Journal
MOLECULAR CELL
Volume 31, Issue 5, Pages 722-736Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2008.06.025
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Funding
- NCI NIH HHS [T32 CA009109, T32CA009109-30] Funding Source: Medline
- NIGMS NIH HHS [GM50526, R01 GM050526, R01 GM037537, GM084386, R01 GM084386, R01 GM084386-01] Funding Source: Medline
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Stress granules aid cell survival in response to environmental stressors; by acting as sites of translational repression. We report an unanticipated link between stress granules and the serine/threonine kinase RSK2. In stressed breast cells, endogenous RSK2 colocalizes in granules with TIA-1 and poly(A)-binding protein 1, and the sequestration of RSK2 and TIA-1 exhibits codependency. The RSK2 N-terminal kinase domain controls the direct interaction with the prion-related domain of TIA-1. Silencing RSK2 decreases cell survival in response to stress. Mitogen releases RSK2 from the stress granules and permits its nuclear import via a nucleocytoplasmic shuttling sequence in the C-terminal domain. Nuclear accumulation is dependent on TIA-1. Surprisingly, nuclear localization of RSK2 is sufficient to enhance proliferation through induction of cyclin D1, in the absence of other active signaling pathways. Hence, RSK2 is a pivotal factor linking the stress response to survival and proliferation.
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