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J Neurosci. 2012 Feb 22;32(8):2628-36. doi: 10.1523/JNEUROSCI.2901-11.2012.

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

Author information

1
Department of Pharmacology, University of Minnesota, Minneapolis, MN, USA. bgrill@umn.edu

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.

PMID:
22357847
PMCID:
PMC3302171
DOI:
10.1523/JNEUROSCI.2901-11.2012
[Indexed for MEDLINE]
Free PMC Article

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