Cited by 1,650Metabolism, Diabetes, and CancerPI3K/AKT/mTOR signaling in cancerProtein Kinase Regulation and GTPase Signaling

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LKB1 Is the Upstream Kinase in the AMP-Activated Protein Kinase Cascade

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Woods, Angela, Johnstone, Stephen R., Dickerson, Kristina, Leiper, Fiona C., Fryer, Lee G.D., Neumann, Dietbert, Schlattner, Uwe, Wallimann, Theo, Carlson, Marian, Carling, David·2003·Current Biology

DOI 10.1016/j.cub.2003.10.031

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Abstract

Inactivating mutations in the protein kinase LKB1 lead to a dominantly inherited cancer in humans termed Peutz-Jeghers syndrome. The role of LKB1 is unclear, and only one target for LKB1 has been identified in vivo [3]. AMP-activated protein kinase (AMPK) is the downstream component of a protein kinase cascade that plays a pivotal role in energy homeostasis. AMPK may have a role in protecting the body from metabolic diseases including type 2 diabetes, obesity, and cardiac hypertrophy. We previously reported the identification of three protein kinases (Elm1, Pak1, and Tos3 [9]) that lie upstream of Snf1, the yeast homologue of AMPK. LKB1 shares sequence similarity with Elm1, Pak1, and Tos3, and we demonstrated that LKB1 phosphorylates AMPK on the activation loop threonine (Thr172) within the catalytic subunit and activates AMPK in vitro [9]. Here, we have investigated whether LKB1 corresponds to the major AMPKK activity present in cell extracts. AMPKK purified from rat liver corresponds to LKB1, and blocking LKB1 activity in cells abolishes AMPK activation in response to different stimuli. These results identify a link between two protein kinases, previously thought to lie in unrelated, distinct pathways, that are associated with human diseases.

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Taylor, E. B., Ellingson, W. J., Lamb, J. D., Chesser, D. G., & Winder, W. W. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00516.2004 · Cited by 58
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Truong, M., Kim, H. G., Choi, J. H., Khanal, T., Park, B. H., Tran, T. T. P., Hwang, Y. P., Na, M., & Jeong, H. G. (2012) · Food Chemistry · doi:10.1016/j.foodchem.2012.09.012 · Cited by 57
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McInnes, K. J., Brown, K. A., Hunger, N. I., & Simpson, E. R. (2011) · International Journal of Obesity · doi:10.1038/ijo.2011.172 · Cited by 57
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Liu, N., Kataoka, M., Wang, Y., Pu, L., Dong, X., Fu, X., Zhang, F., Gao, F., Liang, T., Pei, J., et al. (2021) · Basic Research in Cardiology · doi:10.1007/s00395-021-00887-3 · Cited by 57
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Hashimoto, Y. K., Satoh, T., Okamoto, M., & Takemori, H. (2008) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21737 · Cited by 57
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Chauhan, A. S., Liu, X., Ji, J., Lee, H., Yadav, R. K., Liu, J., Zhou, Y., & Gan, B. (2018) · The FASEB Journal · doi:10.1096/fj.201801225r · Cited by 56
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Georgakis, G. V., & Younes, A. (2006) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.6.1.131 · Cited by 55
Contraction-mediated phosphorylation of AMPK is lower in skeletal muscle of adenylate kinase-deficient mice
Hancock, C. R., Janssen, E., & Terjung, R. L. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00885.2005 · Cited by 55
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Leclerc, I., Sun, G., Morris, C., Fernández‐Millán, E., Nyirenda, M., & Rutter, G. A. (2010) · Diabetologia · doi:10.1007/s00125-010-1929-z · Cited by 54
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Ching, L., Chen, C., Su, K., Hou, H., Shyue, S., Kou, Y. R., & Lee, T. (2012) · Molecular Medicine · doi:10.2119/molmed.2011.00461 · Cited by 54
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Bone, N. B., Liu, Z., Pittet, J., & Zmijewski, J. W. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.3hi0216-068rr · Cited by 55
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Tian, J., Zhao, Y., Liu, Y., Liu, Y., Chen, K., & Lyu, S. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/8214541 · Cited by 55

Authors: Woods, A., Johnstone, S. R., Dickerson, K., Leiper, F. C., Fryer, L. G. D., Neumann, D., Schlattner, U., Wallimann, T., Carlson, M., & Carling, D.
Affiliations: Hammersmith Hospital (GB)
ETH Zurich (CH)
Columbia University (US)
Corresponding author: Carling, David
ORCID: Woods, Angela
Leiper, Fiona C.
Neumann, Dietbert
Schlattner, Uwe
Wallimann, Theo
Carling, David
Venue: Current Biology
Publisher: Elsevier BV
Published: 2003-11
Volume: 13
Issue: 22
Pages: 2004-2008
ISSN: 0960-9822 (ISSN-L)
DOI: 10.1016/j.cub.2003.10.031
OpenAlex: W1990278643
Cited by: 1,650
References: 24
Citations by year: 2026: 40 · 2025: 26 · 2024: 47 · 2023: 51 · 2022: 60 · 2021: 86 · 2020: 64 · 2019: 62 · 2018: 83 · 2017: 85 · 2016: 75 · 2015: 85 · 2014: 86 · 2013: 96 · 2012: 90
FWCI: 25.86
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3546 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Current Biology (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
Funders: National Institute of General Medical Sciences (GM-34095)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: LKB1, AMPK, AMPK activation, upstream kinases, kinase cascade, Peutz-Jeghers syndrome, energy homeostasis, Snf1, PAK1, rat liver
MeSH terms: Animals, Chromatography, Ion Exchange, Enzyme Activation, Liver, Multienzyme Complexes, Precipitin Tests, Blotting, Western, Protein Serine-Threonine Kinases, Rats, AMP-Activated Protein Kinases

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LKB1 Is the Upstream Kinase in the AMP-Activated Protein Kinase Cascade

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