Potential role of TBC1D4 in enhanced post-exercise insulin action in human skeletal muscle. (Q36767833)

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22 January 2020

title

Potential role of TBC1D4 in enhanced post-exercise insulin action in human skeletal muscle (English)

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22 January 2020

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1

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22 January 2020

Carol MacKintosh

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22 January 2020

Juleen Zierath

8

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22 January 2020

Grahame Hardie

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22 January 2020

Bente Kiens

10

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22 January 2020

Erik A Richter

11

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22 January 2020

Henriette Pilegaard

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22 January 2020

Jørgen Wojtaszewski

13

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22 January 2020

author name string

C Frøsig

2

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22 January 2020

C Pehmøller

3

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22 January 2020

S Chen

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22 January 2020

S J Maarbjerg

5

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N Brandt

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publication date

28 February 2009

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22 January 2020

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22 January 2020

volume

52

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22 January 2020

issue

5

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22 January 2020

page(s)

891-900

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https://scigraph.springernature.com/pub.10.1007/s00125-009-1294-y

22 January 2020

exact match

0 references

cites work

Resistance exercise increases human skeletal muscle AS160/TBC1D4 phosphorylation in association with enhanced leg glucose uptake during postexercise recovery.

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Discovery of TBC1D1 as an insulin-, AICAR-, and contraction-stimulated signaling nexus in mouse skeletal muscle.

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Inhibition of GLUT4 translocation by Tbc1d1, a Rab GTPase-activating protein abundant in skeletal muscle, is partially relieved by AMP-activated protein kinase activation

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Effects of endurance exercise training on insulin signaling in human skeletal muscle: interactions at the level of phosphatidylinositol 3-kinase, Akt, and AS160.

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AS160 phosphorylation is associated with activation of alpha2beta2gamma1- but not alpha2beta2gamma3-AMPK trimeric complex in skeletal muscle during exercise in humans

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Interaction of the Akt substrate, AS160, with the glucose transporter 4 vesicle marker protein, insulin-regulated aminopeptidase

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AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain

29 September 2017

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Insulin-stimulated phosphorylation of the Akt substrate AS160 is impaired in skeletal muscle of type 2 diabetic subjects

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A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain

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Distribution of the lactate/H+ transporter isoforms MCT1 and MCT4 in human skeletal muscle

29 September 2017

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Muscle glucose metabolism following exercise in the rat: increased sensitivity to insulin

29 September 2017

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29 September 2017

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29 September 2017

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5 September 2018

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5 September 2018

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5 September 2018

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5 September 2018

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5 September 2018

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5 September 2018

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Increased phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle in response to insulin or contractile activity

5 September 2018

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5 September 2018

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Exercise improves phosphatidylinositol-3,4,5-trisphosphate responsiveness of atypical protein kinase C and interacts with insulin signalling to peptide elongation in human skeletal muscle

5 September 2018

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20 October 2018

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20 October 2018

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20 October 2018

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AMPK-Mediated AS160 Phosphorylation in Skeletal Muscle Is Dependent on AMPK Catalytic and Regulatory Subunits

20 October 2018

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Prior exercise increases phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle

4 December 2018

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12 December 2020

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12 December 2020

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12 December 2020

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Increased GLUT-4 translocation mediates enhanced insulin sensitivity of muscle glucose transport after exercise

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Exercise-Induced Phosphorylation of the Novel Akt Substrates AS160 and Filamin A in Human Skeletal Muscle

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12 December 2020

Distinct signals regulate AS160 phosphorylation in response to insulin, AICAR, and contraction in mouse skeletal muscle

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12 December 2020

10.1007/S00125-009-1294-Y

Identifiers

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22 January 2020

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22 January 2020

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