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Title: POPX2 phosphatase regulates the KIF3 kinesin motor complex
Authors: Phang, Hui-Qun
Hoon, Jing-Ling
Lai, Soak-Kuan
Zeng, Yukai
Chiam, Keng-Hwee
Li, Hoi-Yeung
Koh, Cheng-Gee
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2014
Source: Phang, H.-Q., Hoon, J.-L., Lai, S.-K., Zeng, Y., Chiam, K.-H., Li, H.-Y., et al. (2014). POPX2 phosphatase regulates the KIF3 kinesin motor complex. Journal of cell science, 127(4), 727-739.
Series/Report no.: Journal of cell science
Abstract: 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.
DOI: 10.1242/jcs.126482
Rights: © The Authors (published by The Company of Biologists Ltd.). This is the author created version of a work that has been peer reviewed and accepted for publication in Journal of Cell Science, published by The Company of Biologists Ltd. on behalf of The Authors. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [Article DOI:].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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