RAE-1, a novel PHR binding protein, is required for axon termination and synapse formation in Caenorhabditis elegans.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
Brock GrillCraig C Garner

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.

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Citations

Mar 12, 2013·Neural Plasticity·Andrew M Hamilton, Karen Zito
Dec 5, 2014·Wiley Interdisciplinary Reviews. Developmental Biology·Salvatore J Cherra, Yishi Jin
Apr 14, 2016·European Journal of Human Genetics : EJHG·Valeria NofriniCristina Mecucci
May 1, 2019·Cellular and Molecular Life Sciences : CMLS·Ardalan HendiKota Mizumoto
Oct 19, 2014·The Journal of Biological Chemistry·Jaiprakash SharmaBrock Grill
Oct 16, 2015·G3 : Genes - Genomes - Genetics·Andrew C GilesBrock Grill
Apr 28, 2020·Neural Development·Andrew C Giles, Brock Grill
Jan 3, 2018·PloS One·Anna StockumGoedele N Maertens
Nov 5, 2019·Nature Communications·Oliver CrawleyBrock Grill

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