PT  - JOURNAL ARTICLE
AU  - Orhi Barroso-Gomila
AU  - Fredrik Trulsson
AU  - Veronica Muratore
AU  - Iñigo Canosa
AU  - Ana Rosa Cortazar
AU  - Coralia Perez
AU  - Mikel Azkargorta
AU  - Ibon Iloro
AU  - Arkaitz Carracedo
AU  - Ana M Aransay
AU  - Felix Elortza
AU  - Ugo Mayor
AU  - Alfred C. O. Vertegaal
AU  - Rosa Barrio
AU  - James D. Sutherland
TI  - Identification of proximal SUMO-dependent interactors using SUMO-ID
AID  - 10.1101/2020.12.28.424528
DP  - 2020 Jan 01
TA  - bioRxiv
PG  - 2020.12.28.424528
4099  - http://biorxiv.org/content/early/2020/12/28/2020.12.28.424528.short
4100  - http://biorxiv.org/content/early/2020/12/28/2020.12.28.424528.full
AB  - 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 developed 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 allowed us to identify novel interactors of SUMOylated SALL1, a less characterized SUMO substrate. 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.Competing Interest StatementThe authors have declared no competing interest.