Cited by 109Autophagy in Disease and TherapyMuscle Physiology and DisordersMuscle metabolism and nutrition

Physical exercise increases autophagic signaling through ULK1 in human skeletal muscle

Møller, Andreas Buch, Vendelbo, Mikkel Holm, Christensen, Britt, Clasen, Berthil Forrest, Bak, Ann Mosegaard, Jørgensen, Jens O. L., Møller, Niels, Jessen, Niels·2015·Journal of Applied Physiology

Abstract

Data from transgenic animal models suggest that exercise-induced autophagy is critical for adaptation to physical training, and that Unc-51 like kinase-1 (ULK1) serves as an important regulator of autophagy. Phosphorylation of ULK1 at Ser 555 stimulates autophagy, whereas phosphorylation at Ser 757 is inhibitory. To determine whether exercise regulates ULK1 phosphorylation in humans in vivo in a nutrient-dependent manner, we examined skeletal muscle biopsies from healthy humans after 1-h cycling exercise at 50% maximal O 2 uptake on two occasions: 1) during a 36-h fast, and 2) during continuous glucose infusion at 0.2 kg/h. Physical exercise increased ULK1 phosphorylation at Ser 555 and decreased lipidation of light chain 3B. ULK1 phosphorylation at Ser 555 correlated positively with AMP-activated protein kinase-α Thr 172 phosphorylation and negatively with light chain 3B lipidation. ULK1 phosphorylation at Ser 757 was not affected by exercise. Fasting increased ULK1 and p62 protein expression, but did not affect exercise-induced ULK1 phosphorylation. These data demonstrate that autophagy signaling is activated in human skeletal muscle after 60 min of exercise, independently of nutritional status, and suggest that initiation of autophagy constitutes an important physiological response to exercise in humans.

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Crossref · 10.1152/japplphysiol.01116.2014

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  • Exercise triggers autophagy by activating ULK1 and dissociating BCL2 from BECN1, thereby disinhibiting the initiation complex.

    “Exercise triggers autophagy by activating ULK1 and dissociating BCL2 from BECN1, thereby disinhibiting the initiation complex [484,485].”

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Authors
Møller, A. B., Vendelbo, M. H., Christensen, B., Clasen, B. F., Bak, A. M., Jørgensen, J. O. L., Møller, N., & Jessen, N.
Affiliations
Aarhus University (DK)
Corresponding author
Jessen, Niels
Venue
Journal of Applied Physiology
Published
2015-04-15
Volume
118
Issue
8
Pages
971-979
ISSN
  • 0161-7567 (ISSN-L)
  • 8750-7587
  • 1522-1601
OpenAlex
W2024145500
Cited by
109
References
32
Citations by year
2026: 5 · 2025: 5 · 2024: 10 · 2023: 6 · 2022: 9 · 2021: 11 · 2020: 7 · 2019: 13 · 2018: 11 · 2017: 14 · 2016: 15 · 2015: 3
FWCI
11.24
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Applied Physiology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Danish Councin for Strategic Research
  • Beckett Foundation
  • The Danish PhD Schools for Metabolism and Endocrinology
  • A.P. M�ller Foundation for the Advancement of Medical Science
Topics
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Keywords
ULK1, skeletal muscle, AMPK, fasting, glucose infusion, p62, autophagy initiation
MeSH terms
Autophagy-Related Protein-1 Homolog, Sequestosome-1 Protein, Adult, Autophagy, Blood Glucose, Fasting, Fatty Acids, Nonesterified, Humans, Male, Microtubule-Associated Proteins, Nutritional Status, Phosphorylation, Random Allocation, Exercise, Protein Serine-Threonine Kinases, Muscle, Skeletal, Cross-Over Studies, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, AMP-Activated Protein Kinases, Young Adult, Healthy Volunteers

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