title: RAE-1, a novel PHR binding protein, is required for axon termination and synapse formation in Caenorhabditis elegans.
abstract: Previous studies in Caenorhabditis elegans showed that RPM-1 (Regulator of Presynaptic Morphology-1) regulates axon termination and synapse formation. To understand the mechanism of how rpm-1 functions, we have used mass spectrometry to identify RPM-1 binding proteins, and have identified RAE-1 (RNA Export protein-1) as an evolutionarily conserved binding partner. We define a RAE-1 binding region in RPM-1, and show that this binding interaction is conserved and also occurs between Rae1 and the human ortholog of RPM-1 called Pam (protein associated with Myc). rae-1 loss of function causes similar axon and synapse defects, and synergizes genetically with two other RPM-1 binding proteins, GLO-4 and FSN-1. Further, we show that RAE-1 colocalizes with RPM-1 in neurons, and that rae-1 functions downstream of rpm-1. These studies establish a novel postmitotic function for rae-1 in neuronal development.
authors.affiliation: Department of Pharmacology, University of Minnesota, Minneapolis, MN, USA. bgrill@umn.edu
authors.forename: Brock
authors.initials: B
authors.lastname: Grill
authors.forename: Lizhen
authors.initials: L
authors.lastname: Chen
authors.forename: Erik D
authors.initials: ED
authors.lastname: Tulgren
authors.forename: Scott T
authors.initials: ST
authors.lastname: Baker
authors.forename: Willy
authors.initials: W
authors.lastname: Bienvenut
authors.forename: Matthew
authors.initials: M
authors.lastname: Anderson
authors.forename: Manfredo
authors.initials: M
authors.lastname: Quadroni
authors.forename: Yishi
authors.initials: Y
authors.lastname: Jin
authors.forename: Craig C
authors.initials: CC
authors.lastname: Garner
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000235:genetics / Q000378:metabolism; D020816:Amino Acid Motifs / Q000235:genetics; D000595:Amino Acid Sequence / Q000235:genetics; D000818:Animals; D030801:Animals, Genetically Modified; D001369:Axons / Q000502:physiology*; D017173:Caenorhabditis elegans; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism; D044783:F-Box Proteins / Q000235:genetics / Q000378:metabolism; D005786:Gene Expression Regulation / Q000235:genetics; D020662:Guanine Nucleotide Exchange Factors / Q000235:genetics / Q000378:metabolism; D006801:Humans; D047468:Immunoprecipitation; D008164:Luminescent Proteins / Q000235:genetics; D013058:Mass Spectrometry; D008465:Mechanoreceptors / Q000166:cytology*; D018613:Microscopy, Confocal; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D034521:Nuclear Matrix-Associated Proteins / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D029543:Nucleocytoplasmic Transport Proteins / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding / Q000235:genetics; D015398:Signal Transduction / Q000235:genetics; D013569:Synapses / Q000235:genetics / Q000502:physiology*; D044767:Ubiquitin-Protein Ligases / Q000235:genetics / Q000378:metabolism; D020691:rab GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D029742:Caenorhabditis elegans Proteins; D044783:F-Box Proteins; C530278:FSN-1 protein, C elegans; D020662:Guanine Nucleotide Exchange Factors; D008164:Luminescent Proteins; D034521:Nuclear Matrix-Associated Proteins; D029543:Nucleocytoplasmic Transport Proteins; C490522:RAE1 protein, human; C409634:RPM-1 protein, C elegans; C114022:MYCBP2 protein, human; D044767:Ubiquitin-Protein Ligases; C505598:Glo-1 protein, C elegans; D020691:rab GTP-Binding Proteins