Proteomics

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Identification of Mono-ADP-Ribose Readers Using Well-Defined Photoaffinity-based Probes

ABSTRACT: In this study, well-defined photoaffinity-based monoADPr probes (biotin-linked) were synthesized and used to study direct interactors of monoADPr. Either a benzophenone or diazirine group was incorporated to assess their performance in enriching for known mnonoADPr readers. To ensure only monoADPr readers were enriched and not proteins interacting with the linker and/or photocrosslinker, control probes were synthesized containing all but the monoADPr moiety.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cervical Carcinoma Cell, Cell Culture

SUBMITTER: Suzanne Weijers  

LAB HEAD: Michiel Vermeulen

PROVIDER: PXD065574 | Pride | 2025-12-15

REPOSITORIES: Pride

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20250312_Astral_AUR325075C18TS_DIA_30SPD_SW_V136_strep_IP_LB_1.raw Raw
20250312_Astral_AUR325075C18TS_DIA_30SPD_SW_V136_strep_IP_LB_2.raw Raw
20250312_Astral_AUR325075C18TS_DIA_30SPD_SW_V136_strep_IP_LB_3.raw Raw
20250312_Astral_AUR325075C18TS_DIA_30SPD_SW_V136_strep_IP_LD_1.raw Raw
20250312_Astral_AUR325075C18TS_DIA_30SPD_SW_V136_strep_IP_LD_2.raw Raw
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Identification of mono-ADP-ribose readers using well-defined photoaffinity-based probes.

van der Heijden Femke L A M FLAM   Weijers Suzanne A SA   Kondyli Spyridoula S   Bleijerveld Onno O   Vermeulen Michiel M   Filippov Dmitri V DV  

RSC chemical biology 20251128

Adenosine diphosphate ribosylation is a significant post-translational modification implicated in various cellular processes and diseases, yet identifying its mono-ADP-ribose readers has posed considerable challenges. Previous proteomic screenings have predominantly focused on poly-ADP-ribose, resulting in the oversight of mono-ADP-ribose readers due to undefined ADP-ribose structures with randomly placed photo-crosslinking moieties. This study introduces novel, well-defined mono-ADP-ribose phot  ...[more]

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