ULK1 targets Beclin-1 in autophagy

Volodymyr Y. Nazarko; Qing Zhong

doi:10.1038/ncb2797

ULK1 targets Beclin-1 in autophagy

Volodymyr Y. Nazarko, Qing Zhong

Research output: Contribution to journal › Article › peer-review

66 Scopus citations

Abstract

The substrates of mammalian ULK1/2 and its yeast homologue Atg1 in autophagy have remained elusive. The class III phosphatidylinositol 3-kinase component Beclin-1 has now been identified as a physiological substrate of the ULK kinases in autophagy following amino acid starvation, therefore suggesting a critical molecular link between the upstream kinases and the autophagy core machinery.

Original language	English (US)
Pages (from-to)	727-728
Number of pages	2
Journal	Nature cell biology
Volume	15
Issue number	7
DOIs	https://doi.org/10.1038/ncb2797
State	Published - Jul 2013

ASJC Scopus subject areas

Cell Biology

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title = "ULK1 targets Beclin-1 in autophagy",

abstract = "The substrates of mammalian ULK1/2 and its yeast homologue Atg1 in autophagy have remained elusive. The class III phosphatidylinositol 3-kinase component Beclin-1 has now been identified as a physiological substrate of the ULK kinases in autophagy following amino acid starvation, therefore suggesting a critical molecular link between the upstream kinases and the autophagy core machinery.",

author = "Nazarko, {Volodymyr Y.} and Qing Zhong",

year = "2013",

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AB - The substrates of mammalian ULK1/2 and its yeast homologue Atg1 in autophagy have remained elusive. The class III phosphatidylinositol 3-kinase component Beclin-1 has now been identified as a physiological substrate of the ULK kinases in autophagy following amino acid starvation, therefore suggesting a critical molecular link between the upstream kinases and the autophagy core machinery.

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ULK1 targets Beclin-1 in autophagy

Abstract

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