Acute exercise and physiological insulin induce distinct phosphorylation signatures on TBC1D1 and TBC1D4 in human skeletal muscle

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Standard

Acute exercise and physiological insulin induce distinct phosphorylation signatures on TBC1D1 and TBC1D4 in human skeletal muscle. / Treebak, Jonas Thue; Pehmøller, Christian; Kristensen, Jonas Møller; Kjøbsted, Rasmus; Birk, Jesper Bratz; Schjerling, Peter; Richter, Erik A.; Goodyear, Laurie J; Wojtaszewski, Jørgen.

I: Journal of Physiology, Bind 592, Nr. 2, 2014, s. 351-375.

Publikation: Bidrag til tidsskriftTidsskriftartikelfagfællebedømt

Harvard

Treebak, JT, Pehmøller, C, Kristensen, JM, Kjøbsted, R, Birk, JB, Schjerling, P, Richter, EA, Goodyear, LJ & Wojtaszewski, J 2014, 'Acute exercise and physiological insulin induce distinct phosphorylation signatures on TBC1D1 and TBC1D4 in human skeletal muscle', Journal of Physiology, bind 592, nr. 2, s. 351-375. https://doi.org/10.1113/jphysiol.2013.266338

APA

Treebak, J. T., Pehmøller, C., Kristensen, J. M., Kjøbsted, R., Birk, J. B., Schjerling, P., Richter, E. A., Goodyear, L. J., & Wojtaszewski, J. (2014). Acute exercise and physiological insulin induce distinct phosphorylation signatures on TBC1D1 and TBC1D4 in human skeletal muscle. Journal of Physiology, 592(2), 351-375. https://doi.org/10.1113/jphysiol.2013.266338

Vancouver

Treebak JT, Pehmøller C, Kristensen JM, Kjøbsted R, Birk JB, Schjerling P o.a. Acute exercise and physiological insulin induce distinct phosphorylation signatures on TBC1D1 and TBC1D4 in human skeletal muscle. Journal of Physiology. 2014;592(2):351-375. https://doi.org/10.1113/jphysiol.2013.266338

Author

Treebak, Jonas Thue ; Pehmøller, Christian ; Kristensen, Jonas Møller ; Kjøbsted, Rasmus ; Birk, Jesper Bratz ; Schjerling, Peter ; Richter, Erik A. ; Goodyear, Laurie J ; Wojtaszewski, Jørgen. / Acute exercise and physiological insulin induce distinct phosphorylation signatures on TBC1D1 and TBC1D4 in human skeletal muscle. I: Journal of Physiology. 2014 ; Bind 592, Nr. 2. s. 351-375.

Bibtex

@article{afe294ebe3be44fe9950720eee0a7b94,
title = "Acute exercise and physiological insulin induce distinct phosphorylation signatures on TBC1D1 and TBC1D4 in human skeletal muscle",
abstract = "We investigated the phosphorylation signatures of two Rab GTPase activating proteins TBC1D1 and TBC1D4 in human skeletal muscle in response to physical exercise and physiological insulin levels induced by a carbohydrate rich meal using a paired experimental design. Eight healthy male volunteers exercised in the fasted or fed state and muscle biopsies were taken before and immediately after exercise. We identified TBC1D1/4 sites that did not respond to either exercise or insulin (TBC1D4: S666), that responded to insulin only (TBC1D4: S318), that responded to exercise only (TBC1D1: S237, S660, S700; TBC1D4: S588, S751), and that responded to both insulin and exercise (TBC1D1: T596; TBC1D4: S341, T642, S704). In the insulin stimulated leg, Akt phosphorylation on both T308 and S473 correlated significantly with multiple sites on both TBC1D1 (T596) and TBC1D4 (S318, S341, S704). Interestingly, in the exercised leg in the fasted state TBC1D1 phosphorylation (S237, T596) correlated significantly with the activity of the α2β2γ3 AMPK trimer, whereas TBC1D4 phosphorylation (S341, S704) correlated with the activity of the α2β2γ1 AMPK trimer. Our data show differential phosphorylation of TBC1D1 and TBC1D4 in response to physiological stimuli in human skeletal muscle and support the idea that Akt and AMPK are upstream kinases. TBC1D1 phosphorylation signatures were comparable between in vitro contracted mouse skeletal muscle and exercised human muscle, and we show that AMPK was regulating phosphorylation of these sites in mouse muscle. Contraction and exercise elicited a different phosphorylation pattern of TBC1D4 in mouse compared with human muscle, and although different circumstances in our experimental setup may contribute to this difference, the observation exemplifies that transferring findings between species are difficult.",
author = "Treebak, {Jonas Thue} and Christian Pehm{\o}ller and Kristensen, {Jonas M{\o}ller} and Rasmus Kj{\o}bsted and Birk, {Jesper Bratz} and Peter Schjerling and Richter, {Erik A.} and Goodyear, {Laurie J} and J{\o}rgen Wojtaszewski",
note = "CURIS 2014 NEXS 012",
year = "2014",
doi = "10.1113/jphysiol.2013.266338",
language = "English",
volume = "592",
pages = "351--375",
journal = "The Journal of Physiology",
issn = "0022-3751",
publisher = "Wiley-Blackwell",
number = "2",

