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SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping activity.
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- Author(s): Yamochi T;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 Type:
Journal Article; Research Support, Non-U.S. Gov't
- Language:
English
- Additional Information
- Source:
Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1090-2104 (Electronic) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE
- Publication Information:
Publication: <2002- >: San Diego, CA : Elsevier
Original Publication: New York, Academic Press.
- Subject Terms:
- 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.
- Accession Number:
0 (Autoantigens)
0 (RNA Caps)
0 (Ribonucleoproteins)
0 (SS-A antigen)
EC 3.1.- (Endoribonucleases)
EC 3.1.27.- (DCP2 protein, human)
- Publication Date:
Date Created: 20080326 Date Completed: 20080512 Latest Revision: 20080415
- Publication Date:
20240829
- Accession Number:
10.1016/j.bbrc.2008.03.075
- Accession Number:
18361920
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