Stress granules are phase dense particles containing mRNA in stalled initiation complexes which are protected from degradation. Stress granules are formed in the cytoplasm of eukaryotic cells under environmental stresses such as heat, oxidative stress, hyperosmolarity and UV and form the mechanism by which cells selectively turn off translation of constitutively expressed “housekeeping” transcripts under stress. Hu antigen R (HuR) is an RNA binding protein found in stress granules, which binds to AU rich elements in mRNA. The role of HuR in stress granule assembly and disassembly is poorly understood. Here we investigate the interactions of HuR with stress granule associated proteins. Using surface plasmon resonance we are able to examine the kinetics and affinity of HuR binding. These studies shed light on the interactions of HuR leading to stress granule formation.