Pim serine/threonine kinases regulate the stability of Socs-1 protein
AUTOR(ES)
Chen, X. Peter
FONTE
The National Academy of Sciences
RESUMO
Studies of SOCS-1-deficient mice have implicated Socs-1 in the suppression of JAK-STAT (Janus tyrosine kinase-signal transducers and activators of transcription) signaling and T cell development. It has been suggested that the levels of Socs-1 protein may be regulated through the proteasome pathway. Here we show that Socs-1 interacts with members of the Pim family of serine/threonine kinases in thymocytes. Coexpression of the Pim kinases with Socs-1 results in phosphorylation and stabilization of the Socs-1 protein. The protein levels of Socs-1 are significantly reduced in the Pim-1−/−, Pim-2−/− mice as compared with wild-type mice. Similar to Socs-1−/− mice, thymocytes from Pim-1−/−, Pim-2−/− mice showed prolonged Stat6 phosphorylation upon IL-4 stimulation. These data suggest that the Pim kinases may regulate cytokine-induced JAK-STAT signaling through modulation of Socs-1 protein levels.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=122338Documentos Relacionados
- Structural basis and prediction of substrate specificity in protein serine/threonine kinases
- The serine/threonine kinase Pim-2 is a transcriptionally regulated apoptotic inhibitor
- Eukaryotic phytochromes: Light-regulated serine/threonine protein kinases with histidine kinase ancestry
- Autoregulation of the Raf-1 serine/threonine kinase
- Activation of the pp90rsk and mitogen-activated serine/threonine protein kinases by ionizing radiation.
