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C-terminal amides mark proteins for degradation via SCF/FBXO31 – Expression Proteomics

ABSTRACT: FBXO31 is a substrate adapter for the SCF-type ubiquitin ligase complex SCF/FBXO31 which ubiquitylates C-terminal amide-bearing proteins (CTAPs), thereby triggering their proteasomal degradation in human cells. FBXO31(D334N) is a dominant de novo mutation found among patients with cerebral palsy. To identify proteins affected by FBXO31(D334N) expression, we engineered HEK293T cells to carry a FBXO31 knockout and rapidly inducible FBXO31 expression using the Shield-1 degron system. WT or D334N variants of FBXO31 were induced for 12h and proteomic changes captured by whole cell proteomics using TMT-based quantification. Deposited files include raw MS spectra, protein-, peptide- and psm-level identification results, and differential gene expression results.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Matthias Muhar

LAB HEAD: Prof. Jacob Corn

PROVIDER: PXD055818 | Pride | 2024-11-05

REPOSITORIES: Pride

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			Action	DRS
	20220818_C29220_002_S408177_TMT9plex_pool_f1_A.raw	Raw
	20220818_C29220_003_S408178_TMT9plex_pool_f2_A.raw	Raw
	20220818_C29220_004_S408179_TMT9plex_pool_f3_A.raw	Raw
	20220818_C29220_005_S408180_TMT9plex_pool_f4_A.raw	Raw
	20220818_C29220_006_S408181_TMT9plex_pool_f5_A.raw	Raw

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Project description:E3 ubiquitin ligases mediate the last step of the ubiquitination pathwayin the ubiquitin-proteasome system (UPS). By targeting transcriptional regulators for their turnover, E3s play a crucial role in every aspect of plant biology. In plants, SKP1/CULLIN1/F-BOX PROTEIN (SCF)-type E3 ubiquitin ligases are essential for the perception and signaling of several key hormones including auxins and jasmonates (JAs). F-box proteins, TRANSPORT INHIBITOR RESPONSE 1 (TIR1) and CORONATINE INSENSITIVE 1 (COI1) bind directly transcriptional repressors AUX/IAAs and JAZs in an auxin- and JAs-depending manner, respectively, which permits the perception of the hormones and transcriptional activation of signaling pathways. Redox modification of proteins mainly by S-nitrosation of cysteines via nitric oxide (NO) has emerged as a valued regulatory mechanism in physiological processes requiring its rapid and versatile integration. Previously, we demonstrated that TIR1 and ASK1 (Arabidopsis thaliana SKP1) are targets of S-nitrosation, and these (NO)-dependent post-translational modifications enhance protein-protein interactions, and positively regulate SCFTIR1 complex assembly and expression of auxin response genes. In this work, we provide evidence on the modulation of SCFCOI1 complex by different S-nitrosation events. We demonstrated that S-nitrosation of ASK1 Cys118 enhanced ASK1-COI1 protein-protein interaction. Overexpression of non-nitrosable ask1 mutant protein impaired the activation of JA-responsive genes mediated by SCFCOI1 illustrating the functional relevance of this redox-mediated regulation in planta. Additionally, in silico analysis positioned COI1 as a promising S-nitrosation target. The regulation of SCF components involved in hormonal perception by S- nitrosation may represent a key strategy to determine the precise time and site-dependent activation of each hormonal signaling pathway, and highlights NO as a pivotal molecular player in these scenarios.

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C-terminal amides mark proteins for degradation via SCF/FBXO31 – Expression Proteomics

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