Mol Cell Proteomics 2009,
PMID: 19596686
Matafora, Vittoria; D'Amato, Alfonsina; Mori, Silvia; Blasi, Francesco; Bachi, Angela
Many cellular processes are regulated by the coordination of several post-translational modifications that allow a very fine modulation of substrates. Recently it has been reported that there is a relationship between sumoylation and ubiquitination. Here we propose that the nucleolus is the key organelle in which SUMO-1 conjugates accumulate in response to proteasome inhibition. We demonstrated that, upon proteasome inhibition, the SUMO-1 nuclear dot localization is redirected to nucleolar structures. To better understand this process we investigated, by quantitative proteomics, the effect of proteasome activity on endogenous nucleolar SUMO-1 targets. 193 potential SUMO-1 substrates were identified, and interestingly in several purified SUMO-1 conjugates ubiquitin chains were found to be present, confirming the coordination of these two modifications. 23 SUMO-1 targets were confirmed by an in vitro sumoylation reaction performed on nuclear substrates. They belong to protein families such as small nuclear ribonucleoproteins, heterogeneous nuclear ribonucleoproteins, ribosomal proteins, histones, RNA-binding proteins, and transcription factor regulators. Among these, histone H1, histone H3, and p160 Myb-binding protein 1A were further characterized as novel SUMO-1 substrates. The analysis of the nature of the SUMO-1 targets identified in this study strongly indicates that sumoylation, acting in coordination with the ubiquitin-proteasome system, regulates the maintenance of nucleolar integrity.
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(direct interaction, pull down)
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IRef Biogrid Interaction:
PRKDC
—
SUMO1
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
PRKDC
—
SUMO1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
SUMO1
—
NOP2
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
SUMO1
—
NOP2
(direct interaction, pull down)
-
IRef Biogrid Interaction:
SUMO1
—
ACIN1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
RBM39
—
SUMO1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
SUMO1
—
EIF4G1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
SUMO1
—
NONO
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
SUMO1
—
NONO
(direct interaction, pull down)
-
IRef Biogrid Interaction:
SF3B1
—
SUMO1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
SUMO1
—
HSPA8
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MYBBP1A
—
SUMO1
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MYBBP1A
—
SUMO1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
SUMO1
—
UBTF
(direct interaction, pull down)
-
IRef Biogrid Interaction:
SUMO1
—
TCOF1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
RRBP1
—
SUMO1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
SCAPER
—
SUMO1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
TOP2A
—
SUMO1
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
TOP2A
—
SUMO1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
SART1
—
SUMO1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
PARP1
—
SUMO1
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
PARP1
—
SUMO1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
TOP1
—
SUMO1
(direct interaction, pull down)
-
IRef Biogrid Interaction:
SUMO1
—
HSP90AB1
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
SUMO1
—
SUMO1
(direct interaction, pull down)
In total, 222 gene pairs are associated to this article in curated databases