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Quantitative proteomics of AMBRA1

ABSTRACT: We sought to identify AMBRA1 interacting proteins and to profile its loss/gain of interactions by mutation using quantitative mass spectrometry.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Disease Free

SUBMITTER: Si-Han Chen

LAB HEAD: Nevan Krogan

PROVIDER: PXD008005 | Pride | 2018-07-11

REPOSITORIES: Pride

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CRL4AMBRA1 targets Elongin C for ubiquitination and degradation to modulate CRL5 signaling.

Chen Si-Han SH Jang Gwendolyn M GM Hüttenhain Ruth R Gordon David E DE Du Dan D Newton Billy W BW Johnson Jeffrey R JR Hiatt Joseph J Hultquist Judd F JF Johnson Tasha L TL Liu Yi-Liang YL Burton Lily A LA Ye Jordan J Reichermeier Kurt M KM Stroud Robert M RM Marson Alexander A Debnath Jayanta J Gross John D JD Krogan Nevan J NJ

The EMBO journal 20180830 18

Multi-subunit cullin-RING ligases (CRLs) are the largest family of ubiquitin E3 ligases in humans. CRL activity is tightly regulated to prevent unintended substrate degradation or autocatalytic degradation of CRL subunits. Using a proteomics strategy, we discovered that CRL4AMBRA1 (CRL substrate receptor denoted in superscript) targets Elongin C (ELOC), the essential adapter protein of CRL5 complexes, for polyubiquitination and degradation. We showed that the ubiquitin liga ...[more]

PMID: 30166453

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