ArticleMolecular and cellular biology2003
Protein kinase C phosphorylates ribosomal protein S6 kinase betaII and regulates its subcellular localization.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 73 citations in OpenAlex.
- S6K2 in Focus: Signaling Pathways, Post-Translational Modifications, and Computational Analysis.International journal of molecular sciences · 2024Review
- Article
- Asymmetric Dimethylation of Ribosomal S6 Kinase 2 Regulates Its Cellular Localisation and Pro-Survival Function.International journal of molecular sciences · 2023Article
- Beyond controlling cell size: functional analyses of S6K in tumorigenesis.Cell death & disease · 2022Review
- MAPPINGS, a tool for network analysis of large phospho-signalling datasets: application to host erythrocyte response toCurrent research in microbial sciences · 2022Article
- Repurposed floxacins targeting RSK4 prevent chemoresistance and metastasis in lung and bladder cancer.Science translational medicine · 2021Article
- Protein kinase Cα regulates the nucleocytoplasmic shuttling of KRIT1.Journal of cell science · 2021Article
- Cytosolic calcium regulates cytoplasmic accumulation of TDP-43 through Calpain-A and Importin α3.eLife · 2020Article
- S6K1 blockade overcomes acquired resistance to EGFR-TKIs in non-small cell lung cancer.Oncogene · 2020Article
- Distinct Roles of mTOR Targets S6K1 and S6K2 in Breast Cancer.International journal of molecular sciences · 2020Review
- Inhibition of protein kinase C activity inhibits osteosarcoma metastasis.Archives of medical science : AMS · 2019Article
- Evolving mechanisms of vascular smooth muscle contraction highlight key targets in vascular disease.Biochemical pharmacology · 2018Review
- Signaling Pathways Involved in the Regulation of mRNA Translation.Molecular and cellular biology · 2018Review
- Blocking Stemness and Metastatic Properties of Ovarian Cancer Cells by Targeting p70Molecular therapy : the journal of the American Society of Gene Therapy · 2018Article
- Loss of mTORC1 signalling impairs β-cell homeostasis and insulin processing.Nature communications · 2017Article
- A next-generation microarray further reveals stage-enriched gene expression pattern in the blood fluke Schistosoma japonicum.Parasites & vectors · 2017Article
- Protein Kinase C as Regulator of Vascular Smooth Muscle Function and Potential Target in Vascular Disorders.Advances in pharmacology (San Diego, Calif.) · 2017Review
- Time-varying causal inference from phosphoproteomic measurements in macrophage cells.IEEE transactions on biomedical circuits and systems · 2014Article
- Drug synergy screen and network modeling in dedifferentiated liposarcoma identifies CDK4 and IGF1R as synergistic drug targets.Science signaling · 2013Article
- Molecular Characterization and Expression Analysis of S6K1 in Cashmere Goats (Capra hircus).Asian-Australasian journal of animal sciences · 2013Article
Corrections and comments
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Authors and funding
15 authors at 6 institutions in 4 countries.
Funding
Abstract
The ribosomal protein S6 kinase (S6K) belongs to the AGC family of Ser/Thr kinases and is known to be involved in the regulation of protein synthesis and the G(1)/S transition of the cell cycle. There are two forms of S6K, termed S6Kalpha and S6Kbeta, which have cytoplasmic and nuclear splice variants. Nucleocytoplasmic shuttling has been recently proposed for S6Kalpha, based on the use of the nuclear export inhibitor, leptomycin B. However, the molecular mechanisms regulating subcellular localization of S6Ks in response to mitogenic stimuli remain to be elucidated. Here we present data on the in vitro and in vivo phosphorylation of S6Kbeta, but not S6Kalpha, by protein kinase C (PKC). The site of phosphorylation was identified as S486, which is located within the C-terminal nuclear localization signal. Mutational analysis and the use of phosphospecific antibodies provided evidence that PKC-mediated phosphorylation at S486 does not affect S6K activity but eliminates the function of its nuclear localization signal and causes retention of an activated form of the kinase in the cytoplasm. Taken together, this study uncovers a novel mechanism for the regulation of nucleocytoplasmic shuttling of S6KbetaII by PKC-mediated phosphorylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.