Dataset Information

USP32 regulates non-proteolytic LAMTOR1 ubiquitination and Ragulator function

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 unique domain architecture offers various features for the regulation of specific signaling processes by USP32. To better understand the cellular function of USP32, we performed SILAC-based quantitative ubiquitinome analyses to determine potential USP32 substrates. We found proteins involved in endosomal trafficking as well as lysosomal proteins with regulated diGly sites in USP32 knockout (KO) cells.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Florian Bonn

LAB HEAD: Anja Bremm

PROVIDER: PXD024211 | Pride | 2022-12-16

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20180319_FB_AlexK_GGIP_1_12.raw	Raw
	20180319_FB_AlexK_GGIP_1_5.raw	Raw
	20180319_FB_AlexK_GGIP_1_6.raw	Raw
	20180319_FB_AlexK_GGIP_1_7.raw	Raw
	20180319_FB_AlexK_GGIP_1_85.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]

PMID: 36476874

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