Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level

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

Standard

Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level. / Danielsen, Jannie M R; Sylvestersen, Kathrine B; Bekker-Jensen, Simon; Szklarczyk, Damian; Poulsen, Jon W; Horn, Heiko; Jensen, Lars J; Mailand, Niels; Nielsen, Michael L.

In: Molecular and Cellular Proteomics, Vol. 10, No. 3, 01.03.2011, p. M110.003590.

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

Harvard

Danielsen, JMR, Sylvestersen, KB, Bekker-Jensen, S, Szklarczyk, D, Poulsen, JW, Horn, H, Jensen, LJ, Mailand, N & Nielsen, ML 2011, 'Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level', Molecular and Cellular Proteomics, vol. 10, no. 3, pp. M110.003590. https://doi.org/10.1074/mcp.M110.003590

APA

Danielsen, J. M. R., Sylvestersen, K. B., Bekker-Jensen, S., Szklarczyk, D., Poulsen, J. W., Horn, H., Jensen, L. J., Mailand, N., & Nielsen, M. L. (2011). Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level. Molecular and Cellular Proteomics, 10(3), M110.003590. https://doi.org/10.1074/mcp.M110.003590

Vancouver

Danielsen JMR, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H et al. Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level. Molecular and Cellular Proteomics. 2011 Mar 1;10(3):M110.003590. https://doi.org/10.1074/mcp.M110.003590

Author

Danielsen, Jannie M R ; Sylvestersen, Kathrine B ; Bekker-Jensen, Simon ; Szklarczyk, Damian ; Poulsen, Jon W ; Horn, Heiko ; Jensen, Lars J ; Mailand, Niels ; Nielsen, Michael L. / Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level. In: Molecular and Cellular Proteomics. 2011 ; Vol. 10, No. 3. pp. M110.003590.

Bibtex

@article{fe68c109f9e0400488ad9a088f0fd9c7,
title = "Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level",
abstract = "The covalent attachment of ubiquitin to proteins regulates numerous processes in eukaryotic cells. Here we report the identification of 753 unique lysine ubiquitylation sites on 471 proteins using higher-energy collisional dissociation on the LTQ Orbitrap Velos. In total 5756 putative ubiquitin substrates were identified. Lysine residues targeted by the ubiquitin-ligase system show no unique sequence feature. Surface accessible lysine residues located in ordered secondary regions, surrounded by smaller and positively charged amino acids are preferred sites of ubiquitylation. Lysine ubiquitylation shows promiscuity at the site level, as evidenced by low evolutionary conservation of ubiquitylation sites across eukaryotic species. Among lysine modifications a significant overlap (20%) between ubiquitylation and acetylation at site level highlights extensive competitive crosstalk among these modifications. This site-specific crosstalk is not prevalent among cell cycle ubiquitylations. Between SUMOylation and ubiquitylation the preferred interaction is through mixed-chain conjugation. Overall these data provide novel insights into the site-specific selection and regulatory function of lysine ubiquitylation.",
keywords = "Acetylation, Amino Acid Sequence, Cell Line, Conserved Sequence, Humans, Lysine, Mass Spectrometry, Molecular Sequence Data, Sumoylation, Ubiquitin, Ubiquitinated Proteins, Ubiquitination",
author = "Danielsen, {Jannie M R} and Sylvestersen, {Kathrine B} and Simon Bekker-Jensen and Damian Szklarczyk and Poulsen, {Jon W} and Heiko Horn and Jensen, {Lars J} and Niels Mailand and Nielsen, {Michael L}",
year = "2011",
month = mar,
day = "1",
doi = "10.1074/mcp.M110.003590",
language = "English",
volume = "10",
pages = "M110.003590",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology",
number = "3",

}

RIS

TY - JOUR

T1 - Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level

AU - Danielsen, Jannie M R

AU - Sylvestersen, Kathrine B

AU - Bekker-Jensen, Simon

AU - Szklarczyk, Damian

AU - Poulsen, Jon W

AU - Horn, Heiko

AU - Jensen, Lars J

AU - Mailand, Niels

AU - Nielsen, Michael L

PY - 2011/3/1

Y1 - 2011/3/1

N2 - The covalent attachment of ubiquitin to proteins regulates numerous processes in eukaryotic cells. Here we report the identification of 753 unique lysine ubiquitylation sites on 471 proteins using higher-energy collisional dissociation on the LTQ Orbitrap Velos. In total 5756 putative ubiquitin substrates were identified. Lysine residues targeted by the ubiquitin-ligase system show no unique sequence feature. Surface accessible lysine residues located in ordered secondary regions, surrounded by smaller and positively charged amino acids are preferred sites of ubiquitylation. Lysine ubiquitylation shows promiscuity at the site level, as evidenced by low evolutionary conservation of ubiquitylation sites across eukaryotic species. Among lysine modifications a significant overlap (20%) between ubiquitylation and acetylation at site level highlights extensive competitive crosstalk among these modifications. This site-specific crosstalk is not prevalent among cell cycle ubiquitylations. Between SUMOylation and ubiquitylation the preferred interaction is through mixed-chain conjugation. Overall these data provide novel insights into the site-specific selection and regulatory function of lysine ubiquitylation.

AB - The covalent attachment of ubiquitin to proteins regulates numerous processes in eukaryotic cells. Here we report the identification of 753 unique lysine ubiquitylation sites on 471 proteins using higher-energy collisional dissociation on the LTQ Orbitrap Velos. In total 5756 putative ubiquitin substrates were identified. Lysine residues targeted by the ubiquitin-ligase system show no unique sequence feature. Surface accessible lysine residues located in ordered secondary regions, surrounded by smaller and positively charged amino acids are preferred sites of ubiquitylation. Lysine ubiquitylation shows promiscuity at the site level, as evidenced by low evolutionary conservation of ubiquitylation sites across eukaryotic species. Among lysine modifications a significant overlap (20%) between ubiquitylation and acetylation at site level highlights extensive competitive crosstalk among these modifications. This site-specific crosstalk is not prevalent among cell cycle ubiquitylations. Between SUMOylation and ubiquitylation the preferred interaction is through mixed-chain conjugation. Overall these data provide novel insights into the site-specific selection and regulatory function of lysine ubiquitylation.

KW - Acetylation

KW - Amino Acid Sequence

KW - Cell Line

KW - Conserved Sequence

KW - Humans

KW - Lysine

KW - Mass Spectrometry

KW - Molecular Sequence Data

KW - Sumoylation

KW - Ubiquitin

KW - Ubiquitinated Proteins

KW - Ubiquitination

U2 - 10.1074/mcp.M110.003590

DO - 10.1074/mcp.M110.003590

M3 - Journal article

C2 - 21139048

VL - 10

SP - M110.003590

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

SN - 1535-9476

IS - 3

ER -

ID: 33619267