TY - JOUR
T1 - Basal enrichment within neuroepithelia suggests novel function(s) for Celsr1 protein
AU - Formstone, Caroline
AU - Moxon, Christopher
AU - Murdoch, Jennifer
AU - Little, Peter
AU - Mason, Ivor
PY - 2010/7
Y1 - 2010/7
N2 - 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. (C) 2010 Elsevier Inc. All rights reserved.
AB - 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. (C) 2010 Elsevier Inc. All rights reserved.
U2 - 10.1016/j.mcn.2010.03.008
DO - 10.1016/j.mcn.2010.03.008
M3 - Article
VL - 44
SP - 210
EP - 222
JO - Molecular and Cellular Neurosciences
JF - Molecular and Cellular Neurosciences
IS - 3
ER -