Stress Granules (SGs) are microscopically visible, phase dense aggregates of translationally stalled messenger ribonucleoprotein (mRNP) complexes formed in response to distinct stress conditions. It is generally considered that the SG formation is induced to protect cells from stress. The precise constituents of SGs and how SGs are dynamically regulated in response to stresses are incompletely understood. Hence, it is important to identify proteins which regulate SG assembly and disassembly. Here, we report that NRG2 is a novel SG component whose depletion potently inhibits the SG formation. We show that NRG2 specifically localizes to SGs under various stress conditions. Knockdown of NRG2 has no effect on stress-induced polysome disassembly suggesting that NRG2 does not influence the early step of SG formation. We also found that reduced expression of NRG2 marginally increases cell survival under arsenite stress.