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Interaction and colocalization of HERMES / RBPMS with NonO, PSF , and G3 BP 1 in neuronal cytoplasmic RNP granules in mouse retinal line cells
Author(s) -
Furukawa Mari T.,
Sakamoto Hiroshi,
Inoue Kunio
Publication year - 2015
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/gtc.12224
Subject(s) - biology , microbiology and biotechnology , colocalization , cytoplasm , stress granule , neurite , rna binding protein , granule (geology) , rna , messenger rna , biochemistry , paleontology , translation (biology) , in vitro , gene
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 ( RGC s) 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. G3 BP 1, 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 KIF 5 interacts with neuronal granules, the localization of KIF 5A overlapped with the cytoplasmic granules in differentiated RGC ‐5 cells. Thus, our study strongly suggests that the cytoplasmic granule containing HERMES , NonO, PSF , and G3 BP 1 is a neuronal RNA –protein granule that is transported in neurites during retinal differentiation.