Interaction and colocalization of HERMES/RBPMS with NonO, PSF, and G3BP1 in neuronal cytoplasmic RNP granules in mouse retinal line cells
| Autor: | Mari T. Furukawa, Kunio Inoue, Hiroshi Sakamoto |
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| Rok vydání: | 2014 |
| Předmět: |
Kinesins
RBPMS RNA-binding protein Biology Retinal ganglion Retina Cell Line Mice Stress granule Genetics Neurites Animals PTB-Associated Splicing Factor Poly-ADP-Ribose Binding Proteins Protein Kinase Inhibitors Neurons RNA recognition motif Granule (cell biology) DNA Helicases Colocalization RNA-Binding Proteins Paraspeckle Cell Differentiation Cell Biology Ribonucleoproteins Small Nuclear Staurosporine Cell biology DNA-Binding Proteins RNA Recognition Motif Proteins Carrier Proteins RNA Helicases |
| Zdroj: | Genes to cells : devoted to molecularcellular mechanisms. 20(4) |
| ISSN: | 1365-2443 |
| Popis: | HERMES, also called RBPMS, is a conserved RNA binding protein with a single RNA recognition motif (RRM) that is abundantly expressed in retinal ganglion cells (RGCs) and in the heart in vertebrates. Here, we identified NonO and PSF as the interacting proteins of HERMES only when the neuronal differentiation of the retinal cell line RGC-5 was induced. Although NonO and PSF are nuclear paraspeckle components, these proteins formed cytoplasmic granules with HERMES in the neurites. G3BP1, a component of stress granules, was also colocalized to the granules, interacting with NonO and HERMES even in the absence of cellular stress. Consistent with a previous report that KIF5 interacts with neuronal granules, the localization of KIF5A overlapped with the cytoplasmic granules in differentiated RGC-5 cells. Thus, our study strongly suggests that the cytoplasmic granule containing HERMES, NonO, PSF, and G3BP1 is a neuronal RNA–protein granule that is transported in neurites during retinal differentiation. |
| Databáze: | OpenAIRE |
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