title: A Neurexin-related protein, BAM-2, terminates axonal branches in C. elegans.
abstract: Neuronal axons connect to multiple target cells through the formation of collateral branches, but the mechanisms that regulate this process are largely unknown. We show that BAM-2, a neurexin-related transmembrane protein, is required for development of VC motoneuron branches in the worm Caenorhabditis elegans. Expression analysis and ectopic expression experiments suggest that BAM-2 functions as a branch termination cue and reveal a mechanism for selective control of branches that sprout off a primary axon.
authors.affiliation: Department of Biological Sciences, Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305, USA.
authors.forename: Antonio
authors.initials: A
authors.lastname: Colavita
authors.forename: Marc
authors.initials: M
authors.lastname: Tessier-Lavigne
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D030801:Animals, Genetically Modified; D001369:Axons / Q000502:physiology* / Q000648:ultrastructure; D017173:Caenorhabditis elegans / Q000235:genetics / Q000254:growth & development / Q000502:physiology* / Q000648:ultrastructure; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D003463:Cues; D005260:Female; D020869:Gene Expression Profiling; D017238:Genes, Helminth; D020439:Growth Cones / Q000502:physiology; D008024:Ligands; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D008969:Molecular Sequence Data; D009046:Motor Neurons / Q000502:physiology* / Q000648:ultrastructure; D009154:Mutation; D011401:Promoter Regions, Genetic; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D014844:Vulva / Q000166:cytology / Q000294:innervation
chemical_list: C478249:BAM-2 protein, C elegans; D029742:Caenorhabditis elegans Proteins; D008024:Ligands; D008565:Membrane Proteins; D011993:Recombinant Fusion Proteins