Basal enrichment within neuroepithelia suggests novel function(s) for Celsr1 protein

Mol Cell Neurosci. 2010 Jul;44(3):210-22. doi: 10.1016/j.mcn.2010.03.008. Epub 2010 Mar 28.

Abstract

A characteristic of the 7TM-cadherins, Flamingo and Celsr1, is their asymmetric protein distribution and polarized activity at neighboring epithelial cell interfaces along defined axes of planar cell polarity. Here, we describe a novel distribution of Celsr1 protein to the basal surface of neuroepithelial cells within both the early neural tube and a less well-defined group of ventricular zone cells at the midline of the developing spinal cord. Importantly, this basal enrichment is lost in embryos homozygous for a mutant Celsr1 allele. We also demonstrate an intimate association between basal enrichment of Celsr1 protein and dorsal sensory tract morphogenesis, an intriguing spatio-temporal organization of Celsr1 protein along the apico-basal neuroepithelial axis suggestive of multiple Celsr1 protein isoforms and the existence of distinct cell surface Celsr1 protein species with direct signaling potential. Together, these data raise compelling new questions concerning the role of Celsr1 during neural development.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cell Polarity / physiology*
  • Embryo, Mammalian / anatomy & histology
  • Embryo, Mammalian / physiology*
  • Mice
  • Molecular Sequence Data
  • Morphogenesis / physiology
  • Neuroepithelial Cells / cytology*
  • Neuroepithelial Cells / metabolism
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism*
  • Receptors, G-Protein-Coupled / genetics
  • Receptors, G-Protein-Coupled / metabolism*
  • Sequence Alignment
  • Spinal Cord / cytology
  • Spinal Cord / embryology*
  • Spinal Cord / metabolism*

Substances

  • Celsr1 protein, mouse
  • Protein Isoforms
  • Receptors, G-Protein-Coupled