共查询到20条相似文献,搜索用时 31 毫秒
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Almeida M Han L Bellido T Manolagas SC Kousteni S 《The Journal of biological chemistry》2005,280(50):41342-41351
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Roy SK Shuman JD Platanias LC Shapiro PS Reddy SP Johnson PF Kalvakolanu DV 《The Journal of biological chemistry》2005,280(26):24462-24471
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Wnt signaling controls the phosphorylation status of beta-catenin 总被引:19,自引:0,他引:19
van Noort M Meeldijk J van der Zee R Destree O Clevers H 《The Journal of biological chemistry》2002,277(20):17901-17905
At the heart of the canonical Wnt signaling cascade, adenomatous polyposis coli (APC), axin, and GSK3 constitute the so-called destruction complex, which controls the stability of beta-catenin. It is generally believed that four conserved Ser/Thr residues in the N terminus of beta-catenin are the pivotal targets for the constitutively active serine kinase GSK3. In cells that do not receive Wnt signals, glycogen synthase kinase (GSK) is presumed to phosphorylate beta-catenin, thus marking the latter for proteasomal degradation. Wnt signaling inhibits GSK3 activity. As a consequence, beta-catenin would no longer be phosphorylated and accumulate to form nuclear complexes with TCF/LEF factors. Although mutations in or near the N-terminal Ser/Thr residues stabilize beta-catenin in several types of cancer, the hypothesis that Wnt signaling controls phosphorylation of these residues remains unproven. We have generated a monoclonal antibody that recognizes an epitope containing two of the four residues when both are not phosphorylated. The epitope is generated upon Wnt signaling as well as upon pharmacological inhibition of GSK3 by lithium, providing formal proof for the regulated phosphorylation of the Ser/Thr residues of beta-catenin by Wnt signaling. Immunohistochemical analysis of mouse embryos utilizing the antibody visualizes sites that transduce Wnt signals through the canonical Wnt cascade. 相似文献
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Kim DW Lee JH Park SK Yang WM Jeon GS Lee YH Chung CK Cho SS 《Neurochemical research》2007,32(9):1460-1468
Glycogen synthase kinase 3β (GSK3β) is believed to play important roles in the regulation of synaptic plasticity, cell survival
and circadian rhythms in the mature CNS. However, although several studies have been focused on the GSK3β, little is known
about GSK3β changes in glial cells under neuropathological conditions. In this study, we evaluated the expressions of molecules
associated with the GSK3β signaling pathway, following the induction of an excitotoxic lesion in mouse brain by kainic acid
(KA) injection, which caused pyramidal cell degeneration in the hippocampal CA3 region. In injured hippocampi, Ser47-Akt (protein
kinase B, PKB) phosphorylation increased from 4 h until 1 day post-injection (PI). Ser9-GSK3β and Ser133-cAMP responsive element-binding
protein (CREB) phosphorylations showed similar spatiotemporal patterns in hippocampi at 1 day until 3 days PI. Double immunohistochemistry
also showed that these phosphorylated forms of Akt, GSK3β and CREB were expressed in astrocytes. For the first time, our data
demonstrate the injury-induced astrocytic changes in the levels of phosphorylation of Akt, -GSK3β and -CREB in vivo, which
may reflect mechanisms of glial cells protection or adaptive response to damage.
DW Kim and JH Lee contributed equally to this work. 相似文献
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