Personalized phosphoproteomics identifies functional signaling

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

Standard

Personalized phosphoproteomics identifies functional signaling. / Needham, Elise J; Hingst, Janne Rasmuss; Parker, Benjamin L; Morrison, Kaitlin R; Yang, Guang; Onslev, Johan Dejgaard; Kristensen, Jonas Møller; Højlund, Kurt; Ling, Naomi X Y; Oakhill, Jonathan S; Richter, Erik A.; Kiens, Bente; Petersen, Janni; Pehmøller, Christian; James, David E; Wojtaszewski, Jørgen; Humphrey, Sean J.

In: Nature Biotechnology, Vol. 40, No. 4, 2022, p. 576-584.

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

Harvard

Needham, EJ, Hingst, JR, Parker, BL, Morrison, KR, Yang, G, Onslev, JD, Kristensen, JM, Højlund, K, Ling, NXY, Oakhill, JS, Richter, EA, Kiens, B, Petersen, J, Pehmøller, C, James, DE, Wojtaszewski, J & Humphrey, SJ 2022, 'Personalized phosphoproteomics identifies functional signaling', Nature Biotechnology, vol. 40, no. 4, pp. 576-584. https://doi.org/10.1038/s41587-021-01099-9

APA

Needham, E. J., Hingst, J. R., Parker, B. L., Morrison, K. R., Yang, G., Onslev, J. D., Kristensen, J. M., Højlund, K., Ling, N. X. Y., Oakhill, J. S., Richter, E. A., Kiens, B., Petersen, J., Pehmøller, C., James, D. E., Wojtaszewski, J., & Humphrey, S. J. (2022). Personalized phosphoproteomics identifies functional signaling. Nature Biotechnology, 40(4), 576-584. https://doi.org/10.1038/s41587-021-01099-9

Vancouver

Needham EJ, Hingst JR, Parker BL, Morrison KR, Yang G, Onslev JD et al. Personalized phosphoproteomics identifies functional signaling. Nature Biotechnology. 2022;40(4):576-584. https://doi.org/10.1038/s41587-021-01099-9

Author

Needham, Elise J ; Hingst, Janne Rasmuss ; Parker, Benjamin L ; Morrison, Kaitlin R ; Yang, Guang ; Onslev, Johan Dejgaard ; Kristensen, Jonas Møller ; Højlund, Kurt ; Ling, Naomi X Y ; Oakhill, Jonathan S ; Richter, Erik A. ; Kiens, Bente ; Petersen, Janni ; Pehmøller, Christian ; James, David E ; Wojtaszewski, Jørgen ; Humphrey, Sean J. / Personalized phosphoproteomics identifies functional signaling. In: Nature Biotechnology. 2022 ; Vol. 40, No. 4. pp. 576-584.

Bibtex

@article{cd5ae9d95d204db4a0d02e9c71280f7b,

title = "Personalized phosphoproteomics identifies functional signaling",

abstract = "Protein phosphorylation dynamically integrates environmental and cellular information to control biological processes. Identifying functional phosphorylation amongst the thousands of phosphosites regulated by a perturbation at a global scale is a major challenge. Here we introduce 'personalized phosphoproteomics', a combination of experimental and computational analyses to link signaling with biological function by utilizing human phenotypic variance. We measure individual subject phosphoproteome responses to interventions with corresponding phenotypes measured in parallel. Applying this approach to investigate how exercise potentiates insulin signaling in human skeletal muscle, we identify both known and previously unidentified phosphosites on proteins involved in glucose metabolism. This includes a cooperative relationship between mTOR and AMPK whereby the former directly phosphorylates the latter on S377, for which we find a role in metabolic regulation. These results establish personalized phosphoproteomics as a general approach for investigating the signal transduction underlying complex biology.",

author = "Needham, {Elise J} and Hingst, {Janne Rasmuss} and Parker, {Benjamin L} and Morrison, {Kaitlin R} and Guang Yang and Onslev, {Johan Dejgaard} and Kristensen, {Jonas M{\o}ller} and Kurt H{\o}jlund and Ling, {Naomi X Y} and Oakhill, {Jonathan S} and Richter, {Erik A.} and Bente Kiens and Janni Petersen and Christian Pehm{\o}ller and James, {David E} and J{\o}rgen Wojtaszewski and Humphrey, {Sean J}",

note = "{\textcopyright} 2021. The Author(s), under exclusive licence to Springer Nature America, Inc.",

year = "2022",

doi = "10.1038/s41587-021-01099-9",

language = "English",

volume = "40",

pages = "576--584",

journal = "Nature Biotechnology",

issn = "1087-0156",

publisher = "nature publishing group",

number = "4",

}

RIS

TY - JOUR

T1 - Personalized phosphoproteomics identifies functional signaling

AU - Needham, Elise J

AU - Hingst, Janne Rasmuss

AU - Parker, Benjamin L

AU - Morrison, Kaitlin R

AU - Yang, Guang

AU - Onslev, Johan Dejgaard

AU - Kristensen, Jonas Møller

AU - Højlund, Kurt

AU - Ling, Naomi X Y

AU - Oakhill, Jonathan S

AU - Richter, Erik A.

AU - Kiens, Bente

AU - Petersen, Janni

AU - Pehmøller, Christian

AU - James, David E

AU - Wojtaszewski, Jørgen

AU - Humphrey, Sean J

PY - 2022

Y1 - 2022

N2 - Protein phosphorylation dynamically integrates environmental and cellular information to control biological processes. Identifying functional phosphorylation amongst the thousands of phosphosites regulated by a perturbation at a global scale is a major challenge. Here we introduce 'personalized phosphoproteomics', a combination of experimental and computational analyses to link signaling with biological function by utilizing human phenotypic variance. We measure individual subject phosphoproteome responses to interventions with corresponding phenotypes measured in parallel. Applying this approach to investigate how exercise potentiates insulin signaling in human skeletal muscle, we identify both known and previously unidentified phosphosites on proteins involved in glucose metabolism. This includes a cooperative relationship between mTOR and AMPK whereby the former directly phosphorylates the latter on S377, for which we find a role in metabolic regulation. These results establish personalized phosphoproteomics as a general approach for investigating the signal transduction underlying complex biology.

AB - Protein phosphorylation dynamically integrates environmental and cellular information to control biological processes. Identifying functional phosphorylation amongst the thousands of phosphosites regulated by a perturbation at a global scale is a major challenge. Here we introduce 'personalized phosphoproteomics', a combination of experimental and computational analyses to link signaling with biological function by utilizing human phenotypic variance. We measure individual subject phosphoproteome responses to interventions with corresponding phenotypes measured in parallel. Applying this approach to investigate how exercise potentiates insulin signaling in human skeletal muscle, we identify both known and previously unidentified phosphosites on proteins involved in glucose metabolism. This includes a cooperative relationship between mTOR and AMPK whereby the former directly phosphorylates the latter on S377, for which we find a role in metabolic regulation. These results establish personalized phosphoproteomics as a general approach for investigating the signal transduction underlying complex biology.

U2 - 10.1038/s41587-021-01099-9

DO - 10.1038/s41587-021-01099-9

M3 - Journal article

C2 - 34857927

VL - 40

SP - 576

EP - 584

JO - Nature Biotechnology

JF - Nature Biotechnology

SN - 1087-0156

IS - 4

ER -

ID: 286424076