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Papers In Press, published online ahead of print May 22, 2001
J. Biol. Chem, 10.1074/jbc.C100119200
Submitted on March 8, 2001
Revised on April 16, 2001
Accepted on May 22, 2001
Laboratory for Developmental Neurobiology, Brain Science Institute, RIKEN, Wako, Saitama 351-0198
Corresponding Author: mnfukuda{at}brain.riken.go.jp
The C2 domain was originally defined as a homologous domain to the C2 regulatory region of Ca2+-dependent protein kinase C, and has been identified in more than 50 different signaling molecules. The original C2 domain of protein kinase Ca functions as a Ca2+-binding module, and the Ca2+-binding to the C2 domain allows translocation of proteins to phospholipid membranes. By contrast, however, some C2 domains do not exhibit Ca2+-binding activity due to amino acid substitutions at Ca2+-binding sites, and their physiological meanings remain largely unknown. In this study, we discovered an unexpected function of the Ca2+-independent C2A domain of double C2 protein g (Doc2g) in nuclear localization. Deletion and mutation analyses revealed that the putative Ca2+-binding loop 3 of Doc2g contains six Arg residues (177 RLRRRRR 183) and that this basic cluster is both necessary and sufficient for nuclear localization of Doc2g. Because of the presence of the basic cluster, the C2A domain of Doc2g did not show Ca2+-dependent phospholipid binding activity. Our findings indicate that by changing the nature of the putative Ca2+-binding loops the C2 domain has more diversified function in cellular signaling than a simple Ca2+-binding motif.
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