The DOI matches its OpenAlex record; 4 of the 4 references it cites were found in a registry or an index.
The regulation of AMP-activated protein kinase by phosphorylation
Open accessAbstract
The AMP-activated protein kinase (AMPK) cascade is activated by an increase in the AMP/ATP ratio within the cell. AMPK is regulated allosterically by AMP and by reversible phosphorylation. Threonine-172 within the catalytic subunit (alpha) of AMPK (Thr(172)) was identified as the major site phosphorylated by the AMP-activated protein kinase kinase (AMPKK) in vitro. We have used site-directed mutagenesis to study the role of phosphorylation of Thr(172) on AMPK activity. Mutation of Thr(172) to an aspartic acid residue (T172D) in either alpha1 or alpha2 resulted in a kinase complex with approx. 50% the activity of the corresponding wild-type complex. The activity of wild-type AMPK decreased by greater than 90% following treatment with protein phosphatases, whereas the activity of the T172D mutant complex fell by only 10-15%. Mutation of Thr(172) to an alanine residue (T172A) almost completely abolished kinase activity. These results indicate that phosphorylation of Thr(172) accounts for most of the activation by AMPKK, but that other sites are involved. In support of this we have shown that AMPKK phosphorylates at least two other sites on the alpha subunit and one site on the beta subunit. Furthermore, we provide evidence that phosphorylation of Thr(172) may be involved in the sensitivity of the AMPK complex to AMP.
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Cites
Mammalian AMP-activated protein kinase subfamily
Stapleton, D., Mitchelhill, K. I., Gao, G., Widmer, J., Michell, B. J., Teh, T., House, C. M., Fernandez, C. S., Cox, T., Witters, L. A., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.2.611 · Cited by 652
AMP-Activated Protein Kinase: An Ultrasensitive System for Monitoring Cellular Energy Charge
HARDIE, D. G., SALT, I. P., HAWLEY, S. A., & DAVIES, S. P. (1999) · Biochemical Journal · doi:10.1042/bj3380717 · Cited by 362
Carling, D., & Grahame Hardie, D. (1989) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(89)90014-1 · Cited by 296
Self-citation
Cited by
Yamauchi, T., Kamon, J., Minokoshi, Y., Ito, Y., Waki, H., Uchida, S., Yamashita, S., Noda, M., Kita, S., Ueki, K., et al. (2002) · Nature Medicine · doi:10.1038/nm788 · Cited by 4,238
Self-citationTSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
Mechanisms underlying the resistance to diet-induced obesity in germ-free mice
Bäckhed, F., Manchester, J. K., Semenkovich, C. F., & Gordon, J. I. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605374104 · Cited by 2,615
Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
Minokoshi, Y., Kim, Y.-B., Peroni, O. D., Fryer, L. G. D., Müller, C., Carling, D., & Kahn, B. B. (2002) · Nature · doi:10.1038/415339a · Cited by 2,053
Self-citationAMP-activated protein kinase: an energy sensor that regulates all aspects of cell function
Hardie, D. G. (2011) · Genes & Development · doi:10.1101/gad.17420111 · Cited by 1,638
Metadata
- Authors
- STEIN, S. C., Woods, A., Jones, N. A., DAVISON, M. D., & Carling, D.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2000-01-25
- Volume
- 345
- Issue
- 3
- Pages
- 437-443
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1972762474
- Cited by
- 605
- References
- 4
- FWCI
- 6.53
- Type
- journal article
- Language
- en
- Open access
- bronze
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- STEIN, S. C., Woods, A., Jones, N. A., DAVISON, M. D., & Carling, D. (2000). The regulation of AMP-activated protein kinase by phosphorylation. Biochemical Journal. https://doi.org/10.1042/0264-6021%3A3450437
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