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SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping activity.

Authors :
Yamochi T
Ohnuma K
Hosono O
Tanaka H
Kanai Y
Morimoto C
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2008 May 23; Vol. 370 (1), pp. 195-9. Date of Electronic Publication: 2008 Mar 24.
Publication Year :
2008

Abstract

We identified human decapping enzyme 2 (hDCP2) as a binding protein with Ro52, being colocalized in processing bodies (p-bodies). We also showed that the N-terminus and C-terminus of Ro52 bound to hDCP2. Moreover, Ro52 enhanced decapping activity of hDCP2 in a dose-dependent manner. Our data support the novel notion of the association between Ro52 with hDCP2 protein in cytoplasmic p-bodies, playing a role in mRNA metabolism in response to cellular stimulation.

Details

Language :
English
ISSN :
1090-2104
Volume :
370
Issue :
1
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
18361920
Full Text :
https://doi.org/10.1016/j.bbrc.2008.03.075