【摘 要】
：
The first distinguishable autophagy-specific membranous structure, the omegasome, forms when the autophagy-specific VPS34 complex (VPS34, BECN1/ATG6, ATG14
【机 构】
：
InstitutoLeloir,BuenosAires(1405),Argentina
【出 处】
：
The 7th International Symposium on Autophagy 2015(第七届自噬国际研讨会
论文部分内容阅读
The first distinguishable autophagy-specific membranous structure, the omegasome, forms when the autophagy-specific VPS34 complex (VPS34, BECN1/ATG6, ATG14 and VPS15)mediates local deposition of phospatidylinositol-3-phospate (PI3P) in a specific domain of the ER that interfaces with mitochondria.The molecules and mechanisms that mediate the assembly and localization of this complex remain however poorly defined.We found that the transmembrane domain-containing immunophilin FKBP38 and its Drosophila orthologue Zonda play a critical role at early stages of autophagy.Zonda operates downstream to ATG1 and is required for autophagy-specific VPS34 activation.Zonda displays a reticular distribution under basal conditions, and soon after starvation nucleates in foci associated with the ER that later form the omegasome.Zonda colocalizes first with ATG5 and ATG8, and later with Lamp1,indicating that it is also a component of phagophores, autophagosomes and autophagolysosomes.Consistent with a role of FKBP38/Zonda at early stages of autophagy,FKBP38 forms a complex with BECN1 and colocalizes with ATG14 and BECN1.Thus,FKBP38/Zonda is a novel component of the autophagy cascade essential for activation of the VSP34 complex.
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