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    A novel SDS-stable dimer of a heterogeneous nuclear ribonucleoprotein at presynaptic terminals of squid neurons

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    Lico et al 2015 revisedMS condensed_with_figures.pdf (747.1Kb)
    Date
    2015-05
    Author
    Lico, Diego T. P.  Concept link
    Lopes, Gabriel S.  Concept link
    Brusco, Janaina  Concept link
    Rosa, José C.  Concept link
    Gould, Robert M.  Concept link
    DeGiorgis, Joseph A.  Concept link
    Larson, Roy E.  Concept link
    Metadata
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    Citable URI
    https://hdl.handle.net/1912/7321
    As published
    https://doi.org/10.1016/j.neuroscience.2015.05.040
    Keyword
     hnRNP; Ribonucleoprotein; Presynaptic terminus; Synaptosome; Elav; Squid 
    Abstract
    The presence of mRNAs in synaptic terminals and their regulated translation are important factors in neuronal communication and plasticity. Heterogeneous nuclear ribonucleoprotein (hnRNP) complexes are involved in the translocation, stability, and subcellular localization of mRNA and the regulation of its translation. Defects in these processes and mutations in components of the hnRNP complexes have been related to the formation of cytoplasmic inclusion bodies and neurodegenerative diseases. Despite much data on mRNA localization and evidence for protein synthesis, as well as the presence of translation machinery, in axons and presynaptic terminals, the identity of RNA-binding proteins involved in RNA transport and function in presynaptic regions is lacking. We previously characterized a strongly basic RNA-binding protein (p65), member of the hnRNP A/B subfamily, in squid presynaptic terminals. Intriguingly, in SDS-PAGE, p65 migrated as a 65 kDa protein, whereas members of the hnRNP A/B family typically have molecular masses ranging from 35 to 42 kDa. In this report we present further biochemical and molecular characterization that shows endogenous p65 to be an SDS-stable dimer composed of ~37 kDa hnRNPA/B-like subunits. We cloned and expressed a recombinant protein corresponding to squid hnRNPA/B-like protein and showed its propensity to aggregate and form SDS-stable dimers in vitro. Our data suggest that this unique hnRNPA/B-like protein co-localizes with synaptic vesicle protein 2 and RNA-binding protein ELAV and thus may serve as a link between local mRNA processing and presynaptic function and regulation.
    Description
    Author Posting. © The Author(s), 2015. This is the author's version of the work. It is posted here by permission of Elsevier for personal use, not for redistribution. The definitive version was published in Neuroscience 300 (2015): 381-392, doi:10.1016/j.neuroscience.2015.05.040.
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    Suggested Citation
    Preprint: Lico, Diego T. P., Lopes, Gabriel S., Brusco, Janaina, Rosa, José C., Gould, Robert M., DeGiorgis, Joseph A., Larson, Roy E., "A novel SDS-stable dimer of a heterogeneous nuclear ribonucleoprotein at presynaptic terminals of squid neurons", 2015-05, https://doi.org/10.1016/j.neuroscience.2015.05.040, https://hdl.handle.net/1912/7321
     

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