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A new calcineurin inhibition domain in Cabin1.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Jang H,Cho EJ,Youn HD

doi

10.1016/j.bbrc.2007.05.066

subject

Has Abstract

pub_date

2007-07-20 00:00:00

pages

129-35

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)01039-X

journal_volume

359

pub_type

杂志文章

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