Identification of proximal SUMO-dependent interactors using SUMO-ID.
Nat Commun
; 12(1): 6671, 2021 11 18.
Article
en En
| MEDLINE
| ID: mdl-34795231
ABSTRACT
The fast dynamics and reversibility of posttranslational modifications by the ubiquitin family pose significant challenges for research. Here we present SUMO-ID, a technology that merges proximity biotinylation by TurboID and protein-fragment complementation to find SUMO-dependent interactors of proteins of interest. We develop an optimized split-TurboID version and show SUMO interaction-dependent labelling of proteins proximal to PML and RANGAP1. SUMO-dependent interactors of PML are involved in transcription, DNA damage, stress response and SUMO modification and are highly enriched in SUMO Interacting Motifs, but may only represent a subset of the total PML proximal proteome. Likewise, SUMO-ID also allow us to identify interactors of SUMOylated SALL1, a less characterized SUMO substrate. Furthermore, using TP53 as a substrate, we identify SUMO1, SUMO2 and Ubiquitin preferential interactors. Thus, SUMO-ID is a powerful tool that allows to study the consequences of SUMO-dependent interactions, and may further unravel the complexity of the ubiquitin code.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Procesamiento Proteico-Postraduccional
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Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina
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Mapeo de Interacción de Proteínas
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Sumoilación
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Mapas de Interacción de Proteínas
Tipo de estudio:
Diagnostic_studies
/
Prognostic_studies
Límite:
Humans
Idioma:
En
Año:
2021
Tipo del documento:
Article