کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1937583 | 1050720 | 2007 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: A new calcineurin inhibition domain in Cabin1 A new calcineurin inhibition domain in Cabin1](/preview/png/1937583.png)
Calcineurin (CN), a calcium-activated phosphatase, plays a critical role in various biological processes including T cell activation. Cabin1, a calcineurin binding protein 1, has been shown to bind directly to CN using its C-terminal region and inhibit CN activity. However, no increase in CN activity has been found in Cabin1ΔC T cells, which produce a truncated Cabin1 lacking the C-terminal CN binding region. Here, we report that Cabin1 has additional CN binding domain in its 701–900 amino acid residues. Cabin1 (701–900) blocked both CN-mediated dephosphorylation and nuclear import of NFAT and thus inhibited IL-2 production in response to PMA/ionomycin stimulation. This fact may explain why Cabin1ΔC mice previously showed no significant defect in CN-mediated signaling pathway.
Journal: Biochemical and Biophysical Research Communications - Volume 359, Issue 1, 20 July 2007, Pages 129–135