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Reading ADP-ribosylation signalling using chemical biology and interaction proteomics

ABSTRACT: In this project, we describe a global, proteome-wide screening for ADP-ribosylation interactome. Our data reveals novel MAR and PAR readers. We identify both cell type-dependent and independent ADPr interactors. In addition, we quantify apparent binding affinities of large number of ADPr readers. We also identify proteins, whose interaction with ADPr modifications is regulated upon DNA damage induction.

INSTRUMENT(S): Orbitrap Fusion, Orbitrap Exploris 480, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Keratinocyte, Epithelial Cell Of Cervix

DISEASE(S): Cervix Carcinoma

SUBMITTER: Pascal Jansen

LAB HEAD: Prof. Michiel Vermeulen

PROVIDER: PXD024233 | Pride | 2021-11-02

REPOSITORIES: Pride

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			Action	DRS
	20191101_Fusion1_SA_KK_ADPrPD_19_1x_1.raw	Raw
	20191101_Fusion1_SA_KK_ADPrPD_20_1x_2.raw	Raw
	20191101_Fusion1_SA_KK_ADPrPD_21_1x_3.raw	Raw
	20191101_Fusion1_SA_KK_ADPrPD_22_2x_1.raw	Raw
	20191101_Fusion1_SA_KK_ADPrPD_23_2x_2.raw	Raw

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Reading ADP-ribosylation signaling using chemical biology and interaction proteomics.

Kliza Katarzyna W KW Liu Qiang Q Roosenboom Laura W M LWM Jansen Pascal W T C PWTC Filippov Dmitri V DV Vermeulen Michiel M

Molecular cell 20210921 21

ADP-ribose (ADPr) readers are essential components of ADP-ribosylation signaling, which regulates genome maintenance and immunity. The identification and discrimination between monoADPr (MAR) and polyADPr (PAR) readers is difficult because of a lack of suitable affinity-enrichment reagents. We synthesized well-defined ADPr probes and used these for affinity purifications combined with relative and absolute quantitative mass spectrometry to generate proteome-wide MAR and PAR interactomes, includi ...[more]

PMID: 34551281

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