Cytoplasmic poly(A)-binding proteins (PABPs) regulate mRNA stability and 
translation. Although predominantly localized in the cytoplasm, PABP proteins 
also cycle through the nucleus. Recent work has established that their 
steady-state localization can be altered by cellular stresses such as 
ultraviolet (UV) radiation, and infection by several viruses, resulting in 
nuclear accumulation of PABPs. Here, we present further evidence that their 
interaction with and release from mRNA and translation complexes are important 
in determining their sub-cellular distribution and propose an integrated model 
for regulated nucleo-cytoplasmic transport of PABPs.