排序方式: 共有11条查询结果,搜索用时 31 毫秒
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Neurobiology. trking neurotrophic receptors. 总被引:3,自引:0,他引:3
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The ground state of embryonic stem cell self-renewal 总被引:3,自引:0,他引:3
Ying QL Wray J Nichols J Batlle-Morera L Doble B Woodgett J Cohen P Smith A 《Nature》2008,453(7194):519-523
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Zeng X Tamai K Doble B Li S Huang H Habas R Okamura H Woodgett J He X 《Nature》2005,438(7069):873-877
Signalling by the Wnt family of secreted lipoproteins has essential functions in development and disease. The canonical Wnt/beta-catenin pathway requires a single-span transmembrane receptor, low-density lipoprotein (LDL)-receptor-related protein 6 (LRP6), whose phosphorylation at multiple PPPSP motifs is induced upon stimulation by Wnt and is critical for signal transduction. The kinase responsible for LRP6 phosphorylation has not been identified. Here we provide biochemical and genetic evidence for a 'dual-kinase' mechanism for LRP6 phosphorylation and activation. Glycogen synthase kinase 3 (GSK3), which is known for its inhibitory role in Wnt signalling through the promotion of beta-catenin phosphorylation and degradation, mediates the phosphorylation and activation of LRP6. We show that Wnt induces sequential phosphorylation of LRP6 by GSK3 and casein kinase 1, and this dual phosphorylation promotes the engagement of LRP6 with the scaffolding protein Axin. We show further that a membrane-associated form of GSK3, in contrast with cytosolic GSK3, stimulates Wnt signalling and Xenopus axis duplication. Our results identify two key kinases mediating Wnt co-receptor activation, reveal an unexpected and intricate logic of Wnt/beta-catenin signalling, and illustrate GSK3 as a genuine switch that dictates both on and off states of a pivotal regulatory pathway. 相似文献
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Woodgett J 《Nature》2008,454(7207):939
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The stress-activated protein kinase pathways 总被引:29,自引:0,他引:29
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Phosphorylation of c-jun mediated by MAP kinases 总被引:142,自引:0,他引:142
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Jaworski T Dewachter I Lechat B Gees M Kremer A Demedts D Borghgraef P Devijver H Kügler S Patel S Woodgett JR Van Leuven F 《Nature》2011,480(7376):E4-5; discussion E6
Arising from C. J. Phiel, C. A. Wilson, V. M.-Y. Lee & P. S. Klein 423, 435-439 (2003)A major unresolved issue in Alzheimer's disease is identifying the mechanisms that regulate proteolytic processing of amyloid precursor protein (APP)-glycogen synthase kinase-3 (GSK-3) isozymes are thought to be important in this regulation. Phiel et al. proposed that GSK-3α, but not GSK-3β, controls production of amyloid. We analysed the proteolytic processing of mouse and human APP in mouse brain in vivo in five different genetic and viral models. Our data do not yield evidence for either GSK-3α-mediated or GSK-3β-mediated control of APP processing in brain in vivo. 相似文献
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