【摘 要】
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During autophagic process, autophagosomes carrying cellular cargoes fuse with lysosomes for degradation of damaged proteins and organelles.However, the molecula
【机 构】
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KeyLaboratoryofCarcinogenesisandTranslationalResearch(MinistryofEducation),DepartmentofBiochemistrya
【出 处】
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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
During autophagic process, autophagosomes carrying cellular cargoes fuse with lysosomes for degradation of damaged proteins and organelles.However, the molecular mechanism underlying autophagosome maturation is largely unknown.Here we report that WD domain and FYVE domain containing protein 2 (WDFY2), an early endosome protein, exhibited an inhibitory effect on autophagosome-lysosome fusion.Endogenous WDFY2 served as a signaling platform to recruit arginine methyltransferase PRMT5, by which in turn methylated Vps34.Methylation of Vps34 was required for its interaction with Rubicon, and leading to inhibition of autophagosomes maturation.Furthermore, MEF from WDFY2 knockout mice showed an acceleration of autophagic flux, which was well associated with cellular senescence.Our data reveal that WDFY2 is a negative regulator of autophagy by mediating a series of interactions among PRMT5, Vps34 and Rubicon.
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