Phosphorylation of Vps34 by Atg1 is required for autophagy

来源 :The 7th International Symposium on Autophagy 2015(第七届自噬国际研讨会 | 被引量 : 0次 | 上传用户:Alkaid
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  The budding yeast has only one class Ⅲ PI3-kinase, Vps34, which specifically phosphorylates position-3 of phosphatidylinositol.The product, phosphatidylinositol 3-phosphate (PI3P), is essential not only for autophagosome formation but also for the vacuolar protein sorting (VPS)pathway in yeast.To function in these two processes, Vps34 forms distinct complexes: PI3-kinase complex Ⅰ (Vps34, Vps15, Vps30/Atg6, Atg14 and Atg38), which functions in autophagy,and PI3-kinase complex Ⅱ (Vps34, Vps15, Vps30/Atg6, and Vps38), which is involved in the VPS pathway.The highly specific nature of these complexes is determined by the presence of the unique proteins Atg14 and Atg38, and Vps38, which associate exclusively with complex Ⅰ or Ⅱ, respectively.In spite of these fundamental roles played by PI3-kinase complexes in the cell, little is known about how these complexes exert their characteristic functional specificity and their regulation.
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