The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism
Open accessAbstract
In mammals, an AMP-activated protein kinase (AMPK) phosphorylates both acetyl-CoA carboxylase and 3-hydroxy-3-methylglutaryl-CoA reductase in vitro and has been proposed to play a major role in the regulation of lipid metabolism in vivo. We report here the primary sequence of rat AMPK and show that antibodies raised against synthetic peptides based on the deduced sequence of AMPK immunoprecipitate AMPK activity from rat liver extracts. AMPK has a remarkable degree of sequence identity to the proteins encoded by the yeast SNF1 gene and the plant RKIN1 gene. SNF1 protein kinase activity is essential for release of genes from glucose repression in Saccharomyces cerevisiae. Expression of cRKIN1 in yeast snf1 mutants restores SNF1 function. These results indicate that AMPK, SNF1, and RKIN1 form part of a family of protein kinases that have been highly conserved throughout evolution. Our results suggest that AMPK may be involved in the regulation of a wide range of metabolic pathways.
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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
Steinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,637
The AMP‐Activated Protein Kinase: Fuel Gauge of the Mammalian Cell?
Hardie, D. G., & Carling, D. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00259.x · Cited by 1,317
Self-citationHawley, S. A., Davison, M., Woods, A., Davies, S. P., Beri, R. K., Carling, D., & Hardie, D. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27879 · Cited by 1,264
Self-citationGuo, S., & Kemphues, K. J. (1995) · Cell · doi:10.1016/0092-8674(95)90082-9 · Cited by 1,122
Zong, H., Ren, J. M., Young, L. H., Pypaert, M., Mu, J., Birnbaum, M. J., & Shulman, G. I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252625599 · Cited by 1,036
Metadata
- Authors
- Carling, D., Aguan, K., Woods, A., Verhoeven, A. J., Beri, R. K., Brennan, C. H., Sidebottom, C., Davison, M. D., & Scott, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1994-04
- Volume
- 269
- Issue
- 15
- Pages
- 11442-11448
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1531537085
- Cited by
- 252
- References
- 1
- FWCI
- 7.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Carling, D., Aguan, K., Woods, A., Verhoeven, A. J., Beri, R. K., Brennan, C. H., Sidebottom, C., Davison, M. D., & Scott, J. (1994). Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)78143-5
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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