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10.1242/jcs.139592

http://scihub22266oqcxt.onion/10.1242/jcs.139592
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C4038942!4038942!24659803
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suck abstract from ncbi


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pmid24659803      J+Cell+Sci 2014 ; 127 (11): 2448-59
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  • Regulation of Cop9 signalosome activity by the EF-hand Ca2+-binding protein tescalcin #MMPMID24659803
  • Levay K; Slepak VZ
  • J Cell Sci 2014[Jun]; 127 (11): 2448-59 PMID24659803show ga
  • The Ca2+-binding protein tescalcin is known to be involved in hematopoietic cell differentiation; however, this mechanism is poorly understood. Here, we identify CSN4 (subunit 4 of the COP9 signalosome) as a novel binding partner of tescalcin. The COP9 signalosome (CSN) is a multiprotein complex that is essential for development in all eukaryotes. This interaction is selective, Ca2+-dependent and involves the PCI domain of CSN4 subunit. We then investigated tescalcin and CSN activity in human erythroleukemia HEL and promyelocytic leukemia K562 cells and find that phorbol 12-myristate 13-acetate (PMA)-induced differentiation, resulting in the upregulation of tescalcin, coincides with reduced deneddylation of cullin-1 (Cul1) and stabilization of p27Kip1 ? molecular events that are associated with CSN activity. The knockdown of tescalcin led to an increase in Cul1 deneddylation, expression of F-box protein Skp2 and the transcription factor c-Jun, whereas the levels of cell cycle regulators p27Kip1 and p53 decreased. These effects are consistent with the hypothesis that tescalcin might play a role as a negative regulator of CSN activity towards Cul1 in the process of induced cell differentiation.
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