Publication . Article . 2016

Regulation of Autophagy By Signaling Through the Atg1/ULK1 Complex

Name: Regulation of Autophagy By Signaling Through the Atg1/ULK1 Complex
Keywords: Autophagy, Autophagy signaling, Atg1/ULK1 regulation, Atg1/ULK1 phosphorylation sites, Atg1/ULK1 substrates, Molecular Biology

Papinski, Daniel; Kraft, Claudine;

Open Access

English

Published: 01 May 2016 Journal: Journal of Molecular Biology, issue 9, pages 1,725-1,741 (issn: 00222836,

Publisher: The Authors. Published by Elsevier Ltd.

- Summary
- References
  (127)
- Related research
  (7)

Abstract

AbstractAutophagy is an intracellular degradation pathway highly conserved in eukaryotic species. It is characterized by selective or bulk trafficking of cytosolic structures—ranging from single proteins to cell organelles—to the vacuole or a lysosome, in which the autophagic cargo is degraded. Autophagy fulfils a large set of roles, including nutrient mobilization in starvation conditions, clearance of protein aggregates and host defence against intracellular pathogens. Not surprisingly, autophagy has been linked to several human diseases, among them neurodegenerative disorders and cancer. Autophagy is coordinated by the action of the Atg1/ULK1 kinase, which is the target of several important stress signaling cascades. In this review, we will discuss the available information on both upstream regulation and downstream effectors of Atg1/ULK1, with special focus on reported and proposed kinase substrates.

Subjects

Autophagy, Autophagy signaling, Atg1/ULK1 regulation, Atg1/ULK1 phosphorylation sites, Atg1/ULK1 substrates, Molecular Biology

Related Organizations

Max F. Perutz Laboratories
Austria
University of Vienna
Austria

127 references, page 1 of 13

[1] Z. Xie, D.J. Klionsky, Autophagosome formation: core machinery and adaptations, Nat. Cell Biol. 9 (10) (2007) 1102-1109.

[2] K. Suzuki, T. Kirisako, Y. Kamada, V. Montana, T. Noda, Y. Ohsumi, The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation, EMBO J. 20 (21) (2001) 5971-5981.

[3] K. Suzuki, Y. Kubota, T. Sekito, Y. Ohsumi, Hierarchy of Atg proteins in pre-autophagosomal structure organization, Genes Cells 12 (2) (2007) 209-218.

[4] K.R. Parzych, D.J. Klionsky, An overview of autophagy: morphology, mechanism, and regulation, Antioxid. Redox Signal. 20 (3) (2014) 460-473.

[5] Y. Kabeya, N. Mizushima, T. Ueno, A. Yamamoto, T. Kirisako, T. Noda, et al., LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing, EMBO J. 19 (21) (2000) 5720-5728.

[6] C. Kraft, F. Reggiori, M. Peter, Selective types of autophagy in yeast, Biochim. Biophys. Acta, Mol. Cell Res. 1793 (9) (2009) 1404-1412. [OpenAIRE]

[7] K. Takeshige, M. Baba, S. Tsuboi, T. Noda, Y. Ohsumi, Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction, J. Cell Biol. 119 (2) (1992) 301-311.

[8] M. Veenhuis, A. Douma, W. Harder, M. Osumi, Degradation and turnover of peroxisomes in the yeast Hansenula polymorpha induced by selective inactivation of peroxisomal enzymes, Arch. Microbiol. 134 (3) (1983) 193-203. [OpenAIRE]

[9] M. Hamasaki, T. Noda, M. Baba, Y. Ohsumi, Starvation triggers the delivery of the endoplasmic reticulum to the vacuole via autophagy in yeast, Traffic 6 (1) (2005) 56-65.

[10] C. Kraft, A. Deplazes, M. Sohrmann, M. Peter, Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease, Nat. Cell Biol. 10 (5) (2008) 602-610.