FATP1 mediates fatty acid-induced activation of AMPK in 3T3-L1 adipocytes

Brian M. Wiczer, Sandra Lobo, G. Luke Machen, Lee M. Graves, David A. Bernlohr

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


Fatty acid transport proteins are integral membrane acyl-CoA synthetases implicated in adipocyte fatty acid influx and esterification. FATP-dependent production of AMP was evaluated using FATP4 proteoliposomes, and fatty acid-dependent activation of AMP-activated protein kinase (AMPK) was assessed in 3T3-L1 adipocytes. Insulin-stimulated fatty acid influx (palmitate or arachidonate) into cultured adipocytes resulted in an increase in the phosphorylation of AMPK and its downstream target acetyl-CoA carboxylase. Consistent with the activation of AMPK, palmitate uptake into 3T3-L1 adipocytes resulted in an increase in intracellular [AMP]/[ATP]. The fatty acid-induced increase in AMPK activation was attenuated in a cell line expressing shRNA targeting FATP1. Taken together, these results demonstrate that, in adipocytes, insulin-stimulated fatty acid influx mediated by FATP1 regulates AMPK and provides a potential regulatory mechanism for balancing de novo production of fatty acids from glucose metabolism with influx of preformed fatty acids via phosphorylation of acetyl-CoA carboxylase.

Original languageEnglish (US)
Pages (from-to)234-238
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Sep 18 2009

Bibliographical note

Funding Information:
We thank members of the Bernlohr Laboratory for their comments and discussions concerning this manuscript. Supported by ADA 7-06-RA-12 and the Minnesota Obesity Center.


  • AMPK
  • Acyl-CoA synthetase
  • Adipocytes
  • Fatty acid transport
  • Fatty acids


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