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Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites

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Standard

Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites. / Lundby, Alicia; Franciosa, Giulia; Emdal, Kristina B; Refsgaard, Jan C; Gnosa, Sebastian P; Bekker-Jensen, Dorte B; Secher, Anna; Maurya, Svetlana R; Paul, Indranil; Mendez, Blanca L; Kelstrup, Christian D; Francavilla, Chiara; Kveiborg, Marie; Montoya, Guillermo; Jensen, Lars J; Olsen, Jesper V.

I: Cell, Bind 179, Nr. 2, 2019, s. 543-560.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Lundby, A, Franciosa, G, Emdal, KB, Refsgaard, JC, Gnosa, SP, Bekker-Jensen, DB, Secher, A, Maurya, SR, Paul, I, Mendez, BL, Kelstrup, CD, Francavilla, C, Kveiborg, M, Montoya, G, Jensen, LJ & Olsen, JV 2019, 'Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites', Cell, bind 179, nr. 2, s. 543-560. https://doi.org/10.1016/j.cell.2019.09.008

APA

Lundby, A., Franciosa, G., Emdal, K. B., Refsgaard, J. C., Gnosa, S. P., Bekker-Jensen, D. B., Secher, A., Maurya, S. R., Paul, I., Mendez, B. L., Kelstrup, C. D., Francavilla, C., Kveiborg, M., Montoya, G., Jensen, L. J., & Olsen, J. V. (2019). Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites. Cell, 179(2), 543-560. https://doi.org/10.1016/j.cell.2019.09.008

Vancouver

Lundby A, Franciosa G, Emdal KB, Refsgaard JC, Gnosa SP, Bekker-Jensen DB o.a. Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites. Cell. 2019;179(2):543-560. https://doi.org/10.1016/j.cell.2019.09.008

Author

Lundby, Alicia ; Franciosa, Giulia ; Emdal, Kristina B ; Refsgaard, Jan C ; Gnosa, Sebastian P ; Bekker-Jensen, Dorte B ; Secher, Anna ; Maurya, Svetlana R ; Paul, Indranil ; Mendez, Blanca L ; Kelstrup, Christian D ; Francavilla, Chiara ; Kveiborg, Marie ; Montoya, Guillermo ; Jensen, Lars J ; Olsen, Jesper V. / Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites. I: Cell. 2019 ; Bind 179, Nr. 2. s. 543-560.

Bibtex

@article{75017f9dbe1d4a25b9a480a3971e7d8d,
title = "Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites",
abstract = "Tyrosine phosphorylation regulates multi-layered signaling networks with broad implications in (patho)physiology, but high-throughput methods for functional annotation of phosphotyrosine sites are lacking. To decipher phosphotyrosine signaling directly in tissue samples, we developed a mass-spectrometry-based interaction proteomics approach. We measured the in vivo EGF-dependent signaling network in lung tissue quantifying >1,000 phosphotyrosine sites. To assign function to all EGF-regulated sites, we determined their recruited protein signaling complexes in lung tissue by interaction proteomics. We demonstrated how mutations near tyrosine residues introduce molecular switches that rewire cancer signaling networks, and we revealed oncogenic properties of such a lung cancer EGFR mutant. To demonstrate the scalability of the approach, we performed >1,000 phosphopeptide pulldowns and analyzed them by rapid mass spectrometric analysis, revealing tissue-specific differences in interactors. Our approach is a general strategy for functional annotation of phosphorylation sites in tissues, enabling in-depth mechanistic insights into oncogenic rewiring of signaling networks.",
author = "Alicia Lundby and Giulia Franciosa and Emdal, {Kristina B} and Refsgaard, {Jan C} and Gnosa, {Sebastian P} and Bekker-Jensen, {Dorte B} and Anna Secher and Maurya, {Svetlana R} and Indranil Paul and Mendez, {Blanca L} and Kelstrup, {Christian D} and Chiara Francavilla and Marie Kveiborg and Guillermo Montoya and Jensen, {Lars J} and Olsen, {Jesper V}",
note = "Copyright {\textcopyright} 2019 Elsevier Inc. All rights reserved.",
year = "2019",
doi = "10.1016/j.cell.2019.09.008",
language = "English",
volume = "179",
pages = "543--560",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "2",

}

RIS

TY - JOUR

T1 - Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites

AU - Lundby, Alicia

AU - Franciosa, Giulia

AU - Emdal, Kristina B

AU - Refsgaard, Jan C

AU - Gnosa, Sebastian P

AU - Bekker-Jensen, Dorte B

AU - Secher, Anna

AU - Maurya, Svetlana R

AU - Paul, Indranil

AU - Mendez, Blanca L

AU - Kelstrup, Christian D

AU - Francavilla, Chiara

AU - Kveiborg, Marie

AU - Montoya, Guillermo

AU - Jensen, Lars J

AU - Olsen, Jesper V

N1 - Copyright © 2019 Elsevier Inc. All rights reserved.

PY - 2019

Y1 - 2019

N2 - Tyrosine phosphorylation regulates multi-layered signaling networks with broad implications in (patho)physiology, but high-throughput methods for functional annotation of phosphotyrosine sites are lacking. To decipher phosphotyrosine signaling directly in tissue samples, we developed a mass-spectrometry-based interaction proteomics approach. We measured the in vivo EGF-dependent signaling network in lung tissue quantifying >1,000 phosphotyrosine sites. To assign function to all EGF-regulated sites, we determined their recruited protein signaling complexes in lung tissue by interaction proteomics. We demonstrated how mutations near tyrosine residues introduce molecular switches that rewire cancer signaling networks, and we revealed oncogenic properties of such a lung cancer EGFR mutant. To demonstrate the scalability of the approach, we performed >1,000 phosphopeptide pulldowns and analyzed them by rapid mass spectrometric analysis, revealing tissue-specific differences in interactors. Our approach is a general strategy for functional annotation of phosphorylation sites in tissues, enabling in-depth mechanistic insights into oncogenic rewiring of signaling networks.

AB - Tyrosine phosphorylation regulates multi-layered signaling networks with broad implications in (patho)physiology, but high-throughput methods for functional annotation of phosphotyrosine sites are lacking. To decipher phosphotyrosine signaling directly in tissue samples, we developed a mass-spectrometry-based interaction proteomics approach. We measured the in vivo EGF-dependent signaling network in lung tissue quantifying >1,000 phosphotyrosine sites. To assign function to all EGF-regulated sites, we determined their recruited protein signaling complexes in lung tissue by interaction proteomics. We demonstrated how mutations near tyrosine residues introduce molecular switches that rewire cancer signaling networks, and we revealed oncogenic properties of such a lung cancer EGFR mutant. To demonstrate the scalability of the approach, we performed >1,000 phosphopeptide pulldowns and analyzed them by rapid mass spectrometric analysis, revealing tissue-specific differences in interactors. Our approach is a general strategy for functional annotation of phosphorylation sites in tissues, enabling in-depth mechanistic insights into oncogenic rewiring of signaling networks.

U2 - 10.1016/j.cell.2019.09.008

DO - 10.1016/j.cell.2019.09.008

M3 - Journal article

C2 - 31585087

VL - 179

SP - 543

EP - 560

JO - Cell

JF - Cell

SN - 0092-8674

IS - 2

ER -

ID: 228455146