, Fouzi
Platta, Harald W.
Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades
title Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades
title_full Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades
title_fullStr Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades
title_full_unstemmed Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades
title_short Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades
title_sort regulation of the tumor-suppressor beclin 1 by distinct ubiquitination cascades
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5751144/
https://www.ncbi.nlm.nih.gov/pubmed/29186924
http://dx.doi.org/10.3390/ijms18122541
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