Eukaryotic cells are able to respond promptly to environmental stresses at the level of mRNA translation. In response to heat, starvation, oxidative stress and viral infection cytoplasmic granules known as stress granules (SGs) are formed by quick sequestration of target mRNAs bound by their associated proteins. T-cell intracellular antigen-1 (TIA-1) is an RNA binding protein, which continuously shuttles between the nucleus and the cytoplasm. Upon stress TIA protein accumulate in the cytoplasm along with its bound mRNA. In particular, TIA-1 binds to mRNA containing A/U-rich elements in their 3’UTR and then escorts the translationally stalled mRNA into stress granule through the aggregation of its prion related domain (PRD). TIA-1 possesses three RNA recognition motifs RRM1, RRM2, RRM3 and a PRD, among the domains, RRM2 is the major RNA recognition domain for U and A/U-rich sequences. Here we report the first crystal structure of RRM2 engaged with nucleic acid. We also investigate the affect of TIA serine phosphorylation and the other components of stress granule on the amyloid-like properties of TIA-1 aggregation and cytoplasmic accumulation.