AI Article Synopsis
- Recent studies show how AMPK gets activated in cells during low glucose conditions, involving a specific interaction between AXIN and LKB1 on late endosomes/lysosomes.
- The lysosomal v-ATPase-Ragulator complex plays a crucial role when glucose levels are low, helping to bring AXIN/LKB1 together with AMPK.
- The chapter outlines experimental procedures to track the movement of AXIN/LKB1 and how these complexes form, which is important for understanding AMPK activation under metabolic stress and its impact on mTORC1.
Article Abstract
Recent studies have revealed how AMPK is activated inside the cell and animal tissues: in response to low glucose, AXIN tethers LKB1, by virtue of their constitutive association, to AMPK located on the surface of late endosome/lysosome. Importantly, the lysosomal v-ATPase (vacuolar ATPase)-Ragulator complex, when primed by glucose starvation or concanamycin A, facilitates AXIN/LKB1 to interact with AMPK. Here, we describe the experimental procedures of the assays for detecting the translocation of AXIN/LKB1 or the assembly of the AXIN-based AMPK-activating complexes on the late endosome/lysosome. The methods in this chapter will be useful for determining whether various metabolic stresses or pharmacological stimuli activate AMPK via the v-ATPase-Ragulator-AXIN/LKB1 axis, which also concomitantly inactivates mTORC1. Detailed protocols for determining the levels of adenylates are also described.
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| http://dx.doi.org/10.1007/978-1-4939-7598-3_25 | DOI Listing |
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Determining AMPK Activation via the Lysosomal v-ATPase-Ragulator-AXIN/LKB1 Axis.
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State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, Fujian, China.
Article Synopsis
- Recent studies show how AMPK gets activated in cells during low glucose conditions, involving a specific interaction between AXIN and LKB1 on late endosomes/lysosomes.
- The lysosomal v-ATPase-Ragulator complex plays a crucial role when glucose levels are low, helping to bring AXIN/LKB1 together with AMPK.
- The chapter outlines experimental procedures to track the movement of AXIN/LKB1 and how these complexes form, which is important for understanding AMPK activation under metabolic stress and its impact on mTORC1.
Methods to Study Lysosomal AMPK Activation.
Methods Enzymol
October 2017
State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, China. Electronic address:
The AMP-activated protein kinase (AMPK) is a master regulator of metabolic homeostasis. It is activated by the upstream kinase LKB1 (liver kinase B1) when the AMP/ATP ratio is increased during starvation or heightened exercises. Based on reconstitution experiments using purified individual proteins, AMPK was demonstrated to be directly phosphorylated on its conserved residue Thr172 by LKB1, which was promoted by increased levels of AMP.
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