Phosphoproteomics of three exercise modalities identifies canonical signaling and C18ORF25 as an AMPK substrate regulating skeletal muscle function

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

Phosphoproteomics of three exercise modalities identifies canonical signaling and C18ORF25 as an AMPK substrate regulating skeletal muscle function. / Blazev, Ronnie; Carl, Christian Strini; Ng, Yaan-Kit; Molendijk, Jeffrey; Voldstedlund, Christian Thomas; Zhao, Yuanyuan; Xiao, Di; Kueh, Andrew J; Miotto, Paula M; Haynes, Vanessa R; Hardee, Justin P; Chung, Jin D; McNamara, James W; Qian, Hongwei; Gregorevic, Paul; Oakhill, Jonathan S; Herold, Marco J; Jensen, Thomas Elbenhardt; Lisowski, Leszek; Lynch, Gordon S; Dodd, Garron T; Watt, Matthew J; Yang, Pengyi; Kiens, Bente; Richter, Erik A.; Parker, Benjamin L.

I: Cell Metabolism, Bind 34, Nr. 10, 2022, s. 1561-1577.e9.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Blazev, R, Carl, CS, Ng, Y-K, Molendijk, J, Voldstedlund, CT, Zhao, Y, Xiao, D, Kueh, AJ, Miotto, PM, Haynes, VR, Hardee, JP, Chung, JD, McNamara, JW, Qian, H, Gregorevic, P, Oakhill, JS, Herold, MJ, Jensen, TE, Lisowski, L, Lynch, GS, Dodd, GT, Watt, MJ, Yang, P, Kiens, B, Richter, EA & Parker, BL 2022, 'Phosphoproteomics of three exercise modalities identifies canonical signaling and C18ORF25 as an AMPK substrate regulating skeletal muscle function', Cell Metabolism, bind 34, nr. 10, s. 1561-1577.e9. https://doi.org/10.1016/j.cmet.2022.07.003

APA

Blazev, R., Carl, C. S., Ng, Y-K., Molendijk, J., Voldstedlund, C. T., Zhao, Y., Xiao, D., Kueh, A. J., Miotto, P. M., Haynes, V. R., Hardee, J. P., Chung, J. D., McNamara, J. W., Qian, H., Gregorevic, P., Oakhill, J. S., Herold, M. J., Jensen, T. E., Lisowski, L., ... Parker, B. L. (2022). Phosphoproteomics of three exercise modalities identifies canonical signaling and C18ORF25 as an AMPK substrate regulating skeletal muscle function. Cell Metabolism, 34(10), 1561-1577.e9. https://doi.org/10.1016/j.cmet.2022.07.003

Vancouver

Blazev R, Carl CS, Ng Y-K, Molendijk J, Voldstedlund CT, Zhao Y o.a. Phosphoproteomics of three exercise modalities identifies canonical signaling and C18ORF25 as an AMPK substrate regulating skeletal muscle function. Cell Metabolism. 2022;34(10):1561-1577.e9. https://doi.org/10.1016/j.cmet.2022.07.003

Author

Blazev, Ronnie ; Carl, Christian Strini ; Ng, Yaan-Kit ; Molendijk, Jeffrey ; Voldstedlund, Christian Thomas ; Zhao, Yuanyuan ; Xiao, Di ; Kueh, Andrew J ; Miotto, Paula M ; Haynes, Vanessa R ; Hardee, Justin P ; Chung, Jin D ; McNamara, James W ; Qian, Hongwei ; Gregorevic, Paul ; Oakhill, Jonathan S ; Herold, Marco J ; Jensen, Thomas Elbenhardt ; Lisowski, Leszek ; Lynch, Gordon S ; Dodd, Garron T ; Watt, Matthew J ; Yang, Pengyi ; Kiens, Bente ; Richter, Erik A. ; Parker, Benjamin L. / Phosphoproteomics of three exercise modalities identifies canonical signaling and C18ORF25 as an AMPK substrate regulating skeletal muscle function. I: Cell Metabolism. 2022 ; Bind 34, Nr. 10. s. 1561-1577.e9.

Bibtex

@article{8021d86f993244ef84e37fba659eff0e,

title = "Phosphoproteomics of three exercise modalities identifies canonical signaling and C18ORF25 as an AMPK substrate regulating skeletal muscle function",

abstract = "Exercise induces signaling networks to improve muscle function and confer health benefits. To identify divergent and common signaling networks during and after different exercise modalities, we performed a phosphoproteomic analysis of human skeletal muscle from a cross-over intervention of endurance, sprint, and resistance exercise. This identified 5,486 phosphosites regulated during or after at least one type of exercise modality and only 420 core phosphosites common to all exercise. One of these core phosphosites was S67 on the uncharacterized protein C18ORF25, which we validated as an AMPK substrate. Mice lacking C18ORF25 have reduced skeletal muscle fiber size, exercise capacity, and muscle contractile function, and this was associated with reduced phosphorylation of contractile and Ca2+ handling proteins. Expression of C18ORF25 S66/67D phospho-mimetic reversed the decreased muscle force production. This work defines the divergent and canonical exercise phosphoproteome across different modalities and identifies C18ORF25 as a regulator of exercise signaling and muscle function.",

