title: delta-catenin is a nervous system-specific adherens junction protein which undergoes dynamic relocalization during development.
abstract: delta-catenin is a member of the Armadillo repeat family and component of the adherens junction discovered in a two-hybrid assay as a bona fide interactor with presenilin-1 (Zhou et al., [1997], NeuroReport 8:2085-2090), a protein which carries mutations that cause familial Alzheimer's disease. The expression pattern of delta-catenin was mapped between embryonic day 10 (E10) and adulthood by Northern blots, in situ hybridization and immunohistochemistry in the mouse. In development, delta-catenin is dynamically regulated with respect to its site of expression. It is first expressed within proliferating neuronal progenitor cells of the neuroepithelium, becomes down-regulated during neuronal migration, and is later reexpressed in the dendritic compartment of postmitotic neurons. In the mouse, delta-catenin mRNA is expressed by E10, increases and peaks at postnatal day (P)7, with lower levels in adulthood. In the developing neocortex, delta-catenin mRNA is strongly expressed in the proliferative ventricular zone and the developing cortical plate, yet is conspicuously less prominent in the intermediate zone, which contains migrating cortical neurons, delta-catenin protein forms a honeycomb pattern in the neuroepithelium by labeling the cell periphery in a typical adherens junction pattern. By E18, delta-catenin expression shifts primarily to nascent apical dendrites, a pattern that continues through adulthood. The dynamic relocalization of delta-catenin expression during development, taken together with previously published data which described a role for delta-catenin in cell motility (Lu et al., [1999] J. Cell. Biol. 144:519-532), suggests the hypothesis that delta-catenin regulation is closely linked to neuronal migration and may play a role in the establishment of mature dendritic relationships in the neuropil.
authors.affiliation: Department of Neurology, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA.
authors.forename: C
authors.initials: C
authors.lastname: Ho
authors.forename: J
authors.initials: J
authors.lastname: Zhou
authors.forename: M
authors.initials: M
authors.lastname: Medina
authors.forename: T
authors.initials: T
authors.lastname: Goto
authors.forename: M
authors.initials: M
authors.lastname: Jacobson
authors.forename: P G
authors.initials: PG
authors.lastname: Bhide
authors.forename: K S
authors.initials: KS
authors.lastname: Kosik
mesh_terms: D000818:Animals; D051186:Armadillo Domain Proteins; D051177:Catenins; D015815:Cell Adhesion Molecules; D002465:Cell Movement / Q000502:physiology; D002490:Central Nervous System / Q000166:cytology / Q000196:embryology* / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000032:analysis* / Q000235:genetics*; D004622:Embryo, Mammalian; D051379:Mice; D008815:Mice, Inbred Strains; D009474:Neurons / Q000166:cytology / Q000378:metabolism; D010750:Phosphoproteins; D012333:RNA, Messenger / Q000032:analysis; D013687:Telencephalon / Q000166:cytology / Q000196:embryology / Q000378:metabolism; D019108:Tight Junctions / Q000378:metabolism* / Q000648:ultrastructure; D000095002:Delta Catenin
chemical_list: D051186:Armadillo Domain Proteins; D051177:Catenins; D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins; D010750:Phosphoproteins; D012333:RNA, Messenger; D000095002:Delta Catenin