SND1 protein co-localization with TIA-1 on stress granules under stress stimuli / 天津医药

ABSTRACT

Objective To analyze the association of staphylococcal nuclease domain-containing protein 1(SND1) and T-cell intracellular antigen 1(TIA-1) on stress granules, and the regulation of SND1 on stress granules under stress stimuli. Methods The immunofluorescence assay and laser scanning confocal microscopy were used to observe the co-localization of SND1 protein and TIA-1 protein under stress stimuli, and the over-expression plasmids of pEGFP vector were transfected into HeLa cells and to verify which domain of SND1 co-localized with TIA-1 under stress stimuli. RNA interference-mediated knockdown of the expression of SND1 protein in HeLa cells was measured by Western Blotting assay. Then whether the knockdown of SND1 affected the recruitment of TIA-1 on stress granules was observed. Heat shocks under different times were used to identify whether there were dynamic changes in transportation of SND1 and TIA-1 on stress granules. Results SND1 co-localized with TIA-1 on stress granules under stress stimuli, and the associated domain of SND1 were SN domain. TIA-1 still can be recruited on stress granules but a large amount of stress granules were reduced even though the expression of SND1 protein was decreased. And the transportation of SND1 on stress granules was laged behind TIA-1 under different-times of heat shocks. Conclusion SND1 protein co-localizes with TIA-1 on stress granules, and which co-regulates the cellular stress response under stress stimuli.