}

RIS

TY - JOUR

T1 - Acute exercise and physiological insulin induce distinct phosphorylation signatures on TBC1D1 and TBC1D4 in human skeletal muscle

AU - Treebak, Jonas Thue

AU - Pehmøller, Christian

AU - Kristensen, Jonas Møller

AU - Kjøbsted, Rasmus

AU - Birk, Jesper Bratz

AU - Schjerling, Peter

AU - Richter, Erik A.

AU - Goodyear, Laurie J

AU - Wojtaszewski, Jørgen

N1 - CURIS 2014 NEXS 012

PY - 2014

Y1 - 2014

N2 - We investigated the phosphorylation signatures of two Rab GTPase activating proteins TBC1D1 and TBC1D4 in human skeletal muscle in response to physical exercise and physiological insulin levels induced by a carbohydrate rich meal using a paired experimental design. Eight healthy male volunteers exercised in the fasted or fed state and muscle biopsies were taken before and immediately after exercise. We identified TBC1D1/4 sites that did not respond to either exercise or insulin (TBC1D4: S666), that responded to insulin only (TBC1D4: S318), that responded to exercise only (TBC1D1: S237, S660, S700; TBC1D4: S588, S751), and that responded to both insulin and exercise (TBC1D1: T596; TBC1D4: S341, T642, S704). In the insulin stimulated leg, Akt phosphorylation on both T308 and S473 correlated significantly with multiple sites on both TBC1D1 (T596) and TBC1D4 (S318, S341, S704). Interestingly, in the exercised leg in the fasted state TBC1D1 phosphorylation (S237, T596) correlated significantly with the activity of the α2β2γ3 AMPK trimer, whereas TBC1D4 phosphorylation (S341, S704) correlated with the activity of the α2β2γ1 AMPK trimer. Our data show differential phosphorylation of TBC1D1 and TBC1D4 in response to physiological stimuli in human skeletal muscle and support the idea that Akt and AMPK are upstream kinases. TBC1D1 phosphorylation signatures were comparable between in vitro contracted mouse skeletal muscle and exercised human muscle, and we show that AMPK was regulating phosphorylation of these sites in mouse muscle. Contraction and exercise elicited a different phosphorylation pattern of TBC1D4 in mouse compared with human muscle, and although different circumstances in our experimental setup may contribute to this difference, the observation exemplifies that transferring findings between species are difficult.

AB - We investigated the phosphorylation signatures of two Rab GTPase activating proteins TBC1D1 and TBC1D4 in human skeletal muscle in response to physical exercise and physiological insulin levels induced by a carbohydrate rich meal using a paired experimental design. Eight healthy male volunteers exercised in the fasted or fed state and muscle biopsies were taken before and immediately after exercise. We identified TBC1D1/4 sites that did not respond to either exercise or insulin (TBC1D4: S666), that responded to insulin only (TBC1D4: S318), that responded to exercise only (TBC1D1: S237, S660, S700; TBC1D4: S588, S751), and that responded to both insulin and exercise (TBC1D1: T596; TBC1D4: S341, T642, S704). In the insulin stimulated leg, Akt phosphorylation on both T308 and S473 correlated significantly with multiple sites on both TBC1D1 (T596) and TBC1D4 (S318, S341, S704). Interestingly, in the exercised leg in the fasted state TBC1D1 phosphorylation (S237, T596) correlated significantly with the activity of the α2β2γ3 AMPK trimer, whereas TBC1D4 phosphorylation (S341, S704) correlated with the activity of the α2β2γ1 AMPK trimer. Our data show differential phosphorylation of TBC1D1 and TBC1D4 in response to physiological stimuli in human skeletal muscle and support the idea that Akt and AMPK are upstream kinases. TBC1D1 phosphorylation signatures were comparable between in vitro contracted mouse skeletal muscle and exercised human muscle, and we show that AMPK was regulating phosphorylation of these sites in mouse muscle. Contraction and exercise elicited a different phosphorylation pattern of TBC1D4 in mouse compared with human muscle, and although different circumstances in our experimental setup may contribute to this difference, the observation exemplifies that transferring findings between species are difficult.

U2 - 10.1113/jphysiol.2013.266338

DO - 10.1113/jphysiol.2013.266338

M3 - Journal article

C2 - 24247980

VL - 592

SP - 351

EP - 375

JO - The Journal of Physiology

JF - The Journal of Physiology

SN - 0022-3751

IS - 2

ER -

ID: 87309430