PUBLICATION

Semaphorin/neuropilin binding specificities are stable over 400 million years of evolution

Authors
He, Z., Crenshaw, E., Raper, J.A.
ID
ZDB-PUB-190729-12
Date
2019
Source
Biochemical and Biophysical Research Communications   517(1): 23-28 (Journal)
Registered Authors
Raper, Jonathan
Keywords
Axonal guidance, Evolutionary conservation, Neuropilins, Semaphorins
MeSH Terms
  • Animals
  • Biological Evolution
  • Humans
  • Mice
  • Neuropilins/genetics
  • Neuropilins/metabolism*
  • Phylogeny
  • Protein Binding
  • Semaphorins/genetics
  • Semaphorins/metabolism*
  • Species Specificity
  • Zebrafish
PubMed
31349972 Full text @ Biochem. Biophys. Res. Commun.
Abstract
Semaphorins are a large and important family of signaling molecules conserved in Bilateria. An important determinant of the biological function of their largest class, the secreted class 3 semaphorins, is the specificity of their binding to neuropilins, a key component of a larger holoreceptor complex. We compared these binding specificities in mice and zebrafish, species whose most recent common ancestor was more than 400 million years in the past. We also compared the binding specificities of zebrafish class 3 semaphorins that were duplicated very early within the teleost lineage. We found a surprising conservation of neuropilin binding specificities when comparing both paralogous zebrafish semaphorin pairs and orthologous zebrafish and mouse semaphorin pairs. This finding was further supported by a remarkable conservation of binding specificities in cross-species pairings of semaphorins and neuropilins. Our results suggest that the qualitative specificities with which particular semaphorins bind to particular neuropilins has remained nearly invariant over approximately 400 million years of evolution.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping