A non-connexon protein (MIP) is involved in eye lens gap-junction formation.
New immunolocalization data put the role of the lens MP26 (MIP) protein in a new perspective. During maturation of lens fibre cells, MIP is found to associate specifically with two structures, gap junctions and cell interlocking processes (known as ball and socket domains). It is significant that the zone in which these associations are most striking is discrete, coinciding with the zone of rapidly enlarging junctional plaques and newly forming ball and socket domains. Observation of domain-specific interactions of MIP with forming gap junctions and ball and socket domains suggests that MIP may be involved in the formation of close membrane appositions. Furthermore, previous ambiguities in the literature over the presence of MIP in gap junctions are clarified by the knowledge that, in situ, MIP associates strongly with gap junctions for only a brief period (with less than about 5% of all lens gap junctions at any one time) during the assembly of junctional plaques.
Gruijters
W T
WT
Department of Cellular and Molecular Biology, University of Auckland, New Zealand.
D000818:Animals; D020346:Aquaporins; D005136:Eye Proteins / Q000502:physiology*; D005455:Fluorescent Antibody Technique; D007365:Intercellular Junctions / Q000502:physiology* / Q000648:ultrastructure; D007908:Lens, Crystalline / Q000502:physiology* / Q000648:ultrastructure; D008562:Membrane Glycoproteins; D008854:Microscopy, Electron; D012756:Sheep
D020346:Aquaporins; D005136:Eye Proteins; D008562:Membrane Glycoproteins; C030328:aquaporin 0