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

DOI Web Site PubMed 5 Citations 32 References
  • Atik Nur
    Department of Cell Biology, Graduate School of Medicine, Osaka University Department of Cell Biology, Faculty of Medicine, Padjadjaran University
  • Kunii Masataka
    Department of Cell Biology, Graduate School of Medicine, Osaka University
  • Avriyanti Erda
    Department of Cell Biology, Graduate School of Medicine, Osaka 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
  • Yoshimura Shin‑ichiro
    Department of Cell Biology, Graduate School of Medicine, Osaka 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

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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 in vivo. 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.

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