Trafficking of GFP-AQP5 chimeric proteins conferred with unphosphorylated amino acids at their PKA-target motif (152SRRTS) in MDCK-II cells

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  • Ratko Karabasil Mileva
    Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
  • Hasegawa Takahiro
    Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
  • Azlina Ahmad
    Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
  • Purwanti Nunuk
    Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
  • Purevjav Javkhlan
    Department of Periodontology and Endodontology, Institute of Health Biosciences, the University of Tokushima Graduate School
  • Yao Chenjuan
    Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
  • Akamatsu Tetsuya
    Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
  • Hosoi Kazuo
    Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School

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  • Trafficking of GFP-AQP5 chimeric proteins conferred with unphosphorylated amino acid at their PKA-target motif (152SRRTS) in MDCK-II cells

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Abstract

Three constructs having mutated PKA-target motif at 152SRRTS of AQP5, an exocrine type water channel, were prepared and fused to C-terminus of green fluorescence protein cDNA to examine the effects of blocking of phosphorylation at 152SRRTS (a consensus PKA-target motif of AQP5) on translocation or trafficking of the chimeric proteins expressed in the Madin-Darby canine kidney-II (MDCK-II) cells. H-89 treatment increased translocation of wild-type GFP-AQP5 to the apical membrane. All 3 mutant molecules translocated 1.5 to 2 times more than the control wild-type GFP-AQP5. Colchicine but not cytochalasin B inhibited the translocation of wild-type GFP-AQP5. Present results suggest dephosphorylation of this consensus sequence increase GFP-AQP5 translocation, and that microtubules but not microfilaments are involved in this event. J. Med. Invest. 56: 55-63, February, 2009

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