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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 |
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