keywords = "Faculty of Science, Exercise, Skeletal muscle, Phosphoproteomics, AMPK, C18ORF25, Signaling",

author = "Ronnie Blazev and Carl, {Christian Strini} and Yaan-Kit Ng and Jeffrey Molendijk and Voldstedlund, {Christian Thomas} and Yuanyuan Zhao and Di Xiao and Kueh, {Andrew J} and Miotto, {Paula M} and Haynes, {Vanessa R} and Hardee, {Justin P} and Chung, {Jin D} and McNamara, {James W} and Hongwei Qian and Paul Gregorevic and Oakhill, {Jonathan S} and Herold, {Marco J} and Jensen, {Thomas Elbenhardt} and Leszek Lisowski and Lynch, {Gordon S} and Dodd, {Garron T} and Watt, {Matthew J} and Pengyi Yang and Bente Kiens and Richter, {Erik A.} and Parker, {Benjamin L}",

year = "2022",

doi = "10.1016/j.cmet.2022.07.003",

language = "English",

volume = "34",

pages = "1561--1577.e9",

journal = "Cell Metabolism",

issn = "1550-4131",

publisher = "Cell Press",

number = "10",

}

RIS

TY - JOUR

T1 - Phosphoproteomics of three exercise modalities identifies canonical signaling and C18ORF25 as an AMPK substrate regulating skeletal muscle function

AU - Blazev, Ronnie

AU - Carl, Christian Strini

AU - Ng, Yaan-Kit

AU - Molendijk, Jeffrey

AU - Voldstedlund, Christian Thomas

AU - Zhao, Yuanyuan

AU - Xiao, Di

AU - Kueh, Andrew J

AU - Miotto, Paula M

AU - Haynes, Vanessa R

AU - Hardee, Justin P

AU - Chung, Jin D

AU - McNamara, James W

AU - Qian, Hongwei

AU - Gregorevic, Paul

AU - Oakhill, Jonathan S

AU - Herold, Marco J

AU - Jensen, Thomas Elbenhardt

AU - Lisowski, Leszek

AU - Lynch, Gordon S

AU - Dodd, Garron T

AU - Watt, Matthew J

AU - Yang, Pengyi

AU - Kiens, Bente

AU - Richter, Erik A.

AU - Parker, Benjamin L

PY - 2022

Y1 - 2022

N2 - Exercise induces signaling networks to improve muscle function and confer health benefits. To identify divergent and common signaling networks during and after different exercise modalities, we performed a phosphoproteomic analysis of human skeletal muscle from a cross-over intervention of endurance, sprint, and resistance exercise. This identified 5,486 phosphosites regulated during or after at least one type of exercise modality and only 420 core phosphosites common to all exercise. One of these core phosphosites was S67 on the uncharacterized protein C18ORF25, which we validated as an AMPK substrate. Mice lacking C18ORF25 have reduced skeletal muscle fiber size, exercise capacity, and muscle contractile function, and this was associated with reduced phosphorylation of contractile and Ca2+ handling proteins. Expression of C18ORF25 S66/67D phospho-mimetic reversed the decreased muscle force production. This work defines the divergent and canonical exercise phosphoproteome across different modalities and identifies C18ORF25 as a regulator of exercise signaling and muscle function.

AB - Exercise induces signaling networks to improve muscle function and confer health benefits. To identify divergent and common signaling networks during and after different exercise modalities, we performed a phosphoproteomic analysis of human skeletal muscle from a cross-over intervention of endurance, sprint, and resistance exercise. This identified 5,486 phosphosites regulated during or after at least one type of exercise modality and only 420 core phosphosites common to all exercise. One of these core phosphosites was S67 on the uncharacterized protein C18ORF25, which we validated as an AMPK substrate. Mice lacking C18ORF25 have reduced skeletal muscle fiber size, exercise capacity, and muscle contractile function, and this was associated with reduced phosphorylation of contractile and Ca2+ handling proteins. Expression of C18ORF25 S66/67D phospho-mimetic reversed the decreased muscle force production. This work defines the divergent and canonical exercise phosphoproteome across different modalities and identifies C18ORF25 as a regulator of exercise signaling and muscle function.

KW - Faculty of Science

KW - Exercise

KW - Skeletal muscle

KW - Phosphoproteomics

KW - AMPK

KW - C18ORF25

KW - Signaling

U2 - 10.1016/j.cmet.2022.07.003

DO - 10.1016/j.cmet.2022.07.003

M3 - Journal article

C2 - 35882232

VL - 34

SP - 1561-1577.e9

JO - Cell Metabolism

JF - Cell Metabolism

SN - 1550-4131

IS - 10

ER -

ID: 315181021

Institut for Idræt og Ernæring