Cited by 24RNA Research and SplicingNeuroscience and Neuropharmacology ResearchGenetics and Neurodevelopmental Disorders

Somatodendritic localization and mRNA association of the splicing regulatory protein Sam68 in the hippocampus and cortex

Grange, Julien, Boyer, Véronique, Fabian‐Fine, Ruth, Fredj, Naïla Ben, Sadoul, Rémy, Goldberg, Yves·2004·Journal of Neuroscience Research

Abstract

The RNA‐binding protein Sam68 has been implicated in the signal‐dependent processing of pre‐mRNA and in the utilization of intron‐containing retroviral mRNAs. Sam68 is predominantly nuclear but exhibits remarkable binding affinity for signalling proteins located at the membrane. We have investigated the subcellular distribution of Sam68 in adult rat cortex and hippocampus. Subcellular fractionation showed that the protein was most abundant in nuclei but also was present at a significant level in the cytosol and membrane fractions, including light and synaptic membranes derived from crude synaptosomes. Sam68 extracted from the synaptosomal fraction cosedimented with polysomes on sucrose gradients. In agreement with these findings, immunohistochemical staining indicated that Sam68 was concentrated in neuronal nuclei but was also detectable in the soma and dendrites. Sam68 immunoreactivity examined at the ultrastructural level was found to associate with dendritic microtubules, endoplasmic reticulum, and free polyribosomes, sometimes close to synapses. A combination of immunoprecipitation and RT‐PCR directly confirmed that Sam68 was bound to polyadenylated mRNA in cortical lysates. The αCaMKII mRNA was identified as one of the coprecipitated transcripts; in contrast, the gephyrin and NR1‐1 mRNAs were not coprecipitated, indicating a certain degree of sequence specificity in the association. In electrophoretic mobility shift assays, recombinant GST‐Sam68 as well as brain‐derived Sam68 bound with high affinity to the αCaMKII 3′ untranslated region. These results suggest that Sam68 may accompany and, conceivably, regulate mature mRNAs during nuclear export, somatodendritic transport, and translation. © 2004 Wiley‐Liss, Inc.

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Crossref · 10.1002/jnr.20003

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  • SAM68 is found in both the nucleus and the cytosol of many cell types and affects a variety of cellular processes, including splicing in the nucleus.

    “SAM68 is found in both the nucleus and the cytosol of many cell types81 and affects a variety of cellular processes, including splicing in the nucleus82,83.”

    From The neurogenetics of alternative splicing (2016) · cites this paper as [83]

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Authors
Grange, J., Boyer, V., Fabian‐Fine, R., Fredj, N. B., Sadoul, R., & Goldberg, Y.
Affiliations
  • Inserm (FR)
  • Dalhousie University (CA)
Corresponding author
Goldberg, Yves
Venue
Journal of Neuroscience Research
Publisher
Wiley
Published
2004-01-26
Volume
75
Issue
5
Pages
654-666
ISSN
  • 0360-4012 (ISSN-L)
  • 1097-4547
OpenAlex
W2067867820
Cited by
24
References
47
Citations by year
2024: 1 · 2018: 2 · 2016: 2 · 2015: 1 · 2012: 1
FWCI
0.47
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Neuroscience Research (publishedVersion)
  • PubMed (publishedVersion)
Funders
Killam Trusts
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
Keywords
Sam68, RNA-binding proteins, hippocampus, cerebral cortex, subcellular localization, synaptosomes, dendritic microtubules, polysomes, 3' untranslated region, nuclear export, mRNA transport, translational regulation
MeSH terms
Animals, Cell Nucleus, Cerebral Cortex, Dendrites, Hippocampus, Immunohistochemistry, Male, Neurons, Polyribosomes, Rats, Inbred Strains, RNA, Messenger, Subcellular Fractions, Synaptosomes, RNA-Binding Proteins, Calcium-Calmodulin-Dependent Protein Kinases, Protein Transport, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2

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