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Profiling of activated RBR E3 ligases using E2V derived activity-based probes

ABSTRACT: Structure-based E2 enzyme variants (E2Vs) were used to create biotinylated activity-based probes use as handles for affinity purification-mass spectrometry to identify interacting E3s.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Gisele Andree

LAB HEAD: Brenda Schulman

PROVIDER: PXD068594 | Pride | 2026-01-05

REPOSITORIES: Pride

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			Action	DRS
	E2V_combinedRawData.zip	Other
	E2V_pg_matrix_filesFromDIANN.zip	Other
	checksum.txt	Txt

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Publications

E2 variants for probing E3 ubiquitin ligase activities.

Du Jiale J Andree Gisele A GA Horn-Ghetko Daniel D Stier Luca L Singh Jaspal J Kostrhon Sebastian S Kiss Leo L Mann Matthias M Sidhu Sachdev S SS Schulman Brenda A BA

Proceedings of the National Academy of Sciences of the United States of America 20260102 1

E3 ligases partner with E2 enzymes to regulate vast eukaryotic biology. The hierarchical nature of these pairings, with >600 E3s and ~40 E2s in humans, necessitates that E2s cofunction with numerous different E3s. Here, focusing on E3s in the RING-between-RING (RBR) family and their partner UBE2L3 and UBE2D-family E2s, we report an approach to interrogate selected pathways. We screened phage-displayed libraries of structure-based E2 variants (E2Vs) to discover enzymes with enhanced affinity and ...[more]

PMID: 41481455

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