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Primary Study of CREB4 Translocation Mechanism from Cytoplasm to Nucleus

Author: LiuYongQiang
Tutor: NiXiaoHua
School: East China Normal University
Course: Biochemistry and Molecular Biology
Keywords: CREB4 Yeast two-hybrid system Fluorescence colocalization
CLC: Q343
Type: Master's thesis
Year: 2006
Downloads: 27
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Abstract

Signal transduction pathway focused on cell regulation at the transcriptional level, through transcriptional activation of the expression of specific genes against environmental stimuli factor. The activation of specific transcription factor binding and gene regulatory region or the co-expression of these signaling pathways can regulate transcription initiation. The study of the structure and function of these transcription factors to investigate the transcriptional activation mechanism provides a new point of view. cAMP response element binding protein (cAMP response element-binding proteins, CREB) is a mammalian transcription factor family, cAMP response element cAMP-response element (CRE)-mediated cAMP and calcium-dependent gene expression involved in cell proliferation and differentiation embryonic development, learning a variety of physiological processes such as memory and tumorigenesis. The abnormal expression of these proteins, causing tissue is not normal development and apoptosis of the abnormal cells, or even cause the individual death. . CREB4 is a new member of the human CREB family, human Tumor MTC panel results show, CREB4 in the human lung cancer LX-1 Colonic Adenocarcinoma CX-1, prostate cancer PC-3, colon G1-112 and pancreatic G1-103 expression, GI-101 in breast cancer, ovarian cancer tissue GI-102 and the lung cancer tissue GI-117 was not detected to a specific band. The prompt CREB4 play a role in the regulation of gene expression in a variety of tumor tissue. The full length CREB4 protein localized in the cytoplasm, while missing the C-terminal assumes the transmembrane domain CREB4 ^{1-279 mutants transferred to the nucleus, suggesting CREB4 the C-terminal transmembrane domain its from the cytoplasm related to the transfer of the nucleus. Construction, expression the CREB4 ^{215-279 -LexA and CREB ^{, 215-395 a-LexA The pLexA to plasmids were transformed into yeast EGY48 containing p8opLacZ report plasmid strains, yeast two-hybrid screening human fetal brain cDNA library found with CREB4 ^{215-279 interacting protein kayopherin α2 and nuclear pore complex-associated protein TPR. TPR related proteins of the nuclear pore complex. karyopherin α2 Karyopherin α2β1 involved in receptor-mediated pathways for macromolecules the protein transporter from the cytoplasm to the nucleus, suggesting that karyopherin α2 may be involved in CREB4 the transmembrane transport process. The CREB4, CREB4 ^{1-279 , karyopherin α2 three proteins were constructed AD293 cells were transfected with the eukaryotic expression vector pEGFP-C1 and pDsRed-N1, fluorescence colocalization further, CREB4 and karyopherin α2 co-localized in the cytoplasm, CREB4 ^{1-279 and karyopherin α2 co-localization in the nucleus. CREB4 and CREB4 ^{1-279 changed karyopherin α2 positioning in the cell. The combined results suggest CREB4 karyopherin α2, cut off the C-terminal only after transfer of nuclear transcription.}}}}}}}

Primary Study of CREB4 Translocation Mechanism from Cytoplasm to Nucleus

Abstract

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