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Proximity-dependent biotinylation reveals an interaction between ubiquitin-specific peptidase 46 and centrosome-related proteins

ABSTRACT: To characterize the protein interaction network of USP46, BioID analysis was conducted on a knock-in cell line that expresses USP46 and biotin ligase fusion protein stably.

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Kazuya Murata

PROVIDER: PXD053674 | JPOST Repository | Tue Mar 25 00:00:00 GMT 2025

REPOSITORIES: jPOST

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Proximity-dependent biotinylation reveals an interaction between ubiquitin-specific peptidase 46 and centrosome-related proteins.

Yoshioka Kazuma K Nakagawa Reiko R Nguyen Chi Lieu Kim CLK Suzuki Hayate H Ishigaki Kiyohiro K Mizuno Seiya S Okiyoneda Tsukasa T Ebihara Shizufumi S Murata Kazuya K

FEBS open bio 20241031 1

Protein ubiquitination extensively modulates protein functions and controls various biological processes, such as protein degradation, signal transduction, transcription, and DNA repair. Ubiquitination is a reversible post-translational modification, and deubiquitinating enzymes cleave ubiquitin from proteins. Ubiquitin-specific peptidase 46 (USP46), a deubiquitinase, is highly expressed in the brain and regulates neural functions. Deleting lysine 92 (ΔK92) in USP46 reduces murine depression-lik ...[more]

PMID: 39482856

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