title: Structure and function of the ULK1 complex in autophagy.
abstract: The ULK1 complex initiates autophagosome formation, linking cellular nutrient status to downstream events in autophagy. Recent work suggests that the ULK1 complex might also be activated in selective autophagy independent of nutrient or energy status. In this review we will discuss our current understanding of how the ULK1 complex is regulated by different signals, as well as how this complex then regulates other components of the autophagy machinery. Recently obtained structural data both on ULK1 and the orthologous yeast Atg1 complex are beginning to shed light on the higher-order organization of ULK1 complex. Ultimately, these insights might make it possible to understand how cargo organization and structure recruits and regulates ULK1 in selective autophagy initiation.
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, United States; California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, United States.
authors.forename: Mary G
authors.initials: MG
authors.lastname: Lin
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, United States; California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, United States; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, United States. Electronic address: jimhurley@berkeley.edu.
authors.forename: James H
authors.initials: JH
authors.lastname: Hurley
mesh_terms: D000818:Animals; D001343:Autophagy; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism*; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; D017346:Protein Serine-Threonine Kinases