Differences in a single extracellular residue underlie adhesive functions of two zebrafish aqp0s

Irene Vorontsova, James E. Hall, Thomas F. Schilling, Noriaki Nagai, Yosuke Nakazawa

研究成果: Article査読

抄録

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.

本文言語English
論文番号2005
ジャーナルCells
10
8
DOI
出版ステータスPublished - 2021 8

ASJC Scopus subject areas

  • 医学(全般)

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