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J Comp Neurol. 2017 Oct 15;525(15):3341-3359. doi: 10.1002/cne.24281. Epub 2017 Jul 24.

Proteomic analyses of nucleus laminaris identified candidate targets of the fragile X mental retardation protein.

Author information

1
Virginia Merrill Bloedel Hearing Research Center, Department of Otolaryngology-Head and Neck Surgery, University of Washington, School of Medicine, Seattle, Washington.
2
Department of Biomedical Sciences, Florida State University, Tallahassee, Florida.
3
Department of Genome Sciences, University of Washington, Seattle, Washington.
4
Program in Neuroscience, Florida State University, Tallahassee, Florida.

Abstract

The avian nucleus laminaris (NL) is a brainstem nucleus necessary for binaural processing, analogous in structure and function to the mammalian medial superior olive. In chickens (Gallus gallus), NL is a well-studied model system for activity-dependent neural plasticity. Its neurons have bipolar extension of dendrites, which receive segregated inputs from two ears and display rapid and compartment-specific reorganization in response to unilateral changes in auditory input. More recently, fragile X mental retardation protein (FMRP), an RNA-binding protein that regulates local protein translation, has been shown to be enriched in NL dendrites, suggesting its potential role in the structural dynamics of these dendrites. To explore the molecular role of FMRP in this nucleus, we performed proteomic analysis of NL, using micro laser capture and liquid chromatography tandem mass spectrometry. We identified 657 proteins, greatly represented in pathways involved in mitochondria, translation and metabolism, consistent with high levels of activity of NL neurons. Of these, 94 are potential FMRP targets, by comparative analysis with previously proposed FMRP targets in mammals. These proteins are enriched in pathways involved in cellular growth, cellular trafficking and transmembrane transport. Immunocytochemistry verified the dendritic localization of several proteins in NL. Furthermore, we confirmed the direct interaction of FMRP with one candidate, RhoC, by in vitro RNA binding assays. In summary, we provide a database of highly expressed proteins in NL and in particular a list of potential FMRP targets, with the goal of facilitating molecular characterization of FMRP signaling in future studies.

KEYWORDS:

RNA binding protein; RRID: AB_10615780; RRID: AB_1859928; RRID: AB_2155806; RRID: AB_2277755; RRID: AB_2620155; RRID: AB_297884; RRID: AB_309663; RRID: AB_357520; RRID: AB_776174; RRID: AB_94856; RhoC; autism spectrum disorders; cytoskeletal proteins; dendritic plasticity; gene ontology

PMID:
28685837
PMCID:
PMC5564178
DOI:
10.1002/cne.24281
[Indexed for MEDLINE]
Free PMC Article

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