期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 280, 期 21, 页码 20549-20557出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M409563200
关键词
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资金
- NCI NIH HHS [CA100070, R01 CA100070] Funding Source: Medline
- NIAMS NIH HHS [AR44387, AR49222] Funding Source: Medline
- NIA NIH HHS [AG20752] Funding Source: Medline
- NIGMS NIH HHS [GM55188] Funding Source: Medline
Expression of a dominant negative 20-kDa isoform of CCAAT/enhancer-binding protein (C/EBP beta), LIP, is increased in proliferating livers and in tumor cells. Two RNA-binding proteins, CUGBP1 and calreticulin, have been implicated in the translational regulation of C/EBP beta. In this paper, we present evidence showing several critical steps by which liver increases translation of LIP after partial hepatectomy. At early stages after partial hepatectomy, liver activates CUGBP1 by a hyperphosphorylation. The activated CUGBP1 binds to the 5' region of C/EBP beta mRNA and replaces calreticulin, which partially represses translation of C/EBP beta in quiescent livers. The hyperphosphorylated CUGBP1 also interacts with the alpha and beta subunits of initiation factor eIF2. Our data demonstrate that the interaction of CUGBP1 with the eIF2 alpha enhances the association of CUGBP1 with ribosomes and correlates with increased translation of LIP in the liver after partial hepatectomy. Our data support the hypothesis that CUGBP1 increases translation of LIP by the interaction with the eIF2 alpha subunit. This facilitates subsequent recruitment of larger numbers of ribosomes to initiate translation of LIP.
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