Zebrafish calsyntenins mediate homophilic adhesion through their amino-terminal cadherin repeats. (12th February 2015)

• Record Type: Journal Article
• Authors: Ortiz-Medina, H.; Emond, M.R.; Jontes, J.D.
• Is Part Of: Neuroscience. Volume 286(2015)
• Page Start: 87
• Page End: 96
• Publication Date: 2015-02-12
• Subjects: Clstns calsyntenins -- EC endodomain -- EDTA ethylenediaminetetraacetic acid -- hpf hours postfertilization -- IgG Immunoglobulin G -- LGN Leu-Gly-Asn repeat-enriched -- PCR polymerase chain reaction -- RT-PCR reverse transcription polymerase chain reaction; calsyntenin -- zebrafish -- adhesion -- cadherin; Neurochemistry -- Periodicals; Neurophysiology -- Periodicals; Neurology -- Periodicals; Neurochimie -- Périodiques; Neurophysiologie -- Périodiques; Neurochemistry; Neurophysiology; Electronic journals; Periodicals; Electronic journals; 612.8
• DOI: 10.1016/j.neuroscience.2014.11.030
• Languages: English
• ISSNs: 0306-4522

Abstract

Highlights: Zebrafish calsyntenins exhibit distinct expression patterns in the developing zebrafish. Zebrafish calsyntenins mediate homophilic adhesion. The two, amino-terminal cadherin repeats are necessary and sufficient for adhesion. Adhesion requires both cadherin repeats. Adhesive interactions are promiscuous among the calsyntenins. Abstract: The calsyntenins are atypical members of the cadherin superfamily that have been implicated in learning in Caenorhabditis elegans and memory formation in humans. As members of the cadherin superfamily, they could mediate cell–cell adhesion, although their adhesive properties have not been investigated. As an initial step in characterizing the calsyntenins, we have cloned clstn1, clstn2 and clstn3 from the zebrafish and determined their expression in the developing zebrafish nervous system. The three genes each have broad, yet distinct, expression patterns in the zebrafish brain. Each of the ectodomains mediates homophilic interactions through two, amino-terminal cadherin repeats. In bead sorting assays, the calsyntenin ectodomains do not exhibit homophilic preferences. These data support the idea that calsyntenins could either act as adhesion molecules or as diffusible, homophilic or heterophilic ligands in the vertebrate nervous system.