Cargando…
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...
Autores principales: | , , |
---|---|
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 |
_version_ | 1783714313464184832 |
---|---|
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. |
format | Online Article Text |
id | pubmed-8235419 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT transharon beclin1proteinstructurefunctionandregulation AT fairliewdouglas beclin1proteinstructurefunctionandregulation AT leeerinnaf beclin1proteinstructurefunctionandregulation |