Phosphoproteomics reveals conserved exercise-stimulated signaling and AMPK regulation of store-operated calcium entry

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

Standard

Phosphoproteomics reveals conserved exercise-stimulated signaling and AMPK regulation of store-operated calcium entry. / Nelson, Marin E; Parker, Benjamin L; Burchfield, James G; Hoffman, Nolan J; Needham, Elise J; Cooke, Kristen C; Naim, Timur; Sylow, Lykke; Ling, Naomi X Y; Francis, Deanne; Norris, Dougall M; Chaudhuri, Rima; Oakhill, Jonathan S; Richter, Erik A; Lynch, Gordon S; Stöckli, Jacqueline; James, David E.

In: E M B O Journal, Vol. 38, No. 24, e102578, 2019.

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

Harvard

Nelson, ME, Parker, BL, Burchfield, JG, Hoffman, NJ, Needham, EJ, Cooke, KC, Naim, T, Sylow, L, Ling, NXY, Francis, D, Norris, DM, Chaudhuri, R, Oakhill, JS, Richter, EA, Lynch, GS, Stöckli, J & James, DE 2019, 'Phosphoproteomics reveals conserved exercise-stimulated signaling and AMPK regulation of store-operated calcium entry', E M B O Journal, vol. 38, no. 24, e102578. https://doi.org/10.15252/embj.2019102578, https://doi.org/10.15252/embj.2019104246

APA

Nelson, M. E., Parker, B. L., Burchfield, J. G., Hoffman, N. J., Needham, E. J., Cooke, K. C., Naim, T., Sylow, L., Ling, N. X. Y., Francis, D., Norris, D. M., Chaudhuri, R., Oakhill, J. S., Richter, E. A., Lynch, G. S., Stöckli, J., & James, D. E. (2019). Phosphoproteomics reveals conserved exercise-stimulated signaling and AMPK regulation of store-operated calcium entry. E M B O Journal, 38(24), [e102578]. https://doi.org/10.15252/embj.2019102578, https://doi.org/10.15252/embj.2019104246

Vancouver

Nelson ME, Parker BL, Burchfield JG, Hoffman NJ, Needham EJ, Cooke KC et al. Phosphoproteomics reveals conserved exercise-stimulated signaling and AMPK regulation of store-operated calcium entry. E M B O Journal. 2019;38(24). e102578. https://doi.org/10.15252/embj.2019102578, https://doi.org/10.15252/embj.2019104246

Author

Nelson, Marin E ; Parker, Benjamin L ; Burchfield, James G ; Hoffman, Nolan J ; Needham, Elise J ; Cooke, Kristen C ; Naim, Timur ; Sylow, Lykke ; Ling, Naomi X Y ; Francis, Deanne ; Norris, Dougall M ; Chaudhuri, Rima ; Oakhill, Jonathan S ; Richter, Erik A ; Lynch, Gordon S ; Stöckli, Jacqueline ; James, David E. / Phosphoproteomics reveals conserved exercise-stimulated signaling and AMPK regulation of store-operated calcium entry. In: E M B O Journal. 2019 ; Vol. 38, No. 24.

Bibtex

@article{9db04df60bcd4f09b688005216112631,
title = "Phosphoproteomics reveals conserved exercise-stimulated signaling and AMPK regulation of store-operated calcium entry",
abstract = "Exercise stimulates cellular and physiological adaptations that are associated with widespread health benefits. To uncover conserved protein phosphorylation events underlying this adaptive response, we performed mass spectrometry-based phosphoproteomic analyses of skeletal muscle from two widely used rodent models: treadmill running in mice and in situ muscle contraction in rats. We overlaid these phosphoproteomic signatures with cycling in humans to identify common cross-species phosphosite responses, as well as unique model-specific regulation. We identified > 22,000 phosphosites, revealing orthologous protein phosphorylation and overlapping signaling pathways regulated by exercise. This included two conserved phosphosites on stromal interaction molecule 1 (STIM1), which we validate as AMPK substrates. Furthermore, we demonstrate that AMPK-mediated phosphorylation of STIM1 negatively regulates store-operated calcium entry, and this is beneficial for exercise in Drosophila. This integrated cross-species resource of exercise-regulated signaling in human, mouse, and rat skeletal muscle has uncovered conserved networks and unraveled crosstalk between AMPK and intracellular calcium flux.",
keywords = "Faculty of Science, AMPK, Calcium, Exercise, Phosphorylation, STIM1",
author = "Nelson, {Marin E} and Parker, {Benjamin L} and Burchfield, {James G} and Hoffman, {Nolan J} and Needham, {Elise J} and Cooke, {Kristen C} and Timur Naim and Lykke Sylow and Ling, {Naomi X Y} and Deanne Francis and Norris, {Dougall M} and Rima Chaudhuri and Oakhill, {Jonathan S} and Richter, {Erik A} and Lynch, {Gordon S} and Jacqueline St{\"o}ckli and James, {David E}",
note = "CURIS 2019 NEXS 262 {\textcopyright} 2019 The Authors.",
year = "2019",
doi = "10.15252/embj.2019102578",
language = "English",
volume = "38",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "24",

