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A novel 65 kDa RNA-binding protein in squid presynaptic terminals.

D T P Lico¹, J C Rosa, J A DeGiorgis

¹Department of Cellular & Molecular Biology, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, São Paulo 14049-900, Brazil.

|December 17, 2009

Summary

Researchers identified a novel RNA-binding protein, p65, in squid optic lobes. This protein, a heterogeneous nuclear ribonucleoprotein (hnRNP), is localized to presynaptic terminals and may play a role in synaptic RNA localization.

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Area of Science:

Neuroscience
Molecular Biology
Biochemistry

Background:

Myosin V is crucial for intracellular transport.
Identifying novel proteins involved in neuronal function is essential.

Purpose of the Study:

To identify and characterize a 65 kDa polypeptide (p65) recognized by an antibody against chicken myosin Va in squid optic lobes.
To determine the function and localization of p65 within squid neurons.

Main Methods:

Western blotting using polyclonal antibody C4.
Purification of p65 via chromatography.
Mass spectrometry and BLAST analysis for protein identification.
Sucrose gradient centrifugation and RNase treatment.
Immunohistochemistry and immunofluorescence microscopy.

Main Results:

Antibody C4 recognized a 65 kDa polypeptide (p65) in squid optic lobe extracts, distinct from squid myosin V.
Mass spectrometry and sequence analysis identified p65 as belonging to the heterogeneous nuclear ribonucleoprotein (hnRNP) A/B family.
p65 associates with cytoplasmic RNP complexes in an RNA-dependent manner.
Immunolocalization studies revealed p65 is present at presynaptic terminals in the optic lobes and stellate ganglion.

Conclusions:

p65 is a novel RNA-binding protein found in squid presynaptic terminals.
p65 likely plays a role in the synaptic localization, translation, or processing of RNA within neurons.