UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites

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UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. / Akimov, Vyacheslav; Barrio-Hernandez, Inigo; Hansen, Sten V.F.; Hallenborg, Philip; Pedersen, Anna-Kathrine; Bekker-Jensen, Dorte B.; Puglia, Michele; Christensen, Stine D K; Vanselow, Jens T.; Nielsen, Mogens M.; Kratchmarova, Irina; Kelstrup, Christian D.; Olsen, Jesper V.; Blagoev, Blagoy.

In: Nature Structural & Molecular Biology, Vol. 25, 2018, p. 631-640.

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

Harvard

Akimov, V, Barrio-Hernandez, I, Hansen, SVF, Hallenborg, P, Pedersen, A-K, Bekker-Jensen, DB, Puglia, M, Christensen, SDK, Vanselow, JT, Nielsen, MM, Kratchmarova, I, Kelstrup, CD, Olsen, JV & Blagoev, B 2018, 'UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites', Nature Structural & Molecular Biology, vol. 25, pp. 631-640. https://doi.org/10.1038/s41594-018-0084-y

APA

Akimov, V., Barrio-Hernandez, I., Hansen, S. V. F., Hallenborg, P., Pedersen, A-K., Bekker-Jensen, D. B., Puglia, M., Christensen, S. D. K., Vanselow, J. T., Nielsen, M. M., Kratchmarova, I., Kelstrup, C. D., Olsen, J. V., & Blagoev, B. (2018). UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. Nature Structural & Molecular Biology, 25, 631-640. https://doi.org/10.1038/s41594-018-0084-y

Vancouver

Akimov V, Barrio-Hernandez I, Hansen SVF, Hallenborg P, Pedersen A-K, Bekker-Jensen DB et al. UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. Nature Structural & Molecular Biology. 2018;25:631-640. https://doi.org/10.1038/s41594-018-0084-y

Author

Akimov, Vyacheslav ; Barrio-Hernandez, Inigo ; Hansen, Sten V.F. ; Hallenborg, Philip ; Pedersen, Anna-Kathrine ; Bekker-Jensen, Dorte B. ; Puglia, Michele ; Christensen, Stine D K ; Vanselow, Jens T. ; Nielsen, Mogens M. ; Kratchmarova, Irina ; Kelstrup, Christian D. ; Olsen, Jesper V. ; Blagoev, Blagoy. / UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. In: Nature Structural & Molecular Biology. 2018 ; Vol. 25. pp. 631-640.

Bibtex

@article{8b6c3aa15ba24dc087f48a17c284de68,
title = "UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites",
abstract = "Ubiquitination is a post-translational modification (PTM) that is essential for balancing numerous physiological processes. To enable delineation of protein ubiquitination at a site-specific level, we generated an antibody, denoted UbiSite, recognizing the C-terminal 13 amino acids of ubiquitin, which remain attached to modified peptides after proteolytic digestion with the endoproteinase LysC. Notably, UbiSite is specific to ubiquitin. Furthermore, besides ubiquitination on lysine residues, protein N-terminal ubiquitination is readily detected as well. By combining UbiSite enrichment with sequential LysC and trypsin digestion and high-accuracy MS, we identified over 63,000 unique ubiquitination sites on 9,200 proteins in two human cell lines. In addition to uncovering widespread involvement of this PTM in all cellular aspects, the analyses reveal an inverse association between protein N-terminal ubiquitination and acetylation, as well as a complete lack of correlation between changes in protein abundance and alterations in ubiquitination sites upon proteasome inhibition.",
author = "Vyacheslav Akimov and Inigo Barrio-Hernandez and Hansen, {Sten V.F.} and Philip Hallenborg and Anna-Kathrine Pedersen and Bekker-Jensen, {Dorte B.} and Michele Puglia and Christensen, {Stine D K} and Vanselow, {Jens T.} and Nielsen, {Mogens M.} and Irina Kratchmarova and Kelstrup, {Christian D.} and Olsen, {Jesper V.} and Blagoy Blagoev",
year = "2018",
doi = "10.1038/s41594-018-0084-y",
language = "English",
volume = "25",
pages = "631--640",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites

AU - Akimov, Vyacheslav

AU - Barrio-Hernandez, Inigo

AU - Hansen, Sten V.F.

AU - Hallenborg, Philip

AU - Pedersen, Anna-Kathrine

AU - Bekker-Jensen, Dorte B.

AU - Puglia, Michele

AU - Christensen, Stine D K

AU - Vanselow, Jens T.

AU - Nielsen, Mogens M.

AU - Kratchmarova, Irina

AU - Kelstrup, Christian D.

AU - Olsen, Jesper V.

AU - Blagoev, Blagoy

PY - 2018

Y1 - 2018

N2 - Ubiquitination is a post-translational modification (PTM) that is essential for balancing numerous physiological processes. To enable delineation of protein ubiquitination at a site-specific level, we generated an antibody, denoted UbiSite, recognizing the C-terminal 13 amino acids of ubiquitin, which remain attached to modified peptides after proteolytic digestion with the endoproteinase LysC. Notably, UbiSite is specific to ubiquitin. Furthermore, besides ubiquitination on lysine residues, protein N-terminal ubiquitination is readily detected as well. By combining UbiSite enrichment with sequential LysC and trypsin digestion and high-accuracy MS, we identified over 63,000 unique ubiquitination sites on 9,200 proteins in two human cell lines. In addition to uncovering widespread involvement of this PTM in all cellular aspects, the analyses reveal an inverse association between protein N-terminal ubiquitination and acetylation, as well as a complete lack of correlation between changes in protein abundance and alterations in ubiquitination sites upon proteasome inhibition.

AB - Ubiquitination is a post-translational modification (PTM) that is essential for balancing numerous physiological processes. To enable delineation of protein ubiquitination at a site-specific level, we generated an antibody, denoted UbiSite, recognizing the C-terminal 13 amino acids of ubiquitin, which remain attached to modified peptides after proteolytic digestion with the endoproteinase LysC. Notably, UbiSite is specific to ubiquitin. Furthermore, besides ubiquitination on lysine residues, protein N-terminal ubiquitination is readily detected as well. By combining UbiSite enrichment with sequential LysC and trypsin digestion and high-accuracy MS, we identified over 63,000 unique ubiquitination sites on 9,200 proteins in two human cell lines. In addition to uncovering widespread involvement of this PTM in all cellular aspects, the analyses reveal an inverse association between protein N-terminal ubiquitination and acetylation, as well as a complete lack of correlation between changes in protein abundance and alterations in ubiquitination sites upon proteasome inhibition.

U2 - 10.1038/s41594-018-0084-y

DO - 10.1038/s41594-018-0084-y

M3 - Journal article

C2 - 29967540

VL - 25

SP - 631

EP - 640

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

ER -

ID: 199217277