RRC ID 11023
Author Ossipova O, Tabler J, Green JB, Sokol SY.
Title PAR1 specifies ciliated cells in vertebrate ectoderm downstream of aPKC.
Journal Development
Abstract Partitioning-defective 1 (PAR1) and atypical protein kinase C (aPKC) are conserved serine/threonine protein kinases implicated in the establishment of cell polarity in many species from yeast to humans. Here we investigate the roles of these protein kinases in cell fate determination in Xenopus epidermis. Early asymmetric cell divisions at blastula and gastrula stages give rise to the superficial (apical) and the deep (basal) cell layers of epidermal ectoderm. These two layers consist of cells with different intrinsic developmental potential, including superficial epidermal cells and deep ciliated cells. Our gain- and loss-of-function studies demonstrate that aPKC inhibits ciliated cell differentiation in Xenopus ectoderm and promotes superficial cell fates. We find that the crucial molecular substrate for aPKC is PAR1, which is localized in a complementary domain in superficial ectoderm cells. We show that PAR1 acts downstream of aPKC and is sufficient to stimulate ciliated cell differentiation and inhibit superficial epidermal cell fates. Our results suggest that aPKC and PAR1 function sequentially in a conserved molecular pathway that links apical-basal cell polarity to Notch signaling and cell fate determination. The observed patterning mechanism may operate in a wide range of epithelial tissues in many species.
Volume 134(23)
Pages 4297-306
Published 2007-12-1
DOI 10.1242/dev.009282
PII 134/23/4297
PMID 17993468
PMC PMC2170474
MeSH Animals Cilia / enzymology* Ectoderm / enzymology* Ectoderm / physiology Embryo, Nonmammalian / physiology* In Situ Hybridization MicroRNAs / genetics* Protein Kinase C / genetics* Protein Kinase C / metabolism* Protein-Serine-Threonine Kinases / metabolism* Reverse Transcriptase Polymerase Chain Reaction Xenopus / embryology* Xenopus Proteins / genetics* Xenopus Proteins / metabolism*
IF 5.611
Times Cited 35
DNA material pCMX-N/RBP-J (R218H) (RDB03022)