Signal transduction by MAP kinases in T lymphocytes
TLDR
This work presents a novel probabilistic construct called a “spatially aggregating immune checkpoints” that are able to be distinguished between the immune checkpoints of the immune system and other immune checkpoints.Abstract:
Immunobiology Program, Department of Medicine, University of Vermont, Burlington, Vermont, VT 05405, USA; Howard Hughes Medical Institute and Section of Immunobiology, Yale University School of Medicine, New Haven, Connecticut CT 06520, USA; Howard Hughes Medical Institute and Program in Molecular Medicine, Department of Biochemistry & Molecular Biology, University of Massachussetts Medical School, Worcester, Massachusetts, MA 01605, USAread more
Citations
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The JNK signal transduction pathway.
Claire R. Weston,Roger J. Davis +1 more
TL;DR: Insight into the role of scaffold proteins that may assemble functional JNK modules has been achieved and a small molecule pharmacological inhibitor of JNK has been described and it is likely that this drug will facilitate future studies of J NK function.
Journal ArticleDOI
MAP Kinases in the Immune Response
TL;DR: Recent progress in understanding the function and regulation of MAP kinase pathways in these phases of immune responses in mammalian species is summarized.
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JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis
Kui Lei,Roger J. Davis +1 more
TL;DR: It is demonstrated that JNK phosphorylates two members of the BH3-only subgroup of Bcl2-related proteins (Bim and Bmf) that are normally sequestered by binding to dynein and myosin V motor complexes, which provide a molecular link between the JNK signal transduction pathway and the Bax/Bak-dependent mitochondrial apoptotic machinery.
Journal ArticleDOI
Targeting JNK for therapeutic benefit: from junk to gold?
TL;DR: The evidence supporting the application of JNK inhibitors in inflammatory, vascular, neurodegenerative, metabolic and oncological diseases in humans is discussed, and the present status of drug discovery targeting JNK is described.
Journal ArticleDOI
The Bax subfamily of Bcl2-related proteins is essential for apoptotic signal transduction by c-Jun NH(2)-terminal kinase.
Kui Lei,Anjaruwee S. Nimnual,Wei-Xing Zong,Norman J. Kennedy,Richard A. Flavell,Craig B. Thompson,Dafna Bar-Sagi,Roger J. Davis +7 more
TL;DR: Activated JNK is sufficient to induce rapid cytochrome c release and apoptosis, however, activated JNK fails to cause death in cells deficient of members of the Bax subfamily of proapoptotic Bcl2-related proteins.
References
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Journal ArticleDOI
Signal transduction by the JNK group of MAP kinases.
TL;DR: This review will focus on the JNK group of MAP kinases, which are characterized by the sequence TEY and the two stress-activatedMAP kinases: p38 with the sequence TGY, and the c-Jun NH2-terminal kinases (JNK) with the sequences TPY.
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JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
Benoit Dérijard,Benoit Dérijard,Masahiko Hibi,I-Huan Wu,I-Huan Wu,Tamera Barrett,Bing Su,Tiliang Deng,Michael Karin,Roger J. Davis,Roger J. Davis +10 more
TL;DR: JNK1 is a component of a novel signal transduction pathway that is activated by oncoproteins and UV irradiation and its properties indicate that JNK1 activation may play an important role in tumor promotion.
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The stress-activated protein kinase subfamily of c-Jun kinases.
John M. Kyriakis,Papia Banerjee,Eleni Nikolakaki,Eleni Nikolakaki,Tianang Dai,Elizabeth A. Rubie,M. F. Ahmad,Joseph Avruch,James R. Woodgett +8 more
TL;DR: The kinase p54s are the principal c-Jun N-terminal kinases activated by cellular stress and tumour necrosis factor (TNF)-α, hence they are designated stress-activated protein kinases, or SAPKs.
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Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.
TL;DR: This work has identified a serine/threonine kinase whose activity is stimulated by the same signals that stimulate the amino-terminal phosphorylation of c-Jun, and suggests a mechanism through which protein kinase cascades can specifically modulate the activity of distinct nuclear targets.