Structural features of aquaporin 4 supporting the formation of arrays and junctions in biomembranes

Siegfried Höfinger, Eiji Yamamoto, Yoshinori Hirano, Francesco Zerbetto, Tetsu Narumi, Kenji Yasuoka, Masato Yasui

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

A limited class of aquaporins has been described to form regular arrays and junctions in membranes. The biological significance of these structures, however, remains uncertain. Here we analyze the underlying physical principles with the help of a computational procedure that takes into account protein-protein as well as protein-membrane interactions. Experimentally observed array/junction structures are systematically (dis)assembled and major driving forces identified. Aquaporin 4 was found to be markedly different from the non-junction forming aquaporin 1. The environmental stabilization resulting from embedding into the biomembrane was identified as the main driving force. This highlights the role of protein-membrane interactions in aquaporin 4. Analysis of the type presented here can help to decipher the biological role of membrane arrays and junctions formed by aquaporin.

Original languageEnglish
Pages (from-to)2234-2243
Number of pages10
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1818
Issue number9
DOIs
Publication statusPublished - 2012 Sep 1

Keywords

  • Aquaporin 4
  • Array
  • Biomembrane mimicry
  • Free energies
  • Junction
  • MM/PBSA

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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