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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ross, Jeremy A. Ruiz-medina, Blanca E. Kirken, Robert A. |
| Description | Author Affiliation: Ruiz-Medina BE ( From the Department of Biological Sciences and Border Biomedical Research Center, The University of Texas at El Paso, El Paso, Texas 79968.); Ross JA ( From the Department of Biological Sciences and Border Biomedical Research Center, The University of Texas at El Paso, El Paso, Texas 79968.); Kirken RA ( From the Department of Biological Sciences and Border Biomedical Research Center, The University of Texas at El Paso, El Paso, Texas 79968 rkirken@utep.edu.) |
| Abstract | T, B, and natural killer cells are required for normal immune response and are regulated by cytokines such as IL-2. These cell signals are propagated following receptor-ligand engagement, controlling recruitment and activation of effector proteins. The IL-2 receptor ß subunit (IL-2Rß) serves in this capacity and is known to be phosphorylated. Tyrosine phosphorylation of the ß chain has been studied extensively. However, the identification and putative regulatory roles for serine and threonine phosphorylation sites have yet to be fully characterized. Using LC-MS/MS and phosphospecific antibodies, a novel IL-2/IL-15 inducible IL-2Rß phosphorylation site (Thr-450) was identified. IL-2 phosphokinetic analysis revealed that phosphorylation of IL-2Rß Thr-450 is rapid (2.5 min), transient (peaks at 15 min), and protracted compared with receptor tyrosine phosphorylation and occurs in multiple cell types, including primary human lymphocytes. Pharmacological and siRNA-mediated inhibition of various serine/threonine kinases revealed ERK1/2 as a positive regulator, whereas purified protein phosphatase 1 (PP1), dephosphorylated Thr-450 in vitro. Reconstitution assays demonstrated that Thr-450 is important for regulating IL-2R complex formation, recruitment of JAK3, and activation of AKT and ERK1/2 and a transcriptionally active STAT5. These results provide the first evidence of the identification and functional characterization for threonine phosphorylation of an interleukin receptor. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 34 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-08-21 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Interleukin-2 Receptor Beta Subunit Metabolism Interleukin-2 Threonine Amino Acid Sequence Cell Line Gene Expression Regulation Genetics Janus Kinase 3 Antagonists & Inhibitors Mitogen-Activated Protein Kinase 1 Mitogen-Activated Protein Kinase 3 Molecular Sequence Data Phosphorylation Protein Phosphatase 1 Proto-Oncogene Proteins C-akt RNA, Small Interfering STAT5 Transcription Factor Serine Signal Transduction Tyrosine Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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