Journal article
Linking E-cadherin mechanotransduction to cell metabolism through force-mediated activation of AMPK
Nature cell biology, Vol.19(6), pp.724-731
05/29/2017
DOI: 10.1038/ncb3537
PMCID: PMC5494977
PMID: 28553939
Abstract
The response of cells to mechanical force 1–3 is a major determinant of cell behaviour and is an energetically costly event 4,5. How cells derive energy to resist mechanical force is unknown. Here, we show that application of force to E-cadherin stimulates liver kinase B1 (LKB1) to activate AMP-activated protein kinase (AMPK), a master regulator of energy homeostasis. LKB1 recruits AMPK to the E-cadherin mechanotransduction complex, thereby stimulating actomyosin contractility, glucose uptake and ATP production. The increase in ATP provides energy to reinforce the adhesion complex and actin cytoskeleton so that the cell can resist physiological forces. Together, these findings reveal a paradigm for how mechanotransduction and metabolism are linked and provide a framework for understanding how diseases involving contractile and metabolic disturbances arise.
Details
- Title: Subtitle
- Linking E-cadherin mechanotransduction to cell metabolism through force-mediated activation of AMPK
- Creators
- Jennifer Bays - University of Iowa [Iowa City]Hannah Campbell - University of Iowa [Iowa City]Christy Heidema - University of Iowa [Iowa City]Michael Sebbagh - Centre de Recherche en Cancérologie de MarseilleKris DeMali - University of Iowa [Iowa City]
- Resource Type
- Journal article
- Publication Details
- Nature cell biology, Vol.19(6), pp.724-731
- DOI
- 10.1038/ncb3537
- PMID
- 28553939
- PMCID
- PMC5494977
- NLM abbreviation
- Nat Cell Biol
- ISSN
- 1465-7392
- eISSN
- 1476-4679
- Publisher
- Nature Publishing Group
- Language
- English
- Date published
- 05/29/2017
- Academic Unit
- Dermatology; Fraternal Order of Eagles Diabetes Research Center; Biochemistry and Molecular Biology
- Record Identifier
- 9984024561802771
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