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Pyk2 has a role in spine structure and synaptic function; its deficit contributes to Huntington's disease cognitive impairments
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the non-receptor protein tyrosine kinase 2 beta (PTK2B) plays a critical role in murine beige adipocyte differentiation.
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Data provide evidence that activated PYK2 may function as a component of the microtubule organizing center to regulate spindle assembly during the meiotic process of mouse oocytes.
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MMP-9 activation by hypoxia requires LRP1 and Pyk2 phosphorylation in fibroblasts.
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results suggest that although Pyk2 and FAK are involved in inflammasome activation, only Pyk2 directly phosphorylates ASC and brings ASC into an oligomerization-competent state by allowing Tyr146 phosphorylation to participate ASC speck formation and subsequent NLRP3 inflammation.
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Osteoprotegerin may induce podosome reassembly and peripheral adhesive structure detachment by modulating phosphorylation of Pyk2 and Src and their intracellular distribution in osteoclasts.
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These results suggest that mechanical stimuli activate P2X7 might induce ECMPs expression through PYK2 except in the case of OPN expression. Altogether, mechanical stimuli-induced ECMPs production might be implicated by extracellular ATP secretion or integrin via PYK2 activation.
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Lineage-tracing of monocyte populations suggests that Pyk2 promotes apoptosis in BM monocytes, thereby acting as an important homeostatic regulator of turnover in these short-lived, innate immune cells.
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Pyk2 selectively contributes to the coordination of phagocytosis-promoting signals downstream of CR3, but is dispensable for FcgammaR-mediated phagocytosis
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the findings suggest a model in which the oocyte is not a passive participant in fertilization, but instead responds to sperm contact by localized PYK2 signaling that promotes actin remodeling events required to physically incorporate the sperm head into the ooplasm.
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results show that Pyk2 contributes to cytotoxic T lymphocyte(CTL) migration by regulating detachment of CTL at the trailing edge, which could explain why Pyk2 is important for chemotactic and migratory responses.
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Defects in Pyk2 suppress Kawasaki Disease-like experimental vasculitis, presumably through CXCL9- and CXCL10-dependent interference with neo-angiogenesis. Since Pyk2-KO mice show no life-threatening phenotype, Pyk2 may be a promising therapeutic molecular target for KD.
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STIM1-induced Ca(2+) signaling activates Pyk2 to inhibit the interaction of VE-PTP and VE-cadherin and hence increase endothelial permeability.
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At fertilization, Pyk2 and p-Pyk2 were detected predominantly in sperm heads and the oocyte cytoplasm. Upon formation of male and female pronuclei, Pyk2 and its activated form accumulate in the two pronuclei. Pyk2 was in blastomere nuclei and the pre-blastula cytoplasm. Pyk2 and its activated form then localized to the perinuclear regions, where blastula cells come into contact with each other.
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Findings indicate the presence of unique and overlapping Pyk2 signaling pathways in osteoblasts, which may be controlled by regulating the phosphorylation, kinase activity, and scaffolding functions of Pyk2.
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Astrocytes from Pyk2-/- mice displayed a slower wound covering as compared with wild-type littermate mice after a mechanical stab lesion, data confirmed in purified astrocytes in vitro; actin polymerization dynamics was altered in Pyk2-/- astrocytes; gelsolin, an actin-capping protein able to interact with Pyk2, was mislocalized in Pyk2-/- migrating astrocytes compared with Pyk2+/+ astrocytes
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Phosphoproteomic analysis identifies FAK2 as a potential therapeutic target for tamoxifen resistance in breast cancer.
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Src has a role in priming Pyk2 (but not FAK) phosphorylation and subsequent activation downstream of integrins
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Resistance to hypoxia-induced PH was markedly higher in Pyk2-deficient mice than in wild-type mice. Pyk2-dependent generation of ROS is necessary for the activation of HIF-1alpha.
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These results suggest that phloretin was an inhibitor of actin podosomes and sealing zone, disrupting alpha5beta3 integrin-c-Src-Pyk2/Syk signaling pathway for the regulation of actin cytoskeletal organization in osteoclasts.
