Dataset Information

Global and diGLY enriched proteomes of RanBPM depleted HeLa cells and RanBPM APMS

ABSTRACT: The human CTLH complex is a newly discovered multi-subunit E3 ligase. At present, only a few of its ubiquitination targets are known. Here, we use proteomic techniques in RanBPM-depleted HeLa cells to identify ubiquitination substrates of the CTLH complex. First, global proteomics determined proteins that were significantly increased in cells depleted of RanBPM. This analysis revealed potential degradation-induced ubiquitination substrates of the complex. Ubiquitination differences using diGLY-enriched proteomics in shRanBPM cells compared with the endogenous RanBPM interactome also revealed candidate ubiquitination targets.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hela Cell

SUBMITTER: Matthew Maitland

LAB HEAD: Caroline Schild-Poulter

PROVIDER: PXD024872 | Pride | 2021-08-13

REPOSITORIES: Pride

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Publications

Proteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex-dependent regulation of glycolysis.

Maitland Matthew E R MER Kuljanin Miljan M Wang Xu X Lajoie Gilles A GA Schild-Poulter Caroline C

FASEB journal : official publication of the Federation of American Societies for Experimental Biology 20210901 9

Ubiquitination is an essential post-translational modification that regulates protein stability or function. Its substrate specificity is dictated by various E3 ligases. The human C-terminal to LisH (CTLH) complex is a newly discovered multi-subunit really interesting new gene (RING) E3 ligase with only a few known ubiquitination targets. Here, we used mass spectrometry-based proteomic techniques to gain insight into CTLH complex function and ubiquitination substrates in HeLa cells. First, globa ...[more]

PMID: 34383978

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			Action	DRS
	APMS_evidence.txt	Txt
	APMS_parameters.txt	Txt
	APMS_proteinGroups.txt	Txt
	APMS_summary.txt	Txt
	RanBPMdiGLY_GlyGly__K_Sites.txt	Txt