Identification of proximal SUMO-dependent interactors using SUMO-ID

被引：0

作者：

Orhi Barroso-Gomila

Fredrik Trulsson

Veronica Muratore

Iñigo Canosa

Laura Merino-Cacho

Ana Rosa Cortazar

Coralia Pérez

Mikel Azkargorta

Ibon Iloro

Arkaitz Carracedo

Ana M. Aransay

Felix Elortza

Ugo Mayor

Alfred C. O. Vertegaal

Rosa Barrio

James D. Sutherland

机构：

[1] Center for Cooperative Research in Biosciences (CIC bioGUNE),Biochemistry and Molecular Biology Department

[2] Basque Research and Technology Alliance (BRTA),undefined

[3] Bizkaia Technology Park,undefined

[4] Cell and Chemical Biology,undefined

[5] Leiden University Medical Center (LUMC),undefined

[6] CIBERONC,undefined

[7] Instituto de Salud Carlos III,undefined

[8] C/ Monforte de Lemos 3-5,undefined

[9] Pabellón 11,undefined

[10] Planta 0,undefined

[11] CIBERehd,undefined

[12] Instituto de Salud Carlos III,undefined

[13] C/ Monforte de Lemos 3-5,undefined

[14] Pabellón 11,undefined

[15] Planta 0,undefined

[16] ProteoRed-ISCIII,undefined

[17] Instituto de Salud Carlos III,undefined

[18] C/ Monforte de Lemos 3-5,undefined

[19] Pabellón 11,undefined

[20] Planta 0,undefined

[21] Ikerbasque,undefined

[22] Basque Foundation for Science,undefined

[23] University of the Basque Country (UPV/EHU),undefined

来源：

Nature Communications | / 12卷

关键词：

D O I：

暂无

中图分类号：

学科分类号：

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

共 155 条

[1]

Flotho A(2013)Sumoylation: a regulatory protein modification in health and disease Annu. Rev. Biochem. 82 357-385

[2]

Melchior F(2010)The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition Nat. Rev. Mol. Cell Biol. 11 861-871

[3]

Gareau JR(2012)An acetylation switch regulates SUMO-dependent protein interaction networks Mol. Cell 46 759-770

[4]

Lima CD(2010)SUMO chains: polymeric signals Biochem. Soc. Trans. 38 46-49

[5]

Ullmann R(2012)Heterologous SUMO-2/3-ubiquitin chains optimize IkappaBalpha degradation and NF-kappaB activity PLoS One 7 e51672-36

[6]

Chien CD(2017)SUMO conjugation - a mechanistic view Biomol. Concepts 8 13-478

[7]

Avantaggiati ML(2020)The role of SUMOylation during development Biochem. Soc. Trans. 48 463-336

[8]

Muller S(2020)SUMOylation in the control of cholesterol homeostasis Open Biol. 10 200054-595

[9]

Vertegaal AC(2017)Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation Nat. Struct. Mol. Biol. 24 325-555

[10]

Aillet F(2016)A comprehensive compilation of SUMO proteomics Nat. Rev. Mol. Cell Biol. 17 581-298

← 1 2 3 4 5 6 7 8 9 10 →