IndraLab

Statements


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"Jab1 overexpression may induce p27 downregulation."

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"RT-PCR method was adopted to examine the mRNA expression of the Jab1 and p27kip1 gene in Hep-2 cells which was treated with Jab1 siRNA II."

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"Knockdown of Jab1 resulted in a remarkable increase in p27 levels and inhibition of cell proliferation, indicating that Jab1 targets p27 for degradation, thereby controlling its stability."

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"Interestingly, JAB1 mediated p27 degradation was not impaired when S-phase kinase interacting protein 2 (Skp2), an F-box protein required for the ubiquitination and consequent degradation of p27, was silenced."

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"By inhibiting Jun activation domain binding protein 1 (Jab1) trastuzumab increases nuclear retention of p27Kip1."

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"To fill this critical gap, we performed the present study to test the hypothesis that increased CSN5-mediated nuclear exclusion of p27 contributes to the promotion of VSMC proliferation in injured vessels by CSN8 hypomorphism (Figure 1)."

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"This is Jab1 and p27 kip1 interact with each other, Jab1 accelerate p27 kip1 from nuclear to cytoplasm through ubiquitin and proteasome pathway."

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"The fifth component of the COP9 signalosome complex, Jab1 and CSN5, directly binds to and induces specific down-regulation of the cyclin dependent kinase inhibitor p27 (p27 (Kip1))."

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"Although the functional relevance of these mini-complexes remain elusive, XREF_BIBR have revealed that a CSN5 containing mini-complex mediated p27 kip down-regulation in leukemia cells independently of the deneddylation activity of the CSN, suggesting that the mini-complexes may have unique cellular functions."

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"Jab1 and COPS5 can implement its biological function by insulating its target proteins, and the most iconic and persuasive example is that Jab1 and COPS5 triggers p27 protein translocating from cell nucleus to cytoplasm and subsequently prompts p27 degradation."

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"A Jab1 and CSN5 truncation mutant lacking NES reversed p27 down-regulation induced by the full-length Jab1 and CSN5, indicating that this mutant functions as a dominant negative (DN-Jab1)."

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"Introduction of DN-Jab1 into proliferating fibroblasts increased the level of p27 protein, thereby inducing growth arrest of the cells."

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"Gfer inhibits Jab1 mediated degradation of p27 kip1 to restrict proliferation of hematopoietic stem cells."

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"Our data indicating a direct interaction of Gfer with Jab1 to restrict Jab1 mediated destabilization of p27 kip1 (XREF_FIG) underscores the importance of a Gfer-Jab1-p27 kip1 pathway not only in the functional maintenance of normal HSCs, but also in the prevention and/or treatment of malignancies."

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"Additionally, Jab1/CSN5 has a direct interaction with p27, controlling cell proliferation through the inhibition of cyclin E-Cdk2, and mediates the shuttling of p27 between the nucleus and cytoplasm, inducing its degradation [11]."

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"Jab1 overexpression may induce p27 downregulation by nuclear export."

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"Jab1, which enables p27 to be exported from the nucleus and would thus enhance its cytoplasmic degradation, was not obviously over-expressed in adenomas sufficient to account for diminished nuclear p2[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Downregulation of p27 mediated by Jab1 overexpression was inhibited in cells that had been treated with proteasome inhibitors (LLnL, MG132 and LLM) but not in those treated with DMSO (XREF_FIG), indicating that Jab1 promotes p27 degradation through proteolysis and is sensitive to proteasome inhibitors."

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"XREF_BIBR CAPER typically interacts with ESR1 and ESR2 to work as a coactivator of transcription, while JAB1 stimulates the breakdown of the cyclin dependent kinase inhibitor p27Kip1 and regulates HIF by cleaving ubiquitin like proteins."

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"Ectopic expression of Jab1 and CSN5 induces specific down-regulation of the cyclin dependent kinase (Cdk) inhibitor p27 (p27 (Kip1)) in a manner dependent upon transportation from the nucleus to the cytoplasm."

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"Previous studies demonstrated that JAB1 overexpressed in fibroblasts caused translocation of p27 from the nucleus to the cytoplasm accompanied by a reduction in p27 levels."

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"In normal cells, overexpression of JAB1 promotes translocation of p27 from the nucleus and, subsequently reduced levels of p27 due to accelerated degradation [5] ."

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"The possible oxidation and inactivation of Trx through tamoxifen treatment can lead to an increase in p27 removal from the nucleus by Jab1."

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"Depletion of Jab1 by siRNA increases accumulation of p27 and induces cell-cycle arrest and inhibits cell proliferation in NPC cell lines."

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"These data suggest that downregulation of Jab1 induces stabilization of p27, therefore increasing p27 levels and activity."

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"Tomoda K, Kubota Y, Arata Y, Mori S, Maeda M, Tanaka T, Yoshida M, Yoneda-Kato N, Kato JY : The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1 and CSN5 and the COP9 signalosome complex."