The Role of PKD in Cell Polarity, Biosynthetic Pathways, and Organelle/F-actin Distribution

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Author(s)

    • Atik Nur Atik Nur
    • Department of Cell Biology, Graduate School of Medicine, Osaka University|Department of Cell Biology, Faculty of Medicine, Padjadjaran University
    • Furumoto Naomi
    • Laboratory for Molecular Traffic, Department of Cellular and Molecular Biology, Institute for Molecular and Cellular Regulation, Gunma University
    • Inami Keiko
    • Laboratory for Molecular Traffic, Department of Cellular and Molecular Biology, Institute for Molecular and Cellular Regulation, Gunma University
    • Harada Reiko
    • Department of Cell Biology, Graduate School of Medicine, Osaka University|Department of Judo Therapy, Takarazuka University of Medical and Health Care
    • Harada Akihiro
    • Department of Cell Biology, Graduate School of Medicine, Osaka University|Laboratory for Molecular Traffic, Department of Cellular and Molecular Biology, Institute for Molecular and Cellular Regulation, Gunma University

Abstract

Protein Kinase D (PKD) 1, 2, and 3 are members of the PKD family. PKDs influence many cellular processes, including cell polarity, structure of the Golgi, polarized transport from the Golgi to the basolateral plasma membrane, and actin polymerization. However, the role of the PKD family in cell polarity has not yet been elucidated <i>in vivo</i>. Here, we show that KO mice displayed similar localization of the apical and basolateral proteins, transport of VSV-G and a GPI-anchored protein, and similar localization of actin filaments. As DKO mice were embryonic lethal, we generated MEFs that lacked all PKD isoforms from the PKD1 and PKD2 double floxed mice using Cre recombinase and PKD3 siRNA. We observed a similar localization of various organelles, a similar time course in the transport of VSV-G and a GPI-anchored protein, and a similar distribution of F-actin in the PKD-null MEFs. Collectively, our results demonstrate that the complete deletion of PKDs does not affect the transport of VSV-G or a GPI-anchored protein, and the distribution of F-actin. However, simultaneous deletion of PKD1 and PKD2 affect embryonic development, demonstrating their functional redundancy during development.

Journal

  • Cell Structure and Function

    Cell Structure and Function 39(1), 61-77, 2014

    Japan Society for Cell Biology

Codes

  • NII Article ID (NAID)
    130004137601
  • NII NACSIS-CAT ID (NCID)
    AA0060007X
  • Text Lang
    ENG
  • ISSN
    0386-7196
  • NDL Article ID
    026678547
  • NDL Call No.
    Z53-V38
  • Data Source
    NDL  J-STAGE 
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