RGD Reference Report - TLS interaction with NMDA R1 splice variant in retinal ganglion cell line RGC-5. - Rat Genome Database

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TLS interaction with NMDA R1 splice variant in retinal ganglion cell line RGC-5.

Authors: Selamat, W  Jamari, I  Wang, Y  Takumi, T  Wong, F  Fujii, R 
Citation: Selamat W, etal., Neurosci Lett. 2009 Jan 30;450(2):163-6. doi: 10.1016/j.neulet.2008.12.014. Epub 2008 Dec 16.
RGD ID: 9685716
Pubmed: PMID:19103256   (View Abstract at PubMed)
DOI: DOI:10.1016/j.neulet.2008.12.014   (Journal Full-text)

Translocated in liposarcoma (TLS or FUS) is a multifunctional protein component of the heterogenous ribonuclear complex involved in the splicing of pre-mRNA and the export of fully processed mRNA from the nucleus to the cytoplasm. As we determined that TLS was substantially expressed in the adult retina, we investigated the functions of TLS in a rat retinal ganglion cell (RGC) line RGC-5. TLS was found to be associated with N-methyl-d-aspartate (NMDA) receptor 1 (NR1) and myosinVa (MyoVa) in a calcium-dependent manner. We demonstrated that TLS-associated NR1 could be one of the NR1 alternative splice variants, NR1-4, which was predominantly expressed in RGC-5. The degree of colocalization between TLS and NR1 was significantly decreased by depolarization of RGC-5 cells, indicating that the depolarization-induced Ca(2+)-influx triggered a redistribution of NR1 from the TLS-protein complex. These results suggested that TLS might be involved in a calcium-dependent trafficking of specific NR1 splice variants in RGCs.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
FusRatcellular response to calcium ion  IDA  RGD 

Molecular Function

  

Objects Annotated

Genes (Rattus norvegicus)
Fus  (Fus RNA binding protein)
Grin1  (glutamate ionotropic receptor NMDA type subunit 1)
Myo5a  (myosin VA)


Additional Information