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

Brock Grill, Lizhen Chen, Erik D. Tulgren, Scott T. Baker, Willy Bienvenut, Matthew Anderson, Manfredo Quadroni, Yishi Jin, Craig C. Garner

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)2628-2636
Number of pages9
JournalJournal of Neuroscience
Volume32
Issue number8
DOIs
StatePublished - Feb 22 2012
Externally publishedYes

ASJC Scopus subject areas

  • Neuroscience(all)

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