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
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- Hasegawa Takahiro
- Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
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- Azlina Ahmad
- Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
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- Purwanti Nunuk
- Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
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- Purevjav Javkhlan
- Department of Periodontology and Endodontology, Institute of Health Biosciences, the University of Tokushima Graduate School
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- Yao Chenjuan
- Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
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- Akamatsu Tetsuya
- Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
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- Hosoi Kazuo
- Department of Molecular Oral Physiology, Institute of Health Biosciences, the University of Tokushima Graduate School
Bibliographic Information
- Other Title
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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
Journal
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- The Journal of Medical Investigation
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The Journal of Medical Investigation 56 (1,2), 55-63, 2009
The University of Tokushima Faculty of Medicine
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Details
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- CRID
- 1390001204245181696
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- NII Article ID
- 130004465167
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- NII Book ID
- AA11166929
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- ISSN
- 13496867
- 13431420
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- Text Lang
- en
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- Data Source
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- JaLC
- IRDB
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed