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14‐3‐3 ζ binds to hepatitis B virus protein X and maintains its protein stability in hepatocellular carcinoma cells

Cancer medicine (Malden, MA), 2018-11, Vol.7 (11), p.5543-5553 [Peer Reviewed Journal]

2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;ISSN: 2045-7634 ;EISSN: 2045-7634 ;DOI: 10.1002/cam4.1512

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  • Title:
    14‐3‐3 ζ binds to hepatitis B virus protein X and maintains its protein stability in hepatocellular carcinoma cells
  • Author: Tang, Yufu ; Zhang, Yibing ; Wang, Chunhui ; Sun, Zhongyi ; Li, Longfei ; Dong, Jiahong ; Zhou, Wenping
  • Subjects: AKT protein ; Amino acids ; Arginine ; Carcinogenesis ; Glycine ; Hepatitis ; Hepatitis B ; Hepatocellular carcinoma ; Invasiveness ; Leucine ; Liver cancer ; Metastases ; Portal vein ; Proline ; Protein X ; Proteins ; Serine ; Signal transduction ; Thrombosis ; Ubiquitination ; Xenografts
  • Is Part Of: Cancer medicine (Malden, MA), 2018-11, Vol.7 (11), p.5543-5553
  • Description: Abstract 14‐3‐3 ζ , a phosphopeptide‐binding molecule, is reportedly overexpressed in the cancerous tissues of patients with hepatocellular carcinoma ( HCC ). Hepatitis B virus ( HBV ) protein X ( HB x) draws intensive attention in HBV ‐related HCC because it not only regulates HBV replication, but also promotes carcinogenesis by interacting with various tumor or antitumor molecules. This study is performed to investigate whether and how 14‐3‐3 ζ interacts with HB x. The coimmunoprecipitation (Co‐ IP ) results showed that 14‐3‐3 ζ bond to HB x in HBV ‐infected Hep3B HCC cells and CSQT ‐2 portal vein tumor thrombosis ( PVTT ) cells. By performing Co‐ IP assay in HBV ‐free Huh7 cells expressing wild‐type HB x, mutant HB x‐S31A, or HB x‐S31D (serine 31 was mutated into alanine 31 or aspartic acid 31 ), we found that the phosphorylated serine 31 with its near amino acid residues constituted a RPL phosphoS 31 GP (R, arginine; P, proline; L, leucine; S, serine; G, glycine) motif in HB x for 14‐3‐3 ζ docking. This 14‐3‐3 ζ ‐ HB x interaction was partly impaired when Akt signaling transduction was blocked by LY 294002. Furthermore, 14‐3‐3 ζ silencing augmented HB x ubiquitination and decreased its expression in cancer cells and xenograft tumor. The migratory and invasive abilities of CSQT ‐2 cells were inhibited upon 14‐3‐3 ζ silencing, whereas partly restored by HB x overexpression. Additionally, 14‐3‐3 ζ positively correlated with HB x to be overexpressed in the primary HCC tissues ( r  = 0.344) and metastatic PVTT ( r  = 0.348). In summary, findings of this study reveal a novel 14‐3‐3 ζ ‐ HB x interaction in HCC cells and suggest 14‐3‐3 ζ as a candidate target for treating HBV ‐related HCC .
  • Publisher: Bognor Regis: John Wiley & Sons, Inc
  • Language: English
  • Identifier: ISSN: 2045-7634
    EISSN: 2045-7634
    DOI: 10.1002/cam4.1512
  • Source: GFMER Free Medical Journals
    PubMed Central
    Wiley Blackwell Open Access Titles
    ROAD: Directory of Open Access Scholarly Resources
    ProQuest Central
    DOAJ Directory of Open Access Journals
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