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A new calcineurin inhibition domain in Cabin1
Cited 14 time in
Web of Science
Cited 16 time in Scopus
- Authors
- Issue Date
- 2007-05-29
- Publisher
- Elsevier
- Citation
- Biochem Biophys Res Commun. 2007 Jul 20;359(1):129-35. Epub 2007 May 21.
- Keywords
- Calcineurin/*chemistry/*metabolism ; Enzyme Activation ; Enzyme Inhibitors/chemistry/metabolism ; Humans ; Jurkat Cells ; Protein Binding
- Abstract
- 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.
- ISSN
- 0006-291X (Print)
- Language
- English
- URI
- http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WBK-4NSR1JX-K&_user=10&_rdoc=1&_fmt=&_orig=search&_sort=d&_docanchor=&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=6042cd12b6085c7ae0a786fc6913f9e0
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17531200
https://hdl.handle.net/10371/24357
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