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10.1080/15384101.2017.1325039

http://scihub22266oqcxt.onion/10.1080/15384101.2017.1325039
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C5602426!5602426!28816574
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suck abstract from ncbi


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pmid28816574      Cell+Cycle 2017 ; 16 (18): 1683-94
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  • SGT1-HSP90 complex is required for CENP-A deposition at centromeres #MMPMID28816574
  • Niikura Y; Kitagawa R; Ogi H; Kitagawa K
  • Cell Cycle 2017[]; 16 (18): 1683-94 PMID28816574show ga
  • The centromere plays an essential role in accurate chromosome segregation, and defects in its function lead to aneuploidy and thus cancer. The centromere-specific histone H3 variant CENP-A is proposed to be the epigenetic mark of the centromere, as active centromeres require CENP-A?containing nucleosomes to direct the recruitment of multiple kinetochore proteins. CENP-A K124 ubiquitylation, mediated by CUL4A-RBX1-COPS8 E3 ligase activity, is required for CENP-A deposition at the centromere. However, the mechanism that controls the E3 ligase activity of the CUL4A-RBX1-COPS8 complex remains obscure. We have discovered that the SGT1-HSP90 complex is required for recognition of CENP-A by COPS8. Thus, the SGT1-HSP90 complex contributes to the E3 ligase activity of the CUL4A complex that is necessary for CENP-A ubiquitylation and CENP-A deposition at the centromere.
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