Proteomics

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Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 1)


ABSTRACT: Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0–SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structural–predictive analyses revealed that lysines residing in disordered regions are preferentially targeted by SUMO, in notable contrast to other widespread lysine modifications. In our data set, we identified 807 SUMOylated peptides that were co-modified by phosphorylation, along with dozens of SUMOylated peptides that were co-modified by ubiquitylation, acetylation and methylation. Notably, 9% of the identified SUMOylome occurred proximal to phosphorylation, and numerous SUMOylation sites were found to be fully dependent on prior phosphorylation events. SUMO-proximal phosphorylation occurred primarily in a proline-directed manner, and inhibition of cyclin-dependent kinases dynamically affected co-modification. Collectively, we present a comprehensive analysis of the SUMOylated proteome, uncovering the structural preferences for SUMO and providing system-wide evidence for a remarkable degree of cross-talk between SUMOylation and other major PTMs. (part 1)

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

SUBMITTER: Ivo Hendriks  

LAB HEAD: Michael Lund Nielsen

PROVIDER: PXD004927 | Pride | 2017-01-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
HUMAN.fasta Fasta
MaxQuantOutput.tar.gz Other
QE6_LC6_IAH_SUMO_HeLa_1_All.raw Raw
QE6_LC6_IAH_SUMO_HeLa_1_F1.raw Raw
QE6_LC6_IAH_SUMO_HeLa_1_F2.raw Raw
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Publications

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

Hendriks Ivo A IA   Lyon David D   Young Clifford C   Jensen Lars J LJ   Vertegaal Alfred C O AC   Nielsen Michael L ML  

Nature structural & molecular biology 20170123 3


Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0-SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structural-predictive analyses revealed that lysines residing in disordered regions are preferentially targeted by SUMO, in notable contrast to other widespread lysine modifications. In our data set, we identified  ...[more]

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