Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/26918
Title: BECLIN1: Protein Structure, Function and Regulation.
Austin Authors: Tran, Sharon;Fairlie, Walter Douglas ;Lee, Erinna F
Affiliation: La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia
Olivia Newton-John Cancer Research Institute
School of Cancer Medicine, La Trobe University, Bundoora, VIC 3086, Australia
Issue Date: 17-Jun-2021
Date: 2021-06-17
Publication information: Cells 2021; 10(6): 1522
Abstract: 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.
URI: https://ahro.austin.org.au/austinjspui/handle/1/26918
DOI: 10.3390/cells10061522
ORCID: 0000-0002-2498-1160
0000-0003-1255-9808
Journal: Cells
PubMed URL: 34204202
Type: Journal Article
Subjects: BCL-2
BECLIN1
PI3K Class III complexes
autophagy
Appears in Collections:Journal articles

Show full item record

Page view(s)

14
checked on Apr 20, 2024

Google ScholarTM

Check


Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.