Dataset Information

The major lysine residues of PD-L1 ubiquitinated by ARIH1

ABSTRACT: To figure out the major lysine residues of PD-L1 ubiquitinated by ARIH1, mass spectrometry was utilized to identify the ubiquitination site. K271 was identified as the major residues of ubiquitination

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Lin Gao

LAB HEAD: Zan Chen

PROVIDER: PXD063222 | Pride | 2025-08-25

REPOSITORIES: Pride

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Publications

Biochemical analysis of PD-L1 ubiquitination by CRL3SPOP, ARIH1, and NEDD4 family ubiquitin ligases.

Xie Guojiao G Gao Lin L Lu Renee R Tian Linxia L Zheng Tiantian T Li Xinning X Dang Yongjun Y Cole Philip A PA Yu Xian X Jiang Hanjie H Chen Zan Z

Structure (London, England : 1993) 20250604 8

As a key immune checkpoint ligand, PD-L1 is a critical target in cancer immunotherapy. While multiple E3 ubiquitin ligases including CRL3SPOP, ARIH1, and NEDD4 have been implicated in PD-L1 degradation, the precise enzymatic mechanisms remain unclear. In this study, we systematically compared the enzymatic activities of CRL3SPOP, ARIH1, and NEDD4 ligases toward the cytoplasmic domain of PD-L1 through in vitro reconstitution with purified components. ARIH1, rather than CRL3< ...[more]

PMID: 40472843

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Project description:Progression through neuronal loss of substantia nigra pars compacta with Parkinson’s disease depends on various protein post-translational modifications mainly comprising phosphorylation, ubiquitination, acetylation, and methylation. Phosphorylation and ubiquitination regulate major physiological changes and cellular signaling pathways during dopaminergic neuronal death. Phosphorylation and ubiquitination dyshomeostasis of substantia nigra pars compacta tissue occurs earlier than movement symptom appearance. Although many phosphorylation and ubiquitination sites have been identified through site-specific methods, systematic quantitative proteomic analysis of pre-symptomatic Parkinson’s disease remains unexplored. Using quantitative proteomics, we have globally profiled ubiquitination and phosphorylation in substantia nigra pars compacta tissue of a Parkinson’s disease transgenic mouse model (A30P*A53T α-synuclein, hm2α-SYN-39 mouse strain) at pre-symptomatic stage; Our datasets of 5,351 phosphorylation sites in 2,136 proteins and 3,971 ubiquitination sites in 1,595 proteins provide valuable insight into pre-symptomatic Parkinson’s disease. After in-depth analysis of the relationship between phosphorylation and ubiquitination sites, we concluded that correlation of the relationship increased with decreasing distance. Subsequent bioinformatic analyses, including gene ontology annotation, domain annotation, subcellular localization, KEGG pathway annotation, functional cluster analysis, and motif analysis were performed to annotate quantifiable targets of phosphorylation and ubiquitination sites. Individual simultaneous phosphorylation and ubiquitination proteins that were differentially quantified were screened. The endocytosis pathway is likely regulated by both phosphorylation and ubiquitination at the molecular protein Epn2 (S439 and K135) in early-stage Parkinson’s disease. Therefore, this elucidation of the dysregulation of phosphorylation and ubiquitination has implications for understanding the pathophysiological mechanism of dopaminergic neuron degeneration and for developing novel therapeutics for Parkinson’s disease.

			Action	DRS
	F020666.dat	Other
	F020666.noredundant.fasta	Fasta
	F020668.dat	Other
	F020668.noredundant.fasta	Fasta
	YAS202405100002_1_SD.mgf	Mgf

Dataset Information

The major lysine residues of PD-L1 ubiquitinated by ARIH1

Dataset's files

Publications

Biochemical analysis of PD-L1 ubiquitination by CRL3<sup>SPOP</sup>, ARIH1, and NEDD4 family ubiquitin ligases.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

The major lysine residues of PD-L1 ubiquitinated by ARIH1

Dataset's files

Publications

Biochemical analysis of PD-L1 ubiquitination by CRL3&lt;sup&gt;SPOP&lt;/sup&gt;, ARIH1, and NEDD4 family ubiquitin ligases.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Biochemical analysis of PD-L1 ubiquitination by CRL3<sup>SPOP</sup>, ARIH1, and NEDD4 family ubiquitin ligases.