Proteomics

Dataset Information

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LAMTOR1 interactome upon mutation of USP32

ABSTRACT: Ubiquitination is among the most prevalent post-translational modifications regulating a great number of cellular functions, and defects in such processes contribute to many diseases. Deubiquitinating enzymes (DUBs) are essential to control the precise outcome of ubiquitin signals. The ubiquitin-specific protease 32 (USP32) differs from all other DUBs as it comprises in addition to its catalytic USP domain and the DUSP domain also multiple EF hands and a C-terminal prenylation site. This dataset represents an interactome analysis of GFP-tagged LAMTOR1 in human RPE-1 cells upon knock-out and inactivation (C743S) of USP32.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: Georg Tascher  

LAB HEAD: Anja Bremm

PROVIDER: PXD035974 | Pride | 2023-01-16

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
20220623_HF_LC1_GT_AKA_LAMTOR1_CTRL_1.raw Raw
20220623_HF_LC1_GT_AKA_LAMTOR1_CTRL_2.raw Raw
20220623_HF_LC1_GT_AKA_LAMTOR1_CTRL_3.raw Raw
20220623_HF_LC1_GT_AKA_LAMTOR1_USP32_C743S_1.raw Raw
20220623_HF_LC1_GT_AKA_LAMTOR1_USP32_C743S_2.raw Raw
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Publications

USP32-regulated LAMTOR1 ubiquitination impacts mTORC1 activation and autophagy induction.

Hertel Alexandra A   Alves Ludovico Martins LM   Dutz Henrik H   Tascher Georg G   Bonn Florian F   Kaulich Manuel M   Dikic Ivan I   Eimer Stefan S   Steinberg Florian F   Bremm Anja A  

Cell reports 20221201 10

The endosomal-lysosomal system is a series of organelles in the endocytic pathway that executes trafficking and degradation of proteins and lipids and mediates the internalization of nutrients and growth factors to ensure cell survival, growth, and differentiation. Here, we reveal regulatory, non-proteolytic ubiquitin signals in this complex system that are controlled by the enigmatic deubiquitinase USP32. Knockout (KO) of USP32 in primary hTERT-RPE1 cells results among others in hyperubiquitina  ...[more]

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