Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and 4 in lymphoid and myeloid cells

MANY cytokines function through interaction with receptors of the cytokine receptor superfamily. Although lacking catalytic domains, cytokine receptors couple ligand binding to induction of protein tyrosine phosphorylation. Recent studies 1–10 have shown that one or more of the Janus kinase family m...

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Veröffentlicht in:Nature (London) 1994-07, Vol.370 (6485), p.153-157
Hauptverfasser: Witthuhn, Bruce A, Silvennoinen, Olli, Miura, Osamu, Lai, Koon Siew, Cwik, Christopher, Liu, Edison T, Ihle, James N
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container_end_page 157
container_issue 6485
container_start_page 153
container_title Nature (London)
container_volume 370
creator Witthuhn, Bruce A
Silvennoinen, Olli
Miura, Osamu
Lai, Koon Siew
Cwik, Christopher
Liu, Edison T
Ihle, James N
description MANY cytokines function through interaction with receptors of the cytokine receptor superfamily. Although lacking catalytic domains, cytokine receptors couple ligand binding to induction of protein tyrosine phosphorylation. Recent studies 1–10 have shown that one or more of the Janus kinase family members (Jaks) associate with cytokine receptors and are tyrosine phosphorylated and activated following ligand binding. Here we describe a new Jak family kinase, Jak-3, and demonstrate that Jak-3, and to a lesser extent Jak-1, are tyrosine phosphorylated and Jak-3 is activated in the responses to interleukin-2 and interleukin–4 in T cells and myeloid cells. Jak-3 activation requires the serine-rich, membrane-proximal domain of the interleukin-2 receptor β-chain, but does not require the acidic domain that is required for association and activation of Src family kinases.
doi_str_mv 10.1038/370153a0
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Although lacking catalytic domains, cytokine receptors couple ligand binding to induction of protein tyrosine phosphorylation. Recent studies 1–10 have shown that one or more of the Janus kinase family members (Jaks) associate with cytokine receptors and are tyrosine phosphorylated and activated following ligand binding. Here we describe a new Jak family kinase, Jak-3, and demonstrate that Jak-3, and to a lesser extent Jak-1, are tyrosine phosphorylated and Jak-3 is activated in the responses to interleukin-2 and interleukin–4 in T cells and myeloid cells. 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subjects Amino Acid Sequence
Animals
Biochemistry
Biological and medical sciences
Bone Marrow - physiology
Bone Marrow Cells
Cell Line
Cytokines - physiology
Enzyme Activation - physiology
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Humanities and Social Sciences
Immunobiology
Interleukin-2 - physiology
Interleukin-4 - physiology
Janus Kinase 3
letter
Lymphocytes - physiology
Lymphoid cells: ontogeny, maturation, markers, receptors, circulation and recirculation
Mice
Molecular Sequence Data
multidisciplinary
Organ Specificity
Precipitin Tests
Protein-Tyrosine Kinases - physiology
Science
Science (multidisciplinary)
Sequence Homology, Amino Acid
Signal Transduction - physiology
title Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and 4 in lymphoid and myeloid cells
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