Identification of proximal SUMO-dependent interactors using SUMO-ID

Barroso-Gomila, O.; Trulsson, F.; Muratore, V.; Canosa, I.; Cortazar, A. R.; Perez, C.; Azkargorta, M.; Iloro, I.; Carracedo, A.; Aransay, A. M.; Elortza, F.; Mayor, U.; Vertegaal, A. C. O.; Barrio, R.; Sutherland, J. D.

doi:10.1101/2020.12.28.424528

bioRxiv · 10.1101/2020.12.28.424528

Identification of proximal SUMO-dependent interactors using SUMO-ID

Barroso-Gomila, O.·Trulsson, F.·Muratore, V.·Canosa, I.·Cortazar, A. R.·Perez, C.·Azkargorta, M.·Iloro, I.·Carracedo, A.·Aransay, A. M.·Elortza, F.·Mayor, U.·Vertegaal, A. C. O.·Barrio, R.·Sutherland, J. D.

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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 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.

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Barroso-Gomila, O., Trulsson, F., Muratore, V., Canosa, I., Cortazar, A. R., Perez, C., Azkargorta, M., Iloro, I., Carracedo, A., Aransay, A. M., Elortza, F., Mayor, U., Vertegaal, A. C. O., Barrio, R., Sutherland, J. D.. 2020-12-28. Identification of proximal SUMO-dependent interactors using SUMO-ID. https://doi.org/10.1101/2020.12.28.424528

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