Differences in a Single Extracellular Residue Underlie Adhesive Functions of Two Zebrafish Aqp0s
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- Irene Vorontsova
- Physiology and Biophysics, University of California, Irvine, CA 92697, USA
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- James E. Hall
- Physiology and Biophysics, University of California, Irvine, CA 92697, USA
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- Thomas F. Schilling
- Developmental and Cell Biology, University of California, Irvine, CA 92697, USA
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- Noriaki Nagai
- Faculty of Pharmacy, Kindai University, Osaka 577-8502, Japan
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- Yosuke Nakazawa
- School of Pharmaceutical Sciences, Keio University, Tokyo 105-8512, Japan
説明
<jats:p>Aquaporin 0 (AQP0) is the most abundant lens membrane protein, and loss of function in human and animal models leads to cataract formation. AQP0 has several functions in the lens including water transport and adhesion. Since lens optics rely on strict tissue architecture achieved by compact cell-to-cell adhesion between lens fiber cells, understanding how AQP0 contributes to adhesion would shed light on normal lens physiology and pathophysiology. We show in an in vitro adhesion assay that one of two closely related zebrafish Aqp0s, Aqp0b, has strong auto-adhesive properties while Aqp0a does not. The difference appears to be largely due to a single amino acid difference at residue 110 in the extracellular C-loop, which is T in Aqp0a and N in Aqp0b. Similarly, P110 is the key residue required for adhesion in mammalian AQP0, highlighting the importance of residue 110 in AQP0 cell-to-cell adhesion in vertebrate lenses as well as the divergence of adhesive and water permeability functions in zebrafish duplicates.</jats:p>
収録刊行物
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- Cells
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Cells 10 (8), 2005-, 2021-08-06
MDPI AG