Key result
Interaction with and release from mRNA and translation complexes are important in determining the sub-cellular distribution of cytoplasmic poly(A)-binding proteins.
Proposes an integrated model for the regulated nucleo-cytoplasmic transport of PABPs in response to cellular stress.
No immediate clinical implications; leaves open PABP dynamics in human stress responses.
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.
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Burgess et al. (2012) studied this question. Interaction with and release from mRNA and translation complexes are important in determining the sub-cellular distribution of cytoplasmic poly(A)-binding proteins.
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