期刊
JOURNAL OF NEUROSCIENCE
卷 32, 期 8, 页码 2628-2636出版社
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.2901-11.2012
关键词
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资金
- US National Institutes of Health [NS39471, NS353862, NS035546, NS072129]
- US National Science Foundation [1121095]
- United States Israel Binational Science Foundation [2007425]
- Pritzker family
- Division Of Integrative Organismal Systems
- Direct For Biological Sciences [1121095] Funding Source: National Science Foundation
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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