Stress granules (SGs), a type of RNA foci, were formed in the cytoplasm of eukaryotic cells upon some unfavorable environmental stress. Previously, we found that Tudor domain containing 1 (SND1)-containing SGs actively communicate with the nuclear and cytosolic pool of HeLa cells. Here, we are interested to investigate the dynamic distribution of three nuclear proteins, including heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1), Hu Antigen R (HuR) and T cell intracellular antigen 1 (TIA1), in the SG aggregation and nucleus/cytoplasm localization under stress condition. We found that hnRNP A1, HuR and TIA1-containing SGs were aggregated in the cytoplasm of HeLa cells, and accompanies the alteration of nucleus/cytoplasm localization during arsenite induced-oxidative stress. Increased hnRNP A1 fluorescence signal within cytoplasm was detected from 3% of normal cells to the 28% of stressed cells; in contrast, 87% of cells with strong hnRNP A1 signal within nucleus reduced to 50% during stress. In addition, transport receptor importin-β pathway seems to be involved in the nuclear import of hnRNP A1, rather than HuR and TIA1. However, the slightly enhanced cytoplasmic accumulation of hnRNP A1 can not influence the formation of hnRNP A1 granules during oxidative stress. Timely and effective dynamic distribution of specific stress-associated proteins in the section of nucleus, cytoplasm, and SG structure is more likely to contribute to the minimization of the detrimental condition-induced cellular damage.