Pim serine/threonine kinases regulate the stability of Socs-1 protein.

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.
Mesh Terms:
Animals, Carrier Proteins, Cell Line, Cloning, Molecular, DNA, Complementary, Gene Library, Glutathione Transferase, Humans, Interleukin-4, Intracellular Signaling Peptides and Proteins, Luciferases, Mice, Phosphorylation, Plasmids, Precipitin Tests, Protein Binding, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-pim-1, RNA, Messenger, Recombinant Fusion Proteins, Repressor Proteins, STAT6 Transcription Factor, Signal Transduction, Suppressor of Cytokine Signaling Proteins, Thymus Gland, Time Factors, Trans-Activators, Transfection, Two-Hybrid System Techniques
Proc. Natl. Acad. Sci. U.S.A.
Date: Feb. 19, 2002
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