Dataset Information

A global S. cerevisiae small ubiquitin-related modifier (SUMO) system interactome.

ABSTRACT: The small ubiquitin-related modifier (SUMO) system has been implicated in a number of biological functions, yet the individual components of the SUMO machinery involved in each of these activities were largely unknown. Here we report the first global SUMO system interactome. Using affinity purification coupled with mass spectrometry, we identify >450 protein-protein interactions surrounding the SUMO E2, Siz type E3s and SUMO-specific proteases in budding yeast. Exploiting this information-rich resource, we validate several Siz1- and Siz2-specific substrates, identify a nucleoporin required for proper Ulp1 localization, and uncover important new roles for Ubc9 and Ulp2 in the maintenance of ribosomal DNA.

SUBMITTER: Srikumar T

PROVIDER: S-EPMC4039371 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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A global S. cerevisiae small ubiquitin-related modifier (SUMO) system interactome.

Srikumar Tharan T Lewicki Megan C MC Raught Brian B

Molecular systems biology 20130528

The small ubiquitin-related modifier (SUMO) system has been implicated in a number of biological functions, yet the individual components of the SUMO machinery involved in each of these activities were largely unknown. Here we report the first global SUMO system interactome. Using affinity purification coupled with mass spectrometry, we identify >450 protein-protein interactions surrounding the SUMO E2, Siz type E3s and SUMO-specific proteases in budding yeast. Exploiting this information-rich r ...[more]

PMID: 23712011

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Project description:Post-translational protein modifications (PTMs) including small chemical groups and small proteins, belonging to the ubiquitin family, are essential for virtually all cellular processes. In addition to modification by a single PTM, proteins can be modified by a combination of different modifiers, which are able to influence each other. Because little is known about crosstalk among different ubiquitin family members, we developed an improved method enabling identification of co-modified proteins on a system-wide level using mass spectrometry. We focused on the role of crosstalk between SUMO and ubiquitin during proteasomal degradation. Using two complementary approaches, we identified 498 proteins to be significantly co-modified by SUMO and ubiquitin upon MG132 treatment. These targets included many enzymatic components of PTM machinery, involved in SUMOylation and ubiquitylation, but also phosphorylation, methylation and acetylation, revealing a highly complex interconnected network of crosstalk among different PTMs. In addition, various other biological processes were found to be significantly enriched within the group of co-modified proteins, including transcription, DNA repair and the cell cycle. Interestingly, the latter group mostly consisted of proteins involved in mitosis, including a subset of chromosome segregation regulators. We hypothesize that group modification by SUMO-targeted ubiquitin ligases regulates the stability of the identified subset of mitotic proteins, which ensures proper chromosome segregation. The mitotic regulators KIF23 and MIS18BP1 were verified to be co-modified by SUMO and ubiquitin on inhibition of the proteasome and subsequently identified as novel RNF4 targets. Both modifications on MIS18BP1 were observed to increase simultaneously during late mitosis, whereas the total protein level decreased immediately afterward. These results confirm the regulation of MIS18BP1 via SUMO-ubiquitin crosstalk during mitosis. Combined, our work highlights extensive crosstalk between SUMO and ubiquitin, providing a resource for further unraveling of SUMO-ubiquitin crosstalk.

Dataset Information

A global S. cerevisiae small ubiquitin-related modifier (SUMO) system interactome.

Publications

A global S. cerevisiae small ubiquitin-related modifier (SUMO) system interactome.

Similar Datasets

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