Comprehensive Identification of SUMO2/3 Targets and Their Dynamics during Mitosis

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Comprehensive Identification of SUMO2/3 Targets and Their Dynamics during Mitosis. / Schou, Julie; Kelstrup, Christian D; Hayward, Daniel G; Olsen, Jesper V; Nilsson, Jakob.

In: PLOS ONE, Vol. 9, No. 6, 27.06.2014, p. e100692.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Schou, J, Kelstrup, CD, Hayward, DG, Olsen, JV & Nilsson, J 2014, 'Comprehensive Identification of SUMO2/3 Targets and Their Dynamics during Mitosis', PLOS ONE, vol. 9, no. 6, pp. e100692. https://doi.org/10.1371/journal.pone.0100692

APA

Schou, J., Kelstrup, C. D., Hayward, D. G., Olsen, J. V., & Nilsson, J. (2014). Comprehensive Identification of SUMO2/3 Targets and Their Dynamics during Mitosis. PLOS ONE, 9(6), e100692. https://doi.org/10.1371/journal.pone.0100692

Vancouver

Schou J, Kelstrup CD, Hayward DG, Olsen JV, Nilsson J. Comprehensive Identification of SUMO2/3 Targets and Their Dynamics during Mitosis. PLOS ONE. 2014 Jun 27;9(6):e100692. https://doi.org/10.1371/journal.pone.0100692

Author

Schou, Julie ; Kelstrup, Christian D ; Hayward, Daniel G ; Olsen, Jesper V ; Nilsson, Jakob. / Comprehensive Identification of SUMO2/3 Targets and Their Dynamics during Mitosis. In: PLOS ONE. 2014 ; Vol. 9, No. 6. pp. e100692.

Bibtex

@article{c3790e46a7234a45bcf734965a65599d,
title = "Comprehensive Identification of SUMO2/3 Targets and Their Dynamics during Mitosis",
abstract = "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.",
author = "Julie Schou and Kelstrup, {Christian D} and Hayward, {Daniel G} and Olsen, {Jesper V} and Jakob Nilsson",
year = "2014",
month = jun,
day = "27",
doi = "10.1371/journal.pone.0100692",
language = "English",
volume = "9",
pages = "e100692",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "6",

}

RIS

TY - JOUR

T1 - Comprehensive Identification of SUMO2/3 Targets and Their Dynamics during Mitosis

AU - Schou, Julie

AU - Kelstrup, Christian D

AU - Hayward, Daniel G

AU - Olsen, Jesper V

AU - Nilsson, Jakob

PY - 2014/6/27

Y1 - 2014/6/27

N2 - 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.

AB - 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.

U2 - 10.1371/journal.pone.0100692

DO - 10.1371/journal.pone.0100692

M3 - Journal article

C2 - 24971888

VL - 9

SP - e100692

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 6

ER -

ID: 117863798