CaMKK2 is not involved in contraction-stimulated AMPK activation and glucose uptake in skeletal muscle

Negoita, Florentina; Addinsall, Alex B.; Hellberg, Kristina; Bringas, Conchita Fraguas; Hafen, Paul S.; Sermersheim, Tyler J.; Agerholm, Marianne; Lewis, Christopher T. A.; Ahwazi, Danial; Ling, Naomi X.Y.; Larsen, Jeppe K.; Deshmukh, Atul S.; Hossain, Mohammad Anwar; Oakhill, Jonathan S.; Ochala, Julien; Brault, Jeffrey J.; Sankar, Uma; Drewry, David H.; Scott, John W.; Witczak, Carol A.; Sakamoto, Kei

doi:10.1016/j.molmet.2023.101761

Cited by 9 publications

(1 citation statement)

References 60 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, these data were not generated in skeletal muscle cells and recent findings demonstrate that CaMKK2 does not activate AMPK in skeletal muscle in mice. It is more likely that the positive outcomes in earlier studies were due to off-target impact of frequently used CaMKK inhibitors, rather than CaMKK playing a role in AMPK activation in muscle [44].…”

Section: Ampk Is Sufficient But Not Necessary For the Regulation Of T...mentioning

confidence: 99%

AMPK and Beyond: The Signaling Network Controlling RabGAPs and Contraction-Mediated Glucose Uptake in Skeletal Muscle

Peifer-Weiß,

Al-Hasani,

Chadt

2024

IJMS

View full text Add to dashboard Cite

Impaired skeletal muscle glucose uptake is a key feature in the development of insulin resistance and type 2 diabetes. Skeletal muscle glucose uptake can be enhanced by a variety of different stimuli, including insulin and contraction as the most prominent. In contrast to the clearance of glucose from the bloodstream in response to insulin stimulation, exercise-induced glucose uptake into skeletal muscle is unaffected during the progression of insulin resistance, placing physical activity at the center of prevention and treatment of metabolic diseases. The two Rab GTPase-activating proteins (RabGAPs), TBC1D1 and TBC1D4, represent critical nodes at the convergence of insulin- and exercise-stimulated signaling pathways, as phosphorylation of the two closely related signaling factors leads to enhanced translocation of glucose transporter 4 (GLUT4) to the plasma membrane, resulting in increased cellular glucose uptake. However, the full network of intracellular signaling pathways that control exercise-induced glucose uptake and that overlap with the insulin-stimulated pathway upstream of the RabGAPs is not fully understood. In this review, we discuss the current state of knowledge on exercise- and insulin-regulated kinases, hypoxia, nitric oxide (NO) and bioactive lipids that may be involved in the regulation of skeletal muscle glucose uptake.

show abstract

Section: Ampk Is Sufficient But Not Necessary For the Regulation Of T...mentioning

confidence: 99%

AMPK and Beyond: The Signaling Network Controlling RabGAPs and Contraction-Mediated Glucose Uptake in Skeletal Muscle

Peifer-Weiß,

Al-Hasani,

Chadt

2024

IJMS

View full text Add to dashboard Cite

show abstract

USP10 alleviates Nε-carboxymethyl-lysine-induced vascular calcification and atherogenesis in diabetes mellitus by promoting AMPK activation

Mushajiang,

Li,

Sun

et al. 2024

Cellular Signalling

View full text Add to dashboard Cite

PyLKB1 regulates glucose transport via activating PyAMPKα in Yesso Scallop Patinopecten yessoensis under high temperature stress

Jiang,

Yang,

et al. 2024

Developmental & Comparative Immunology

View full text Add to dashboard Cite

CaMKK2 is not involved in contraction-stimulated AMPK activation and glucose uptake in skeletal muscle

Cited by 9 publications

References 60 publications

AMPK and Beyond: The Signaling Network Controlling RabGAPs and Contraction-Mediated Glucose Uptake in Skeletal Muscle

AMPK and Beyond: The Signaling Network Controlling RabGAPs and Contraction-Mediated Glucose Uptake in Skeletal Muscle

USP10 alleviates Nε-carboxymethyl-lysine-induced vascular calcification and atherogenesis in diabetes mellitus by promoting AMPK activation

PyLKB1 regulates glucose transport via activating PyAMPKα in Yesso Scallop Patinopecten yessoensis under high temperature stress

Contact Info

Product

Resources

About