Olivia Newton-John Cancer Research Institute, Heidelberg, VIC 3084, Australia.
School of Cancer Medicine, La Trobe University, Bundoora, VIC 3086, Australia.
Cells. 2021 Jun 17;10(6):1522. doi: 10.3390/cells10061522.
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.
BECLIN1 是自噬的一个重要调控因子,是哺乳动物生存所必需的过程。它与其他蛋白质一起形成 III 类磷酸肌醇 3-激酶(PI3K)复合物,以生成磷酸化磷脂酰肌醇(PtdIns),这对于自噬和其他膜运输过程都是必不可少的。多年来,研究已经阐明了 BECLIN1 的结构、生物物理和生化特性,这些特性揭示了该蛋白如何通过变构调节自噬和膜运输等关键过程。在这里,我们回顾这些发现以及 BECLIN1 的多样化蛋白质相互作用组如何对其进行调节,以及它对生物体生理学的影响。