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BECLIN1: Protein Structure, Function and Regulation

BECLIN1 is a well-established regulator of autophagy, a process essential for mammalian survival. It functions in conjunction with other proteins to form Class III Phosphoinositide 3-Kinase (PI3K) complexes to generate phosphorylated phosphatidylinositol (PtdIns), lipids essential for not only autop...

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Detalles Bibliográficos
Autores principales: Tran, Sharon, Fairlie, W. Douglas, Lee, Erinna F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8235419/
https://www.ncbi.nlm.nih.gov/pubmed/34204202
http://dx.doi.org/10.3390/cells10061522
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author Tran, Sharon
Fairlie, W. Douglas
Lee, Erinna F.
author_facet Tran, Sharon
Fairlie, W. Douglas
Lee, Erinna F.
author_sort Tran, Sharon
collection PubMed
description BECLIN1 is a well-established regulator of autophagy, a process essential for mammalian survival. It functions in conjunction with other proteins to form Class III Phosphoinositide 3-Kinase (PI3K) complexes to generate phosphorylated phosphatidylinositol (PtdIns), lipids essential for not only autophagy but other membrane trafficking processes. Over the years, studies have elucidated the structural, biophysical, and biochemical properties of BECLIN1, which have shed light on how this protein functions to allosterically regulate these critical processes of autophagy and membrane trafficking. Here, we review these findings and how BECLIN1’s diverse protein interactome regulates it, as well as its impact on organismal physiology.
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spelling pubmed-82354192021-06-27 BECLIN1: Protein Structure, Function and Regulation Tran, Sharon Fairlie, W. Douglas Lee, Erinna F. Cells Review BECLIN1 is a well-established regulator of autophagy, a process essential for mammalian survival. It functions in conjunction with other proteins to form Class III Phosphoinositide 3-Kinase (PI3K) complexes to generate phosphorylated phosphatidylinositol (PtdIns), lipids essential for not only autophagy but other membrane trafficking processes. Over the years, studies have elucidated the structural, biophysical, and biochemical properties of BECLIN1, which have shed light on how this protein functions to allosterically regulate these critical processes of autophagy and membrane trafficking. Here, we review these findings and how BECLIN1’s diverse protein interactome regulates it, as well as its impact on organismal physiology. MDPI 2021-06-17 /pmc/articles/PMC8235419/ /pubmed/34204202 http://dx.doi.org/10.3390/cells10061522 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Tran, Sharon
Fairlie, W. Douglas
Lee, Erinna F.
BECLIN1: Protein Structure, Function and Regulation
title BECLIN1: Protein Structure, Function and Regulation
title_full BECLIN1: Protein Structure, Function and Regulation
title_fullStr BECLIN1: Protein Structure, Function and Regulation
title_full_unstemmed BECLIN1: Protein Structure, Function and Regulation
title_short BECLIN1: Protein Structure, Function and Regulation
title_sort beclin1: protein structure, function and regulation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8235419/
https://www.ncbi.nlm.nih.gov/pubmed/34204202
http://dx.doi.org/10.3390/cells10061522
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