Lysophosphatidic acid directly activates TRPV1 through a C-terminal binding site.

@article{NietoPosadas2011LysophosphatidicAD,
  title={Lysophosphatidic acid directly activates TRPV1 through a C-terminal binding site.},
  author={Andr{\'e}s Nieto-Posadas and Giovanni Picazo-Ju{\'a}rez and Itzel Llorente and Andr{\'e}s Jara-Oseguera and Sara Luz Morales-L{\'a}zaro and Diana Escalante-Alcalde and Le{\'o}n D Islas and Tamara Rosenbaum},
  journal={Nature chemical biology},
  year={2011},
  volume={8 1},
  pages={78-85}
}
Since 1992, there has been growing evidence that the bioactive phospholipid lysophosphatidic acid (LPA), whose amounts are increased upon tissue injury, activates primary nociceptors resulting in neuropathic pain. The TRPV1 ion channel is expressed in primary afferent nociceptors and is activated by physical and chemical stimuli. Here we show that in control mice LPA produces acute pain-like behaviors, which are substantially reduced in Trpv1-null animals. Our data also demonstrate that LPA… CONTINUE READING
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Crystal structure of autotaxin and insight into GPCR activation by lipid mediators

  • H. Nishimasu
  • Nat . Struct . Mol . Biol .
  • 2011

Structural basis of substrate discrimination and integrin binding by autotaxin

  • J. Hausmann
  • Nat . Struct . Mol . Biol .
  • 2011

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