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Many of the SG proteins that we have characterized so far as well as others that have not yet been ascribed to this stress granule-like structure can be found in both cytosolic and nuclear foci. It is very likely that SGs have a dynamic life that is not static and that a fraction of the SG proteins may diffuse from one cellular compartment to the other with a constant flow of material. This process has been visualized as “assembling/disassembling of SGs”. It is, however, still unclear if these processes are consecutive to each other or if they are two different entities being simultaneously present at the same cellular space.

SFB3 is a FMRP-interacting protein that can shuttle between the cytosol and the nucleus (Kuriyama et al., 2010). While following the subcellular location of this protein using a cytosolic GFP (mChe) fusion protein, we observed that SFB3 accumulates in the nucleus when PB assembly is disrupted in neurons. Our studies in HeLa cells also revealed that the nuclear accumulation of the SFB3-GFP protein that follows the inhibition of the proteasome is dependent on NMD (unpublished observations). This result suggests that the cytosolic SGs that form upon UPS inhibition may be the result of a release of NMD-sensitive mRNAs from the PBs. Since we have also shown that NMD inhibition can trigger the formation of SGs, we suggest the presence of a pool of mRNAs in decaying PBs that can be released following NMD inhibition. Such a pool of mRNAs could be trafficked to the cytoplasm and SG assembly is triggered by a general decrease in translation that occurs upon inhibition of the UPS.

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Facebook Message Recovery Tool 1079 Extra Quality

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