}

RIS

TY - JOUR

T1 - Phosphoproteomics reveals conserved exercise-stimulated signaling and AMPK regulation of store-operated calcium entry

AU - Nelson, Marin E

AU - Parker, Benjamin L

AU - Burchfield, James G

AU - Hoffman, Nolan J

AU - Needham, Elise J

AU - Cooke, Kristen C

AU - Naim, Timur

AU - Sylow, Lykke

AU - Ling, Naomi X Y

AU - Francis, Deanne

AU - Norris, Dougall M

AU - Chaudhuri, Rima

AU - Oakhill, Jonathan S

AU - Richter, Erik A

AU - Lynch, Gordon S

AU - Stöckli, Jacqueline

AU - James, David E

N1 - CURIS 2019 NEXS 262 © 2019 The Authors.

PY - 2019

Y1 - 2019

N2 - Exercise stimulates cellular and physiological adaptations that are associated with widespread health benefits. To uncover conserved protein phosphorylation events underlying this adaptive response, we performed mass spectrometry-based phosphoproteomic analyses of skeletal muscle from two widely used rodent models: treadmill running in mice and in situ muscle contraction in rats. We overlaid these phosphoproteomic signatures with cycling in humans to identify common cross-species phosphosite responses, as well as unique model-specific regulation. We identified > 22,000 phosphosites, revealing orthologous protein phosphorylation and overlapping signaling pathways regulated by exercise. This included two conserved phosphosites on stromal interaction molecule 1 (STIM1), which we validate as AMPK substrates. Furthermore, we demonstrate that AMPK-mediated phosphorylation of STIM1 negatively regulates store-operated calcium entry, and this is beneficial for exercise in Drosophila. This integrated cross-species resource of exercise-regulated signaling in human, mouse, and rat skeletal muscle has uncovered conserved networks and unraveled crosstalk between AMPK and intracellular calcium flux.

AB - Exercise stimulates cellular and physiological adaptations that are associated with widespread health benefits. To uncover conserved protein phosphorylation events underlying this adaptive response, we performed mass spectrometry-based phosphoproteomic analyses of skeletal muscle from two widely used rodent models: treadmill running in mice and in situ muscle contraction in rats. We overlaid these phosphoproteomic signatures with cycling in humans to identify common cross-species phosphosite responses, as well as unique model-specific regulation. We identified > 22,000 phosphosites, revealing orthologous protein phosphorylation and overlapping signaling pathways regulated by exercise. This included two conserved phosphosites on stromal interaction molecule 1 (STIM1), which we validate as AMPK substrates. Furthermore, we demonstrate that AMPK-mediated phosphorylation of STIM1 negatively regulates store-operated calcium entry, and this is beneficial for exercise in Drosophila. This integrated cross-species resource of exercise-regulated signaling in human, mouse, and rat skeletal muscle has uncovered conserved networks and unraveled crosstalk between AMPK and intracellular calcium flux.

KW - Faculty of Science

KW - AMPK

KW - Calcium

KW - Exercise

KW - Phosphorylation

KW - STIM1

U2 - 10.15252/embj.2019102578

DO - 10.15252/embj.2019102578

M3 - Journal article

C2 - 31381180

VL - 38

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 24

M1 - e102578

ER -

ID: 225956874