{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Eisinger-Mathason TS"],"funding":["NCI NIH HHS","NIGMS NIH HHS"],"pagination":["722-36"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2654589"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(5)"],"pubmed_abstract":["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."],"journal":["Molecular cell"],"pubmed_title":["Codependent functions of RSK2 and the apoptosis-promoting factor TIA-1 in stress granule assembly and cell survival."],"pmcid":["PMC2654589"],"funding_grant_id":["R01 GM037537","GM084386","R01 GM050526","R01 GM084386","T32 CA009109","T32CA009109-30","GM50526","R01 GM084386-01"],"pubmed_authors":["Muratore-Schroeder TL","Lannigan DA","Groehler AL","Shabanowitz J","Hunt DF","Macara IG","Pasic L","Eisinger-Mathason TS","Smith JA","Clark DE","Andrade J"],"additional_accession":[]},"is_claimable":false,"name":"Codependent functions of RSK2 and the apoptosis-promoting factor TIA-1 in stress granule assembly and cell survival.","description":"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.","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Sep","modification":"2020-10-29T10:18:55Z","creation":"2019-03-27T00:21:10Z"},"accession":"S-EPMC2654589","cross_references":{"pubmed":["18775331"],"doi":["10.1016/j.molcel.2008.06.025"]}}