the serine 814 of trpc6 is phosphorylated under unstimulated conditions如果条件下trpc6是磷酸化的丝氨酸814.pdfVIP

The Serine 814 of TRPC6 Is Phosphorylated under Unstimulated Conditions Simon M. Bousquet, Michael Monet, Guylain Boulay* ´ ´ Department of Pharmacology, Universite de Sherbrooke, Sherbrooke, Quebec, Canada Abstract TRPC are nonselective cation channels involved in calcium entry. Their regulation by phosphorylation has been shown to modulate their routing and activity. TRPC6 activity increases following phosphorylation by Fyn, and is inhibited by protein kinase G and protein kinase C. A previous study by our group showed that TRPC6 is phosphorylated under unstimulated conditions in a human embryonic kidney cells line (HEK293). To investigate the mechanism responsible for this phosphorylation, we used a MS/MS approach combined with metabolic labeling and showed that the serine at position 814 is phosphorylated in unstimulated cells. The mutation of Ser814 into Ala decreased basal phosphorylation but did not modify TRPC6 activity. Even though Ser814 is within a consensus site for casein kinase II (CK2), we showed that CK2 is not involved in the phosphorylation of TRPC6 and does not modify its activity. In summary, we identified a new basal phosphorylation site (Ser814) on TRPC6 and showed that CK2 is not responsible for the phosphorylation of this site. Citation: Bousquet SM, Monet M, Boulay G (2011) The Serine 814 of TRPC6 Is Phosphorylated under Unstimulated Conditions. PLoS ONE 6(3): e18121. doi:10.1371/journal.pone.0018121 Editor: Karl-Wilhelm Koch, University of Oldenburg, Germany Received November 22, 2010; Accepted February 22, 2011; Published March 23, 2011 Copyright: 2011 Bousquet et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted