Browse

A new calcineurin inhibition domain in Cabin1

Cited 12 time in Web of Science Cited 14 time in Scopus
Authors
Jang, Hyonchol; Cho, Eun-Jung; Youn, Hong-Duk
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/*metabolismEnzyme ActivationEnzyme Inhibitors/chemistry/metabolismHumansJurkat CellsProtein 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
DOI
https://doi.org/10.1016/j.bbrc.2007.05.066
Files in This Item:
There are no files associated with this item.
Appears in Collections:
College of Medicine/School of Medicine (의과대학/대학원)Program in Cancer Biology (협동과정-종양생물학전공)Journal Papers (저널논문_협동과정-종양생물학전공)
  • mendeley

Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse