Regulation of KIF3 motor by dephosphorylation

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We identified the protein-phosphatase DUSP26 as a novel regulator of the KIF3 motor. Dusp26 is recruited to the KIF3 motor mainly by interaction with Kif3a, and thereby dephosphorylates Kap3. Enzyme activity of the Dusp26 was shown to promote distribution of beta-catenin/N-cadherinto cell-cell junction sites, resulting in increased cell-cell adhesiveness. We also showed that DUSP26 mRNA expression was downregulated in human glioblastoma samples, and a CpG island upstream of the DUSP26 transcrptional start site was heavily methylated in glioma cell lines. These results suggest previously unidentified functions of DUSP26 in intracellular transport and cell-cell adhesion.Downregulation of DUSP26 may contribute to malignant phenotypes of glioma. We showed that DUSP13B inactivated MAPK activation in the order of selectivity, JNK=p38> ERK in cells. Reporter gene analysis showed that DUSP13B had significant inhibitory effect on AP-1 dependent gene expression. DUSP13B is the first identified testis specific phosphatase that inhibits stress-activated MAPKs.