Proteomics

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ULK1 regulated phosphatases in mouse and human cells

ABSTRACT: In the project “ULK1 regulated phosphatases” by Zehan Hu, Devanarayanan Siva Sankar, Björn Stork and Jörn Dengjel two sets of bottom-up MS-based chemical proteomics experiments were performed in which phosphatase complexes were enriched based on their activity using microcystin-LR coupled sepharose beads. (1) Three biological replicates of MEFs (triple labeling) were performed comparing phosphatase activity (36 raw files labeled "2018"). ULK1 MEFs were compared DKO MEFs, both in rapamycin conditions. Empty beads were used as negative control (Ctrl). Following experiments were performed: (2) Three biological replicates of A549 cells (triple labeling) were performed comparing phosphatase activity (30 raw files labeled "A549"). A549 cells in fed conditions (DMEM) were compared to rapamycin treated cells (Rapa). Empty beads were used as negative control (Ctrl).

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Epithelial Cell, Fibroblast

SUBMITTER: Joern Dengjel  

LAB HEAD: Joern Dengjel

PROVIDER: PXD022383 | Pride | 2021-11-03

REPOSITORIES: Pride

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Publications

The evolutionarily conserved ULK1 kinase complex acts as gatekeeper of canonical autophagy and regulates induction of autophagosome biogenesis. To better understand control of ULK1 and analyze whether ULK1 has broader functions that are also linked to the later steps of autophagy, we perform comprehensive phosphoproteomic analyses. Combining in vivo with in vitro data, we identify numerous direct ULK1 target sites within autophagy-relevant proteins that are critical for autophagosome maturation  ...[more]