S-Space College of Medicine/School of Medicine (의과대학/대학원) Program in Cancer Biology (협동과정-종양생물학전공) Journal Papers (저널논문_협동과정-종양생물학전공)
A new calcineurin inhibition domain in Cabin1
- Jang, Hyonchol; Cho, Eun-Jung; Youn, Hong-Duk
- Issue Date
- Biochem Biophys Res Commun. 2007 Jul 20;359(1):129-35. Epub 2007 May 21.
- Calcineurin/*chemistry/*metabolism; Enzyme Activation; Enzyme Inhibitors/chemistry/metabolism; Humans; Jurkat Cells; Protein Binding
- 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 Cabin1DeltaC 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 Cabin1DeltaC mice previously showed no significant defect in CN-mediated signaling pathway.
- 0006-291X (Print)
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