Titre
Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence.
Type
article
Institution
Externe
Périodique
Auteur(s)
Fotiadis, D.
Auteure/Auteur
Hasler, L.
Auteure/Auteur
Müller, D.J.
Auteure/Auteur
Stahlberg, H.
Auteure/Auteur
Kistler, J.
Auteure/Auteur
Engel, A.
Auteure/Auteur
Liens vers les personnes
ISSN
0022-2836
Statut éditorial
Publié
Date de publication
2000-07-21
Volume
300
Numéro
4
Première page
779
Dernière page/numéro d’article
789
Peer-reviewed
Oui
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Publication Status: ppublish
Résumé
The lens major intrinsic protein (MIP, AQP0) is known to function as a water and solute channel. However, MIP has also been reported to occur in close membrane contacts between lens fiber cells, indicating that it has adhesive properties in addition to its channel function. Using atomic force and cryo-electron microscopy we document that crystalline sheets reconstituted from purified ovine lens MIP mostly consisted of two layers. MIP lattices in the apposing membranes were in precise register, and determination of the membrane sidedness demonstrated that MIP molecules bound to each other via their extracellular surfaces. The surface structure of the latter was resolved to 0.61 nm and revealed two protruding domains providing a tight "tongue-and-groove" fit between apposing MIP molecules. Cryo-electron crystallography produced a projection map at 0.69 nm resolution with a mirror symmetry axis at 45 degrees to the lattice which was consistent with the double-layered nature of the reconstituted sheets. These data strongly suggest an adhesive function of MIP, and strengthen the view that MIP serves dual roles in the lens.
Sujets
PID Serval
serval:BIB_523537498636
PMID
Date de création
2023-06-09T14:04:15.320Z
Date de création dans IRIS
2025-05-20T17:02:28Z