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Mol Cell. 2014 Feb 6;53(3):471-83. doi: 10.1016/j.molcel.2013.12.011. Epub 2014 Jan 16.

Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase.

Author information

Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria.
Department of Biology, Institute of Molecular Systems Biology, ETH Zürich, Wolfgang Pauli Strasse 16, 8093 Zürich, Switzerland.
Institute of Biochemistry, Department of Biology, ETH Zürich, Schafmattstrasse 18, 8093 Zürich, Switzerland.
Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA.
Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria. Electronic address:

Erratum in

  • Mol Cell. 2014 Feb 6;53(3):515.


Bulk degradation of cytoplasmic material is mediated by a highly conserved intracellular trafficking pathway termed autophagy. This pathway is characterized by the formation of double-membrane vesicles termed autophagosomes engulfing the substrate and transporting it to the vacuole/lysosome for breakdown and recycling. The Atg1/ULK1 kinase is essential for this process; however, little is known about its targets and the means by which it controls autophagy. Here we have screened for Atg1 kinase substrates using consensus peptide arrays and identified three components of the autophagy machinery. The multimembrane-spanning protein Atg9 is a direct target of this kinase essential for autophagy. Phosphorylated Atg9 is then required for the efficient recruitment of Atg8 and Atg18 to the site of autophagosome formation and subsequent expansion of the isolation membrane, a prerequisite for a functioning autophagy pathway. These findings show that the Atg1 kinase acts early in autophagy by regulating the outgrowth of autophagosomal membranes.

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