1170366_Tran,S_2021.pdf (1.54 MB)
BECLIN1: Protein Structure, Function and Regulation
journal contribution
posted on 2021-07-22, 05:03 authored by Sharon TranSharon Tran, Walter FairlieWalter Fairlie, Erinna LeeErinna LeeBECLIN1 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.
Funding
E.F.L. is a recipient of fellowships from the Australian Research Council (Future Fellowship FT150100212) and the Victorian Cancer Agency (Mid-Career Fellowship MCRF19045). S.T. is a recipient of a La Trobe University Graduate Research Scholarship/Research Training Program Scholarship.
History
Publication Date
2021-06-01Journal
CELLSVolume
10Issue
6Article Number
ARTN 1522Pagination
16p.Publisher
MDPIISSN
2073-4409Rights Statement
The Author reserves all moral rights over the deposited text and must be credited if any re-use occurs. Documents deposited in OPAL are the Open Access versions of outputs published elsewhere. Changes resulting from the publishing process may therefore not be reflected in this document. The final published version may be obtained via the publisher’s DOI. Please note that additional copyright and access restrictions may apply to the published version.Publisher DOI
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