Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/26918
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dc.contributor.authorTran, Sharon-
dc.contributor.authorFairlie, Walter Douglas-
dc.contributor.authorLee, Erinna F-
dc.date2021-06-17-
dc.date.accessioned2021-07-05T06:10:18Z-
dc.date.available2021-07-05T06:10:18Z-
dc.date.issued2021-06-17-
dc.identifier.citationCells 2021; 10(6): 1522en
dc.identifier.urihttps://ahro.austin.org.au/austinjspui/handle/1/26918-
dc.description.abstractBECLIN1 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.en
dc.language.isoeng
dc.subjectBCL-2en
dc.subjectBECLIN1en
dc.subjectPI3K Class III complexesen
dc.subjectautophagyen
dc.titleBECLIN1: Protein Structure, Function and Regulation.en
dc.typeJournal Articleen
dc.identifier.journaltitleCellsen
dc.identifier.affiliationLa Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australiaen
dc.identifier.affiliationOlivia Newton-John Cancer Research Instituteen
dc.identifier.affiliationSchool of Cancer Medicine, La Trobe University, Bundoora, VIC 3086, Australiaen
dc.identifier.doi10.3390/cells10061522en
dc.type.contentTexten
dc.identifier.orcid0000-0002-2498-1160en
dc.identifier.orcid0000-0003-1255-9808en
dc.identifier.pubmedid34204202
local.name.researcherFairlie, Walter Douglas
item.languageiso639-1en-
item.grantfulltextnone-
item.openairetypeJournal Article-
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.author.deptOlivia Newton-John Cancer Research Institute-
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