Regulation of cerebral cortical size by control of cell cycle exit in neural precursors.
Transgenic mice expressing a stabilized beta-catenin in neural precursors develop enlarged brains with increased cerebral cortical surface area and folds resembling sulci and gyri of higher mammals. Brains from transgenic animals have enlarged lateral ventricles lined with neuroepithelial precursor cells, reflecting an expansion of the precursor population. Compared with wild-type precursors, a greater proportion of transgenic precursors reenter the cell cycle after mitosis. These results show that beta-catenin can function in the decision of precursors to proliferate or differentiate during mammalian neuronal development and suggest that beta-catenin can regulate cerebral cortical size by controlling the generation of neural precursor cells.
Department of Pathology, Brigham and Women's Hospital, Boston, MA 02115, USA.
Anjen
A
Chenn
Christopher A
CA
Walsh
D000818:Animals; D000911:Antibodies, Monoclonal; D017209:Apoptosis; D051792:Basic Helix-Loop-Helix Proteins; D001921:Brain / Q000033:anatomy & histology / Q000196:embryology; D015816:Cell Adhesion Molecules, Neuronal / Q000235:genetics / Q000378:metabolism; D002452:Cell Count; D002453:Cell Cycle; D002454:Cell Differentiation; D002455:Cell Division; D002540:Cerebral Cortex / Q000033:anatomy & histology / Q000196:embryology* / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D004848:Epithelium / Q000196:embryology; D016326:Extracellular Matrix Proteins / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D017403:In Situ Hybridization; D019394:Ki-67 Antigen / Q000235:genetics / Q000378:metabolism; D051379:Mice; D008822:Mice, Transgenic; D008938:Mitosis; D009419:Nerve Tissue Proteins; D009474:Neurons / Q000166:cytology / Q000378:metabolism / Q000502:physiology*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D000091042:Reelin Protein; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases; D015398:Signal Transduction; D013234:Stem Cells / Q000166:cytology / Q000378:metabolism / Q000502:physiology*; D020825:T-Box Domain Proteins; D015534:Trans-Activators; D051176:beta Catenin; D000098825:Oxysterol Binding Proteins
D000911:Antibodies, Monoclonal; D051792:Basic Helix-Loop-Helix Proteins; D015816:Cell Adhesion Molecules, Neuronal; D003598:Cytoskeletal Proteins; D004268:DNA-Binding Proteins; D016326:Extracellular Matrix Proteins; D005656:Fungal Proteins; D019394:Ki-67 Antigen; D009419:Nerve Tissue Proteins; D011993:Recombinant Fusion Proteins; D000091042:Reelin Protein; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases; D020825:T-Box Domain Proteins; D015534:Trans-Activators; D051176:beta Catenin; C495267:CTNNB1 protein, mouse; C087902:HES1 protein, S cerevisiae; D000098825:Oxysterol Binding Proteins; C489685:Hes5 protein, mouse; C492271:Tbr1 protein, mouse