Comprehensive identification of SUMO2/3 targets and their dynamics during mitosis

Autor: Jakob Nilsson, Christian D. Kelstrup, Daniel G. Hayward, Jesper V. Olsen, Julie Schou
Jazyk: angličtina
Rok vydání: 2014
Předmět:
Proteomics
SUMO protein
lcsh:Medicine
Polo-like kinase
Biochemistry
rho Guanine Nucleotide Dissociation Inhibitor beta
Cell Signaling
Tandem Mass Spectrometry
Molecular Cell Biology
Cell Cycle and Cell Division
RNA
Small Interfering
lcsh:Science
Chromatography
High Pressure Liquid
Multidisciplinary
Chromosome Biology
Cell cycle
Cell biology
Mitotic Signaling
Cell Processes
Benzamides
Small Ubiquitin-Related Modifier Proteins
RNA Interference
Post-translational modification
Research Article
Signal Transduction
Prometaphase
Paclitaxel
Molecular Sequence Data
Mitosis
Biology
Humans
Amino Acid Sequence
Ubiquitins
Molecular Biology
rho Guanine Nucleotide Dissociation Inhibitor alpha
Tandem affinity purification
Biology and life sciences
lcsh:R
Sumoylation
Proteins
Cell Biology
Amino Acid Substitution
Mitotic exit
Quinazolines
lcsh:Q
HeLa Cells
Zdroj: PLoS ONE, Vol 9, Iss 6, p e100692 (2014)
PLoS ONE
ISSN: 1932-6203
Popis: During mitosis large alterations in cellular structures occur rapidly, which to a large extent is regulated by post-translational modification of proteins. Modification of proteins with the small ubiquitin-related protein SUMO2/3 regulates mitotic progression, but few mitotic targets have been identified so far. To deepen our understanding of SUMO2/3 during this window of the cell cycle, we undertook a comprehensive proteomic characterization of SUMO2/3 modified proteins in mitosis and upon mitotic exit. We developed an efficient tandem affinity purification strategy of SUMO2/3 modified proteins from mitotic cells. Combining this purification strategy with cell synchronization procedures and quantitative mass spectrometry allowed for the mapping of numerous novel targets and their dynamics as cells progressed out of mitosis. This identified RhoGDIα as a major SUMO2/3 modified protein, specifically during mitosis, mediated by the SUMO ligases PIAS2 and PIAS3. Our data provide a rich resource for further exploring the role of SUMO2/3 modifications in mitosis and cell cycle regulation.
Databáze: OpenAIRE
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