Proteomics

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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. A SILAC-based proteomic analysis of purified lysosomes revealed an increase in lysosomal hydrolases in organelles isolated from USP32 KO cells as compared to WT cells, suggesting that hydrolases are not sorted correctly to their destination in the absence of USP32.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Florian Bonn  

LAB HEAD: Anja Bremm

PROVIDER: PXD024227 | Pride | 2022-12-16

REPOSITORIES: pride

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201705017_MH_AlexK_Lysosomen_1_1.raw Raw
201705017_MH_AlexK_Lysosomen_1_2.raw Raw
201705017_MH_AlexK_Lysosomen_1_3.raw Raw
201705017_MH_AlexK_Lysosomen_1_4.raw Raw
201705017_MH_AlexK_Lysosomen_1_5.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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