Nectin: an adhesion molecule involved in formation of synapses.
The nectin-afadin system is a novel cell-cell adhesion system that organizes adherens junctions cooperatively with the cadherin-catenin system in epithelial cells. Nectin is an immunoglobulin-like adhesion molecule, and afadin is an actin filament-binding protein that connects nectin to the actin cytoskeleton. Nectin has four isoforms (-1, -2, -3, and -4). Each nectin forms a homo-cis-dimer followed by formation of a homo-trans-dimer, but nectin-3 furthermore forms a hetero-trans-dimer with nectin-1 or -2, and the formation of each hetero-trans-dimer is stronger than that of each homo-trans-dimer. We show here that at the synapses between the mossy fiber terminals and dendrites of pyramidal cells in the CA3 area of adult mouse hippocampus, the nectin-afadin system colocalizes with the cadherin-catenin system, and nectin-1 and -3 asymmetrically localize at the pre- and postsynaptic sides of puncta adherentia junctions, respectively. During development, nectin-1 and -3 asymmetrically localize not only at puncta adherentia junctions but also at synaptic junctions. Inhibition of the nectin-based adhesion by an inhibitor of nectin-1 in cultured rat hippocampal neurons results in a decrease in synapse size and a concomitant increase in synapse number. These results indicate an important role of the nectin-afadin system in the formation of synapses.
Mizoguchi
Akira
A
Department of Anatomy and Neurobiology, Faculty of Medicine, Kyoto University, Kyoto 606-8501, Japan.
Nakanishi
Hiroyuki
H
Kimura
Kazushi
K
Matsubara
Kaho
K
Ozaki-Kuroda
Kumi
K
Katata
Tatsuo
T
Honda
Tomoyuki
T
Kiyohara
Yoshimoto
Y
Heo
Kyun
K
Higashi
Mikito
M
Tsutsumi
Tomonari
T
Sonoda
Satomi
S
Ide
Chizuka
C
Takai
Yoshimi
Y
D022005:Adherens Junctions / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure; D000818:Animals; D002448:Cell Adhesion / Q000187:drug effects / Q000502:physiology*; D015815:Cell Adhesion Molecules / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002454:Cell Differentiation / Q000187:drug effects / Q000502:physiology*; D003712:Dendrites / Q000378:metabolism / Q000648:ultrastructure; D004305:Dose-Response Relationship, Drug; D005333:Fetus; D007150:Immunohistochemistry; D016547:Kinesins; D008840:Microfilament Proteins / Q000378:metabolism*; D008854:Microscopy, Electron; D019599:Mossy Fibers, Hippocampal / Q000196:embryology* / Q000378:metabolism / Q000648:ultrastructure; D009218:Myosins; D000075983:Nectins; D017434:Protein Structure, Tertiary / Q000502:physiology; D017966:Pyramidal Cells / Q000378:metabolism* / Q000648:ultrastructure; D051381:Rats; D013569:Synapses / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D013570:Synaptic Membranes / Q000378:metabolism / Q000648:ultrastructure; D016708:Synaptophysin / Q000494:pharmacology; D014759:Viral Envelope Proteins / Q000494:pharmacology
C095516:AFDN protein, human; C490657:Afdn protein, mouse; D015815:Cell Adhesion Molecules; D008840:Microfilament Proteins; C000619010:NECTIN1 protein, human; C000619014:NECTIN3 protein, human; C000619015:Nectin1 protein, mouse; C000619017:Nectin3 protein, mouse; D000075983:Nectins; D016708:Synaptophysin; D014759:Viral Envelope Proteins; C108835:afadin; C039447:glycoprotein D, Human herpesvirus 1; D009218:Myosins; D016547:Kinesins