Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases

By Seung-pyo Hong, F. C. Leiper, A. Woods, David Carling, M. Carlson. Proceedings of the National Academy of Sciences of the United States of America, 2003

619 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/a1f7e6c4eb518e7a95664d08e807904fb1d9435f

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Citations in the corpus

• LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR‐1 (2004, background): “Studies performed in Saccharomyces cerevisiae indicated that the T-loop residue of the yeast orthologue of AMPK (SNF1) was phosphorylated by a group of three related protein kinases bearing homology to LKB1 (Hong et al, 2003; Nath et al, 2003; Sutherland et al, 2003).”
• TSC2 mediates cellular energy response to control cell growth and survival. (2003, background): “AMPK can inhibit translation AMPK (Hong et al., 2003; Sutherland et al., 2003; Hawley by at least two mechanisms, one by phosphorylation of et al., 2003).”
• AMP‐activated protein kinase – development of the energy sensor concept (2006, background): “However, after the completion of the budding yeast genome project, three protein kinases acting upstream of the yeast homologue of AMPK (the SNF1 complex) were identified by various genome-wide screening approaches (Hong et al. 2003; Sutherland et al. 2003).”
• Dysregulation of the TSC-mTOR pathway in human disease (2004, background): “Notably, STK11 (also called LKB1 ), the gene inactivated in Peutz-Jeghers syndrome, is an upstream activating kinase of AMP”
• Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade (2003, background): “[39] reported that FLAG-tagged LKB1 expressed in, and purified from, COS7 cells would activate a recombinant AMPK heterotrimer, and phosphorylate the subunit at Thr172, in cell-free assays.”
• AMPK in Health and Disease. (2009, background): “Since the constitutively active AMPK fragment 1 (1-312) is not activated by the PT1 compound, it is proposed that PT1 acts by reversing the autoinhibition of the AIS (313-335).”
• An AMPK-FOXO pathway mediates longevity induced by a novel method of dietary restriction in C. elegans. (2007, neutral): “The stoichiometry of phosphorylation of DAF-16 by human and worm AMPK was higher than that of the SAMS peptide, a peptide containing a known AMPK phosphorylation site [13] (Figure 6B), suggesting that DAF-16 is a good in vitro substrate of AMPK.”
• Membrane fatty acid transporters as regulators of lipid metabolism: implications for metabolic disease. (2010, background): “Namely, Snf1, the yeast homolog of AMPK, is phosphorylated by three kinases (204), and database searches revealed three closely related mammalian kinases, LKB1, CaMKK , and CaMKK (166).”
• Intrasteric control of AMPK via the γ1 subunit AMP allosteric regulatory site (2004, background): “AMPK is activated by phosphorylation of T172 within the subunit activation loop (Hawley et al. 1996) by upstream protein kinases (AMPKK) that includes LKB1 (Hong et al. 2003).”
• Nutritional Control of Growth and Development in Yeast (2012, background): “Three kinases—Elm1, Tos3, and Sak1—serve as redundant SNF1activating kinases (Hong et al. 2003; Nath et al. 2003; Sutherland et al. 2003).”
• Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae (2014, background): “When only Sip2 is present, Tos3 and Elm1 cannot support the induction of invertase activity encoded by SUC2.”