SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping activity.
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.
Yamochi
Tadanori
T
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.
Ohnuma
Kei
K
Hosono
Osamu
O
Tanaka
Hirotoshi
H
Kanai
Yoshiyuki
Y
Morimoto
Chikao
C
D001324:Autoantigens / Q000032:analysis / Q000378:metabolism*; D002384:Catalysis; D003593:Cytoplasm / Q000201:enzymology; D004722:Endoribonucleases / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D012315:RNA Caps / Q000378:metabolism*; D020871:RNA Stability; D012261:Ribonucleoproteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D000099207:SS-A Antigen
D001324:Autoantigens; D004722:Endoribonucleases; D012315:RNA Caps; D012261:Ribonucleoproteins; D000099207:SS-A Antigen; C467723:DCP2 protein, human