Identification of proximal SUMO-dependent interactors using SUMO-ID

被引:34
作者
Barroso-Gomila, Orhi [1 ]
Trulsson, Fredrik [2 ]
Muratore, Veronica [1 ]
Canosa, Inigo [1 ]
Merino-Cacho, Laura [1 ]
Rosa Cortazar, Ana [1 ,3 ]
Perez, Coralia [1 ]
Azkargorta, Mikel [1 ,4 ,5 ]
Iloro, Ibon [1 ,4 ,5 ]
Carracedo, Arkaitz [1 ,3 ,6 ,7 ]
Aransay, Ana M. [1 ,4 ]
Elortza, Felix [1 ,4 ,5 ]
Mayor, Ugo [6 ,7 ]
Vertegaal, Alfred C. O. [2 ]
Barrio, Rosa [1 ]
Sutherland, James D. [1 ]
机构
[1] Ctr Cooperat Res Biosci CIC bioGUNE, Basque Res & Technol Alliance BRTA, Bizkaia Technol Pk,Bldg 801 A, Derio 48160, Spain
[2] Leiden Univ Med Ctr LUMC, Cell & Chem Biol, NL-2333 ZA Leiden, Netherlands
[3] Inst Salud Carlos III, CIBERONC, C Monforte de Lemos 3-5,Pabellon 11,Planta 0, Madrid 28029, Spain
[4] Inst Salud Carlos III, CIBERehd, C Monforte de Lemos 3-5,Pabellon 11,Planta 0, Madrid 28029, Spain
[5] Inst Salud Carlos III, ProteoRed ISCIII, C Monforte de Lemos 3-5,Pabellon 11,Planta 0, Madrid 28029, Spain
[6] Basque Fdn Sci, Ikerbasque, Bilbao 48011, Spain
[7] Univ Basque Country, UPV EHU, Biochem & Mol Biol Dept, E-48940 Leioa, Spain
基金
欧洲研究理事会;
关键词
PML NUCLEAR-BODIES; PROMYELOCYTIC LEUKEMIA; WEB-SERVER; RAR-ALPHA; SUMOYLATION; UBIQUITIN; REVEALS; BODY; PROTEINS; SALL1;
D O I
10.1038/s41467-021-26807-6
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
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页数:19
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