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):

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