The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
5′‐AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP‐activated protein kinase. Studies using bacterially expressed human protein phosphatase‐2C α and native bovine protein phosphatase‐2A c
Abstract
Human protein phosphatase-2C alpha (PP2C alpha) was purified to homogeneity after expression in Escherichia coli. AMP inhibited the dephosphorylation of AMP-activated protein kinase (AMPK), but not phosphocasein, by PP2C alpha. The concentration dependence and the effects of other nucleotides (ATP and formycin A-5'-monophosphate) suggest that AMP acts by binding to the same site which causes direct allosteric activation of AMPK. A similar, although less pronounced, effect was observed with another protein phosphatase (PP2AC). We have now shown that AMPK activates the AMPK cascade by four mechanisms, which should make the system exquisitely sensitive to changes in AMP concentration.
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“Activation loop phosphorylation increases AMPK activity by about 100-fold, while allosteric regulation changes AMPK activity up to tenfold in mammalian cells and about twofold in recombinant, bacterially produced AMPK [26,28,38,39].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [39]
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Cites
Corton, J. M., Gillespie, J. G., Hawley, S. A., & Hardie, D. G. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20498.x · Cited by 1,232
Serine/threonine protein phosphatases
Wera, S., & Hemmings, B. A. (1995) · Biochemical Journal · doi:10.1042/bj3110017 · Cited by 638
Muchmore, D. C., McIntosh, L. P., Russell, C., Anderson, D. E., & Dahlquist, F. W. (1989) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(89)77005-1 · Cited by 454
Hawley, S. A., Selbert, M. A., Goldstein, E. G., Edelman, A. M., Carling, D., & Hardie, D. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.27186 · Cited by 441
DAVIES, S. P., Carling, D., & Hardie, D. G. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb15185.x · Cited by 431
Role of the AMP-activated protein kinase in the cellular stress response
Corton, J. M., Gillespie, J. G., & Hardie, D. G. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00070-1 · Cited by 423
Purification and characterization of the AMP‐activated protein kinase
Carling, D., Clarke, P. R., Zammit, V. A., & Hardie, D. G. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb15186.x · Cited by 418
[37] Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle
Cohen, P., Alemany, S., Therese, B. A., Resink, J., Strålfors, P., & Tung, H. Y. L. (1988) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(88)59039-0 · Cited by 411
Woods, A., Munday, M. R., Scott, J., Yang, X., Carlson, M., & Carling, D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32198-1 · Cited by 409
Mitchelhill, K. I., Stapleton, D., Gao, G., House, C. M., Michell, B. J., Katsis, F., Witters, L. A., & Kemp, B. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41951-x · Cited by 338
Research works printed but not linked: 3
- 10.1111/j.1432-1033.1995.0558k.x · DOI
- Clarke P.R., 1991, Adv. Protein Phosphatases, 6, 187
- MacKintosh C. (1993) in: (Hardie D.G. eds.) pp. 214–216. Oxford University Press Oxford.
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Items 601–606 of 606
Ovens, A. J., Khabib, M. N. H., Yu, D., Ling, N. X. Y., Smiles, W. J., Hoque, A., Onda, D. A., Goycoolea, A. C. P., Cao, M., Zhang, G. X. Y., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.16.744724
The AMPK signaling pathway in cell metabolism and human diseases
Zhang, Z., Gu, Y., He, H., Qiao, S., Shao, Y., 龙先铭, Huang, J., Zhang, L., & Zhou, F. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02790-6
BindingDB (2018) · UC San Diego · doi:10.7270/q2pz5brc
Characterization of the LKB1-MO25-STRAD AMPKK Complex in Adult Mouse Skeletal Muscle
Smith, C. D. (2010) · ScholarsArchive (Brigham Young University)
The Effects of Excess Corticosterone on LKB1 and AMPK Signaling in Skeletal Muscle of Rats
Nakken, G. N. (2008) · ScholarsArchive (Brigham Young University)
Mechanism underlying the anticontractile effect of perivascular adipose tissue
Dong, Y. (2014) · Research Explorer (The University of Manchester)
Metadata
- Authors
- Davies, S. P., Helps, N. R., Cohen, P., & Hardie, D. G.
- Affiliations
- University of Dundee (GB)
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1995-12-27
- Volume
- 377
- Issue
- 3
- Pages
- 421-425
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2030636484
- Cited by
- 595
- References
- 19
- Citations by year
- 2026: 7 · 2025: 6 · 2024: 18 · 2023: 11 · 2022: 16 · 2021: 25 · 2020: 23 · 2019: 17 · 2018: 21 · 2017: 28 · 2016: 25 · 2015: 30 · 2014: 36 · 2013: 32 · 2012: 35
- FWCI
- 3.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- AMPK, AMP, dephosphorylation, phosphorylation, allosteric activation, nucleotide binding, formycin A, energy homeostasis
- MeSH terms
- Protein Phosphatase 2C, Adenosine Monophosphate, Allosteric Regulation, Animals, Base Sequence, Cattle, Dose-Response Relationship, Drug, Enzyme Activation, Escherichia coli, Humans, Isoenzymes, Models, Biological, Molecular Sequence Data, Multienzyme Complexes, Nucleotides, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Recombinant Proteins, Signal Transduction, Protein Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins, Protein Phosphatase 2, AMP-Activated Protein Kinases
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