Proteomics

Dataset Information

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Proteome Composition of Lysosomes and Autophagosomes after Proteasome Inhibition


ABSTRACT: Lysosomes are a major site of intracellular acidic hydrolase-mediated proteolysis and cellular degradation in a membrane-enclosed organelle. Alternatively, soluble, ubiquitin-bound proteins are degraded via the proteasome, a megadalton protein complex within the cytoplasm. The interplay between both degradation pathways has been of increasing interest in recent years. To determine the effects of proteasome inhibition on the lysosomal compartment, we investigated enriched lysosomal fractions, autophagosomal fractions and immunoprecipitated proteasomes from HEK293 cells after proteasome inibition by MG132 or bortezomib in comparison to the respective fractions from control cells.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Fibroblast

SUBMITTER: Melanie Thelen  

LAB HEAD: Volkmar Gieselmann

PROVIDER: PXD015243 | Pride | 2020-04-20

REPOSITORIES: Pride

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Publications

Proteaphagy in Mammalian Cells Can Function Independent of ATG5/ATG7.

Goebel Tatjana T   Mausbach Simone S   Tuermer Andreas A   Eltahir Heba H   Winter Dominic D   Gieselmann Volkmar V   Thelen Melanie M  

Molecular & cellular proteomics : MCP 20200416 7


The degradation of intra- and extracellular proteins is essential in all cell types and mediated by two systems, the ubiquitin-proteasome system (UPS) and the autophagy-lysosome pathway. This study investigates the changes in autophagosomal and lysosomal proteomes upon inhibition of proteasomes by bortezomib (BTZ) or MG132. We find an increased abundance of more than 50 proteins in lysosomes of cells in which the proteasome is inhibited. Among those are dihydrofolate reductase (DHFR), β-Catenin  ...[more]

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