title: Dendrite-like process formation and cytoskeletal remodeling regulated by delta-catenin expression.
abstract: Actin- and microtubule-mediated changes in cell shape are essential for many cellular activities. However, the molecular mechanisms underlying the interplay between the two are complex and remain obscure. Here we show that the expression of delta-catenin (or NPRAP/Neurojungin), a member of p120(ctn) subfamily of armadillo proteins can induce the branching of dendrite-like processes in 3T3 cells and enhance dendritic morphogenesis in primary hippocampal neurons. This induction of branching phenotype involves initially the disruption of filamentous actin, and requires the growth of microtubules. The carboxyl-terminal truncation mutant of delta-catenin can cluster and redistribute the full-length protein, and dominantly inhibit its branching effect. delta-Catenin forms protein complexes and can bind directly to actin in vitro. The carboxyl-terminal truncation of delta-catenin does not interfere with its actin-binding capability; therefore the actin interaction alone is not sufficient for the induction of dendrite-like processes. When delta-catenin-transformed cells establish elaborate dendrite-like branches, the main cellular processes become stabilized and resist the disruption of both actin filaments and microtubules, as determined by fluorescent light microscopy and time-lapse recording analyses. We suggest that delta-catenin can effect a biphasic cytoskeletal remodeling event which differentially regulates actin and microtubules and promotes cellular morphogenesis.
authors.affiliation: Department of Anatomy and Cell Biology, The Brody School of Medicine at East Carolina University, Greenville, North Carolina 27858, USA.
authors.forename: Kwonseop
authors.initials: K
authors.lastname: Kim
authors.forename: Anna
authors.initials: A
authors.lastname: Sirota
authors.forename: Yan-hua
authors.initials: YH
authors.lastname: Chen Yh
authors.forename: Shiloh B
authors.initials: SB
authors.lastname: Jones
authors.forename: Ronald
authors.initials: R
authors.lastname: Dudek
authors.forename: George W
authors.initials: GW
authors.lastname: Lanford
authors.forename: Chittam
authors.initials: C
authors.lastname: Thakore
authors.forename: Qun
authors.initials: Q
authors.lastname: Lu
mesh_terms: D016475:3T3 Cells; D008841:Actin Cytoskeleton / Q000187:drug effects / Q000648:ultrastructure; D000818:Animals; D051186:Armadillo Domain Proteins; D051177:Catenins; D015815:Cell Adhesion Molecules; D048429:Cell Size; D002478:Cells, Cultured; D015638:Cytochalasin D / Q000494:pharmacology; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D003599:Cytoskeleton / Q000648:ultrastructure*; D003712:Dendrites / Q000648:ultrastructure; D006624:Hippocampus / Q000254:growth & development / Q000378:metabolism / Q000648:ultrastructure; D007700:Kinetics; D051379:Mice; D008870:Microtubules / Q000378:metabolism / Q000648:ultrastructure; D008954:Models, Biological; D009024:Morphogenesis; D009474:Neurons / Q000378:metabolism / Q000648:ultrastructure; D010750:Phosphoproteins; D017384:Sequence Deletion; D014162:Transfection; D000095002:Delta Catenin
chemical_list: D051186:Armadillo Domain Proteins; D051177:Catenins; D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins; D010750:Phosphoproteins; D015638:Cytochalasin D; D000095002:Delta Catenin; C000722350:Ctnnd2 protein, mouse; C000722349:Ctnnd1 protein, mouse