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|Title:||Cyclin-dependent kinase 5 modulates nociceptive signaling through direct phosphorylation of transient receptor potential vanilloid 1||Authors:||Pareek, T.K.
|Issue Date:||9-Jan-2007||Citation:||Pareek, T.K., Keller, J., Kesavapany, S., Agarwal, N., Kuner, R., Pant, H.C., Iadarola, M.J., Brady, R.O., Kulkarni, A.B. (2007-01-09). Cyclin-dependent kinase 5 modulates nociceptive signaling through direct phosphorylation of transient receptor potential vanilloid 1. Proceedings of the National Academy of Sciences of the United States of America 104 (2) : 660-665. ScholarBank@NUS Repository. https://doi.org/10.1073/pnas.0609916104||Abstract:||Transient receptor potential vanilloid 1 (TRPV1), a ligand-gated cation channel highly expressed in small-diameter sensory neurons, is activated by heat, protons, and capsaicin. The phosphorylation of TRPV1 provides a versatile regulation of intracellular calcium levels and is critical for TRPV1 function in responding to a pain stimulus. We have previously reported that cyclin-dependent kinase 5 (Cdk5) activity regulates nociceptive signaling. In this article we report that the Cdk5-mediated phosphorylation of TRPV1 at threonine-407 can modulate agonist-induced calcium influx. Inhibition of Cdk5 activity in cultured dorsal root ganglia neurons resulted in a significant reduction of TRPV1-mediated calcium influx, and this effect could be reversed by restoring Cdk5 activity. Primary nociceptor-specific Cdk5 conditional-knockout mice showed reduced TRPV1 phosphorylation, resulting in significant hypoalgesia. Thus, the present study indicates that Cdk5-mediated TRPV1 phosphorylation is important in the regulation of pain signaling. © 2006 by The National Academy of Sciences of the USA.||Source Title:||Proceedings of the National Academy of Sciences of the United States of America||URI:||http://scholarbank.nus.edu.sg/handle/10635/120809||ISSN:||00278424||DOI:||10.1073/pnas.0609916104|
|Appears in Collections:||Staff Publications|
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