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Results suggest a critical role for lck kinase (Lck) as a mediator for programmed death protein 1 (PD-1) induced inhibition of t cell receptor (TCR) signaling network.
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The results suggest that CD45RO modulates HIV-1 gp120-induced apoptosis by regulating the activity of Lymphocyte Specific Protein Tyrosine Kinase p56(lck) (Lck).
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Intrinsic properties and plasma membrane trafficking route of lck SH4 domains sensitive to retargeting by HIV-1 Nef.
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The ionic CD3-epsilon -Lck interaction controls the phosphorylation level of the T-cell receptor.
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a previously unappreciated role for PLC-gamma1 in the positive regulation of Zap-70 and T-cell receptor tyrosine phosphorylation. Conversely, PLC-gamma1 negatively regulated the phosphorylation of SLP-76-associated proteins, including previously established Lck substrate phosphorylation sites within this complex.
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autophosphorylation of the LCK active-site loop is indispensable for its catalytic activity and LCK can stimulate its own activation by adopting a more open conformation, which can be modulated by point mutations, and CD4 and CD8, T-cell coreceptors, can enhance LCK activity
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the central biological role of the novel IL-2-R/Lck/PLCgamma/PKCtheta;/alphaPIX/Rac1/PYGM signalling pathway is directly related to the control of fundamental cellular processes such as T cell migration and proliferation.
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Possible models of regulation of Lck by Aurora-A during T cell activation are described in the review.
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Mutation of the basic clusters in the CD28 cytoplasmic domain reduced the recruitment to the CD28-Lck complex of protein kinase Ctheta; (PKCtheta;), which serves as a key effector kinase in the CD28 signaling pathway.
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Data suggest that T cell activation through the TCR complex is accompanied by the de novo activation of T-lymphocyte specific protein tyrosine kinase p56lck (Lck) and that phosphorylation of Tyr(394) plays a role in Lck function that goes beyond inducing an open conformation of the kinase.
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WASH has a pivotal role for regulation of NK cell cytotoxicity through Lck-mediated Y141 tyrosine phosphorylation.
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A phosphosite within the SH2 Domain of Lck regulates its activation by CD45. A negative feedback loop that responds to signaling events tunes active Lck amounts and TCR sensitivity.
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The results have revealed a novel splicing homozygous mutation of LCK that may be responsible for the clinical phenotype of HPV infection from latency to invasive carcinoma.
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this study show that Lck as a major signaling hub of CD147 in T cells
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data indicate that HSP65 suppresses cholesterol efflux and increases cellular cholesterol content through an Lck-mediated pathway in T cells
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LSKlow cells, which are derived from LSK cells in p18(-/-) mice, possess lymphoid differentiation ability and short-term repopulation capability.
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These results suggest that PM lipids, including phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate, modulate interaction of Lck with its binding partners in the TCR signaling complex and its TCR signaling activities in a spatiotemporally specific manner via its SH2 domain.
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this study shows that p56(lck), which is essential for activation of T cells through the T-cell receptor, is also critical for signal transduction through Toll-like receptors in T cells
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Aurora A inhibition causes delocalized clustering of Lck at the immunological synapses and decreases its phosphorylation levels thus indicating Aurora A is required for maintaining Lck active during T-cell activation.
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Results demonstrate that Lck represses oxidative phosphorylation through competitive binding with mitochondrial CRIF1 in a kinase-independent manner.
