Friday, June 22, 2012, 2:30 pm — John Dunn Seminar Room, Bldg. 463
We found that nitric oxide (NO) modulates its own biosynthesis through the non-competitive inhibition of the low-affinity L-arginine transporter CAT-2A. Since this inhibition involves a direct interaction between NO and CAT-2A, we hypothesize that NO modulates transporter activity through S-nitrosation of cysteine residues. Cys->Ala mutations were generated within CAT-2A to determine the residues involved in NO modulation. Initial targets were Cys347 (putatively located near the loop that confers low-affinity to CAT 2A), and Cys171 and 427 (located within the consensus sequence AXCXXXL, implicated in the S nitrosation of several proteins). Cys347Ala mutant retains ~35% of WT transport activity, an effect not due to decreased membrane expression levels, and NO-donors fail to inhibit L-arginine uptake. Conversely, Cys427Ala and Cys171Ala mutants display WT transport activity, which is fully NO-sensitive. We conclude that Cys347 is implicated in NO modulation of CAT-2A as well as its basal transport activity, and may be the target for S-nitrosation.
Hosted by: Deborah Keszenman
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