Requirement of the actin cytoskeleton for the association of nectins with other cell adhesion molecules at adherens and tight junctions in MDCK cells.
Nectins, Ca(2+)-independent immunoglobulin-like cell adhesion molecules (CAMs), first form cell-cell adhesion where cadherins are recruited, forming adherens junctions (AJs) in epithelial cells and fibroblasts. In addition, nectins recruit claudins, occludin, and junctional adhesion molecules (JAMs) to the apical side of AJs, forming tight junctions (TJs) in epithelial cells. Nectins are associated with these CAMs through peripheral membrane proteins (PMPs), many of which are actin filament-binding proteins. We examined here the roles of the actin cytoskeleton in the association of nectins with other CAMs in MDCK cells stably expressing exogenous nectin-1. The nectin-1-based cell-cell adhesion was formed and maintained irrespective of the presence and absence of the actin filament-disrupting agents, such as cytochalasin D and latrunculin A. In the presence of these agents, only afadin remained at the nectin-1-based cell-cell adhesion sites, whereas E-cadherin and other PMPs at AJs, alpha-catenin, beta-catenin, vinculin, alpha-actinin, ADIP, and LMO7, were not concentrated there. The CAMs at TJs, claudin-1, occludin and JAM-1, or the PMPs at TJs, ZO-1 and MAGI-1, were not concentrated there, either. These results indicate that the actin cytoskeleton is required for the association of the nectin-afadin unit with other CAMs and PMPs at AJs and TJs.
Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Japan.
Akio
A
Yamada
Kenji
K
Irie
Atsunori
A
Fukuhara
Takako
T
Ooshio
Yoshimi
Y
Takai
D008841:Actin Cytoskeleton / Q000187:drug effects / Q000502:physiology*; D022005:Adherens Junctions / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure; D000818:Animals; D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000494:pharmacology; D015820:Cadherins / Q000378:metabolism; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D002460:Cell Line; D062445:Claudin-1; D015638:Cytochalasin D / Q000494:pharmacology; D004285:Dogs; D062726:Junctional Adhesion Molecules; D008565:Membrane Proteins / Q000378:metabolism; D008856:Microscopy, Fluorescence; D000075983:Nectins; D062793:Occludin; D013844:Thiazoles / Q000494:pharmacology; D053778:Thiazolidines; D019108:Tight Junctions / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure
D019086:Bridged Bicyclo Compounds, Heterocyclic; D015820:Cadherins; D015815:Cell Adhesion Molecules; D062445:Claudin-1; D062726:Junctional Adhesion Molecules; D008565:Membrane Proteins; D000075983:Nectins; D062793:Occludin; D013844:Thiazoles; D053778:Thiazolidines; D015638:Cytochalasin D; C037067:latrunculin A