Ubc9 sumoylation regulates SUMO target discrimination

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

Standard

Ubc9 sumoylation regulates SUMO target discrimination. / Knipscheer, Puck; Flotho, Annette; Klug, Helene; Olsen, Jesper V; van Dijk, Willem J; Fish, Alexander; Johnson, Erica S; Mann, Matthias; Sixma, Titia K; Pichler, Andrea.

In: Molecular Cell, Vol. 31, No. 3, 2008, p. 371-82.

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

Harvard

Knipscheer, P, Flotho, A, Klug, H, Olsen, JV, van Dijk, WJ, Fish, A, Johnson, ES, Mann, M, Sixma, TK & Pichler, A 2008, 'Ubc9 sumoylation regulates SUMO target discrimination', Molecular Cell, vol. 31, no. 3, pp. 371-82. https://doi.org/10.1016/j.molcel.2008.05.022

APA

Knipscheer, P., Flotho, A., Klug, H., Olsen, J. V., van Dijk, W. J., Fish, A., Johnson, E. S., Mann, M., Sixma, T. K., & Pichler, A. (2008). Ubc9 sumoylation regulates SUMO target discrimination. Molecular Cell, 31(3), 371-82. https://doi.org/10.1016/j.molcel.2008.05.022

Vancouver

Knipscheer P, Flotho A, Klug H, Olsen JV, van Dijk WJ, Fish A et al. Ubc9 sumoylation regulates SUMO target discrimination. Molecular Cell. 2008;31(3):371-82. https://doi.org/10.1016/j.molcel.2008.05.022

Author

Knipscheer, Puck ; Flotho, Annette ; Klug, Helene ; Olsen, Jesper V ; van Dijk, Willem J ; Fish, Alexander ; Johnson, Erica S ; Mann, Matthias ; Sixma, Titia K ; Pichler, Andrea. / Ubc9 sumoylation regulates SUMO target discrimination. In: Molecular Cell. 2008 ; Vol. 31, No. 3. pp. 371-82.

Bibtex

@article{9d534570e97111deba73000ea68e967b,
title = "Ubc9 sumoylation regulates SUMO target discrimination",
abstract = "Posttranslational modification with small ubiquitin-related modifier, SUMO, is a widespread mechanism for rapid and reversible changes in protein function. Considering the large number of known targets, the number of enzymes involved in modification seems surprisingly low: a single E1, a single E2, and a few distinct E3 ligases. Here we show that autosumoylation of the mammalian E2-conjugating enzyme Ubc9 at Lys14 regulates target discrimination. While not altering its activity toward HDAC4, E2-25K, PML, or TDG, sumoylation of Ubc9 impairs its activity on RanGAP1 and strongly activates sumoylation of the transcriptional regulator Sp100. Enhancement depends on a SUMO-interacting motif (SIM) in Sp100 that creates an additional interface with the SUMO conjugated to the E2, a mechanism distinct from Ubc9 approximately SUMO thioester recruitment. The crystal structure of sumoylated Ubc9 demonstrates how the newly created binding interface can provide a gain in affinity otherwise provided by E3 ligases.",
author = "Puck Knipscheer and Annette Flotho and Helene Klug and Olsen, {Jesper V} and {van Dijk}, {Willem J} and Alexander Fish and Johnson, {Erica S} and Matthias Mann and Sixma, {Titia K} and Andrea Pichler",
note = "Keywords: Amino Acid Motifs; Amino Acid Sequence; Autoantigens; Crystallography, X-Ray; Esters; Hela Cells; Humans; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; Saccharomyces cerevisiae; Small Ubiquitin-Related Modifier Proteins; Substrate Specificity; Ubiquitin-Conjugating Enzymes",
year = "2008",
doi = "10.1016/j.molcel.2008.05.022",
language = "English",
volume = "31",
pages = "371--82",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "3",

}

RIS

TY - JOUR

T1 - Ubc9 sumoylation regulates SUMO target discrimination

AU - Knipscheer, Puck

AU - Flotho, Annette

AU - Klug, Helene

AU - Olsen, Jesper V

AU - van Dijk, Willem J

AU - Fish, Alexander

AU - Johnson, Erica S

AU - Mann, Matthias

AU - Sixma, Titia K

AU - Pichler, Andrea

N1 - Keywords: Amino Acid Motifs; Amino Acid Sequence; Autoantigens; Crystallography, X-Ray; Esters; Hela Cells; Humans; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; Saccharomyces cerevisiae; Small Ubiquitin-Related Modifier Proteins; Substrate Specificity; Ubiquitin-Conjugating Enzymes

PY - 2008

Y1 - 2008

N2 - Posttranslational modification with small ubiquitin-related modifier, SUMO, is a widespread mechanism for rapid and reversible changes in protein function. Considering the large number of known targets, the number of enzymes involved in modification seems surprisingly low: a single E1, a single E2, and a few distinct E3 ligases. Here we show that autosumoylation of the mammalian E2-conjugating enzyme Ubc9 at Lys14 regulates target discrimination. While not altering its activity toward HDAC4, E2-25K, PML, or TDG, sumoylation of Ubc9 impairs its activity on RanGAP1 and strongly activates sumoylation of the transcriptional regulator Sp100. Enhancement depends on a SUMO-interacting motif (SIM) in Sp100 that creates an additional interface with the SUMO conjugated to the E2, a mechanism distinct from Ubc9 approximately SUMO thioester recruitment. The crystal structure of sumoylated Ubc9 demonstrates how the newly created binding interface can provide a gain in affinity otherwise provided by E3 ligases.

AB - Posttranslational modification with small ubiquitin-related modifier, SUMO, is a widespread mechanism for rapid and reversible changes in protein function. Considering the large number of known targets, the number of enzymes involved in modification seems surprisingly low: a single E1, a single E2, and a few distinct E3 ligases. Here we show that autosumoylation of the mammalian E2-conjugating enzyme Ubc9 at Lys14 regulates target discrimination. While not altering its activity toward HDAC4, E2-25K, PML, or TDG, sumoylation of Ubc9 impairs its activity on RanGAP1 and strongly activates sumoylation of the transcriptional regulator Sp100. Enhancement depends on a SUMO-interacting motif (SIM) in Sp100 that creates an additional interface with the SUMO conjugated to the E2, a mechanism distinct from Ubc9 approximately SUMO thioester recruitment. The crystal structure of sumoylated Ubc9 demonstrates how the newly created binding interface can provide a gain in affinity otherwise provided by E3 ligases.

U2 - 10.1016/j.molcel.2008.05.022

DO - 10.1016/j.molcel.2008.05.022

M3 - Journal article

C2 - 18691969

VL - 31

SP - 371

EP - 382

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 3

ER -

ID: 16275371