Activation of Atg1 kinase in autophagy by regulated phosphorylation

作者: Monika Kijanska , Ilse Dohnal , Wolfgang Reiter , Susanne Kaspar , Ingrid Stoffel

DOI: 10.4161/AUTO.6.8.13849

关键词: MAP2K7AutophagyCell biologyProtein kinase domainKinasePhosphorylation cascadeBiologyAutophagy-related protein 13BiochemistryPhosphorylationAtg1

摘要: Autophagy is a highly regulated trafficking pathway that leads to selective degradation of cellular constituents such as protein aggregates and excessive damaged organelles. Atg1 an essential part the core autophagic machinery, which triggers induction autophagy Cvt pathway. Although changes in phosphorylation complex formation are thought regulate its function, mechanism kinase activation remains unclear. Using quantitative mass spectrometry approach, we identified 29 sites, five either upregulated or downregulated by rapamycin treatment. Two threonine 226 serine 230, evolutionarily conserved located loop amino terminal domain Atg1. These events not required for localization phagosome assembly site (PAS), proper multisubunit binding activator Atg13. However, mutation either...

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