PUBLICATION

Zebrafish Calsyntenins mediate homophilic adhesion through their amino-terminal cadherin repeats

Authors
Ortiz-Medina, H., Emond, M.R., Jontes, J.D.
ID
ZDB-PUB-141203-6
Date
2015
Source
Neuroscience   286: 87-96 (Journal)
Registered Authors
Emond, Michelle, Jontes, James
Keywords
Adhesion, Cadherin, Calsyntenin, Zebrafish
MeSH Terms
  • Animals
  • Brain/embryology
  • Brain/metabolism*
  • Cadherins/genetics*
  • Cadherins/metabolism*
  • Cell Adhesion/genetics*
  • Embryo, Nonmammalian/metabolism
  • Gene Expression
  • Zebrafish
  • Zebrafish Proteins/genetics*
  • Zebrafish Proteins/metabolism*
PubMed
25463516 Full text @ Neuroscience
Abstract
The calsyntenins are atypical members of the cadherin superfamily that have been implicated in learning in C. 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 hompphilic 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.
Genes / Markers
Figures
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Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping