Journal
EMBO JOURNAL
Volume 19, Issue 23, Pages 6371-6381Publisher
OXFORD UNIV PRESS
DOI: 10.1093/emboj/19.23.6371
Keywords
adenylate kinase; creatine kinase; energy homeostasis; knockout mice; phosphoryl transfer
Categories
Funding
- NHLBI NIH HHS [T32 HL007111, R01 HL064822, HL64822, HL07111] Funding Source: Medline
- NIAMS NIH HHS [R37 AR021617, R01 AR021617, AR21617] Funding Source: Medline
Ask authors/readers for more resources
Efficient cellular energy homeostasis is a critical determinant of muscle performance, providing evolutionary advantages responsible for species survival. Phosphotransfer reactions, which couple ATP production and utilization, are thought to play a central role in this process. Here, we provide evidence that genetic disruption of AK1-catalyzed beta -phosphoryl transfer in mice decreases the potential of myofibers to sustain nucleotide ratios despite up-regulation of high-energy phosphoryl flux through glycolytic, guanylate and creatine kinase phosphotransfer pathways. A maintained contractile performance of AK1-deficient muscles was associated with higher ATP turnover rate and larger amounts of ATP consumed per contraction. Metabolic stress further aggravated the energetic cost in AK1(-/-) muscles. Thus, AK1-catalyzed phosphotransfer is essential in the maintenance of cellular energetic economy, enabling skeletal muscle to perform at the lowest metabolic cost.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available