| First Author | Phang HQ | Year | 2014 |
| Journal | J Cell Sci | Volume | 127 |
| Issue | Pt 4 | Pages | 727-39 |
| PubMed ID | 24338362 | Mgi Jnum | J:265612 |
| Mgi Id | MGI:6201888 | Doi | 10.1242/jcs.126482 |
| Citation | Phang HQ, et al. (2014) POPX2 phosphatase regulates the KIF3 kinesin motor complex. J Cell Sci 127(Pt 4):727-39 |
| abstractText | The kinesin motors are important in the regulation of cellular functions such as protein trafficking, spindle organization and centrosome separation. In this study, we have identified POPX2, a serine-threonine phosphatase, as an interacting partner of the KAP3 subunit of the kinesin-2 motor. The kinesin-2 motor is a heterotrimeric complex composed of KIF3A, KIF3B motor subunits and KAP3, the non-motor subunit, which binds the cargo. Here we report that the phosphatase POPX2 is a negative regulator of the trafficking of N-cadherin and other cargoes; consequently, it markedly influences cell-cell adhesion. POPX2 affects trafficking by determining the phosphorylation status of KIF3A at serine 690. This is consistent with the observation that the KIF3A-S690A mutant is defective in cargo trafficking. Our studies also implicate CaMKII as the kinase that phosphorylates KIF3A at serine 690. These results strongly suggest that POPX2 and CaMKII are a phosphatase-kinase pair that regulates kinesin-mediated transport and cell-cell adhesion. |
