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

Tadanori Yamochi; Kei Ohnuma; Osamu Hosono; Hirotoshi Tanaka; Yoshiyuki Kanai; Chikao Morimoto

doi:10.1016/j.bbrc.2008.03.075

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

Biochem Biophys Res Commun. 2008 May 23;370(1):195-9. doi: 10.1016/j.bbrc.2008.03.075. Epub 2008 Mar 24.

Authors

Tadanori Yamochi¹, Kei Ohnuma, Osamu Hosono, Hirotoshi Tanaka, Yoshiyuki Kanai, Chikao Morimoto

Affiliation

¹ Department of Clinical Immunology, Advanced Clinical Research Center, Institute of Medical Science, University of Tokyo, 4-6-1, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.

PMID: 18361920
DOI: 10.1016/j.bbrc.2008.03.075

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Autoantigens / analysis
Autoantigens / metabolism*
Catalysis
Cytoplasm / enzymology
Endoribonucleases / analysis
Endoribonucleases / genetics
Endoribonucleases / metabolism*
Humans
Protein Interaction Mapping
Protein Structure, Tertiary
RNA Caps / metabolism*
RNA Stability*
Ribonucleoproteins / analysis
Ribonucleoproteins / genetics
Ribonucleoproteins / metabolism*

Substances

Autoantigens
RNA Caps
Ribonucleoproteins
SS-A antigen
Endoribonucleases
DCP2 protein, human