Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4)

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

Standard

Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4). / Hendriks, Ivo A; Schimmel, Joost; Eifler, Karolin; Olsen, Jesper V; Vertegaal, Alfred C O.

In: The Journal of Biological Chemistry, Vol. 290, No. 25, 19.06.2015, p. 15526-37.

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

Harvard

Hendriks, IA, Schimmel, J, Eifler, K, Olsen, JV & Vertegaal, ACO 2015, 'Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4)', The Journal of Biological Chemistry, vol. 290, no. 25, pp. 15526-37. https://doi.org/10.1074/jbc.M114.618132

APA

Hendriks, I. A., Schimmel, J., Eifler, K., Olsen, J. V., & Vertegaal, A. C. O. (2015). Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4). The Journal of Biological Chemistry, 290(25), 15526-37. https://doi.org/10.1074/jbc.M114.618132

Vancouver

Hendriks IA, Schimmel J, Eifler K, Olsen JV, Vertegaal ACO. Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4). The Journal of Biological Chemistry. 2015 Jun 19;290(25):15526-37. https://doi.org/10.1074/jbc.M114.618132

Author

Hendriks, Ivo A ; Schimmel, Joost ; Eifler, Karolin ; Olsen, Jesper V ; Vertegaal, Alfred C O. / Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4). In: The Journal of Biological Chemistry. 2015 ; Vol. 290, No. 25. pp. 15526-37.

Bibtex

@article{70045bd0d9794b9d99170629a386e82d,
title = "Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4)",
abstract = "Ring finger protein 4 (RNF4) is a SUMO-targeted ubiquitin E3 ligase with a pivotal function in the DNA damage response (DDR). SUMO interaction motifs (SIMs) in the N-terminal part of RNF4 tightly bind to SUMO polymers, and RNF4 can ubiquitinate these polymers in vitro. Using a proteomic approach, we identified the deubiquitinating enzyme ubiquitin-specific protease 11 (USP11), a known DDR-component, as a functional interactor of RNF4. USP11 can deubiquitinate hybrid SUMO-ubiquitin chains to counteract RNF4. SUMO-enriched nuclear bodies are stabilized by USP11, which functions downstream of RNF4 as a counterbalancing factor. In response to DNA damage induced by methyl methanesulfonate, USP11 could counteract RNF4 to inhibit the dissolution of nuclear bodies. Thus, we provide novel insight into cross-talk between ubiquitin and SUMO and uncover USP11 and RNF4 as a balanced SUMO-targeted ubiquitin ligase/protease pair with a role in the DDR.",
author = "Hendriks, {Ivo A} and Joost Schimmel and Karolin Eifler and Olsen, {Jesper V} and Vertegaal, {Alfred C O}",
note = "{\textcopyright} 2015 by The American Society for Biochemistry and Molecular Biology, Inc.",
year = "2015",
month = jun,
day = "19",
doi = "10.1074/jbc.M114.618132",
language = "English",
volume = "290",
pages = "15526--37",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "25",

}

RIS

TY - JOUR

T1 - Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4)

AU - Hendriks, Ivo A

AU - Schimmel, Joost

AU - Eifler, Karolin

AU - Olsen, Jesper V

AU - Vertegaal, Alfred C O

N1 - © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

PY - 2015/6/19

Y1 - 2015/6/19

N2 - Ring finger protein 4 (RNF4) is a SUMO-targeted ubiquitin E3 ligase with a pivotal function in the DNA damage response (DDR). SUMO interaction motifs (SIMs) in the N-terminal part of RNF4 tightly bind to SUMO polymers, and RNF4 can ubiquitinate these polymers in vitro. Using a proteomic approach, we identified the deubiquitinating enzyme ubiquitin-specific protease 11 (USP11), a known DDR-component, as a functional interactor of RNF4. USP11 can deubiquitinate hybrid SUMO-ubiquitin chains to counteract RNF4. SUMO-enriched nuclear bodies are stabilized by USP11, which functions downstream of RNF4 as a counterbalancing factor. In response to DNA damage induced by methyl methanesulfonate, USP11 could counteract RNF4 to inhibit the dissolution of nuclear bodies. Thus, we provide novel insight into cross-talk between ubiquitin and SUMO and uncover USP11 and RNF4 as a balanced SUMO-targeted ubiquitin ligase/protease pair with a role in the DDR.

AB - Ring finger protein 4 (RNF4) is a SUMO-targeted ubiquitin E3 ligase with a pivotal function in the DNA damage response (DDR). SUMO interaction motifs (SIMs) in the N-terminal part of RNF4 tightly bind to SUMO polymers, and RNF4 can ubiquitinate these polymers in vitro. Using a proteomic approach, we identified the deubiquitinating enzyme ubiquitin-specific protease 11 (USP11), a known DDR-component, as a functional interactor of RNF4. USP11 can deubiquitinate hybrid SUMO-ubiquitin chains to counteract RNF4. SUMO-enriched nuclear bodies are stabilized by USP11, which functions downstream of RNF4 as a counterbalancing factor. In response to DNA damage induced by methyl methanesulfonate, USP11 could counteract RNF4 to inhibit the dissolution of nuclear bodies. Thus, we provide novel insight into cross-talk between ubiquitin and SUMO and uncover USP11 and RNF4 as a balanced SUMO-targeted ubiquitin ligase/protease pair with a role in the DDR.

U2 - 10.1074/jbc.M114.618132

DO - 10.1074/jbc.M114.618132

M3 - Journal article

C2 - 25969536

VL - 290

SP - 15526

EP - 15537

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 25

ER -

ID: 140241761