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An internal segment (residues 58–119) of the hepatitis B virus X protein is sufficient to activate MAP kinase pathways in mouse liver
Author(s) -
Nijhara Ruchika,
Jana Siddhartha S.,
Goswami Shyamal K.,
Kumar Vijay,
Sarkar Debi P.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02773-9
Subject(s) - hbx , transactivation , signal transduction , biology , kinase , protein kinase a , amino acid , hepatitis b virus , mapk/erk pathway , microbiology and biotechnology , cytoplasm , biochemistry , chemistry , virus , transcription factor , gene , virology
The human hepatitis B virus X protein (HBx) is known as a dual‐specificity transactivator stimulating the transcriptional machinery in the nucleus and signal transduction pathways in the cytoplasm. HBx‐induced activation of mitogen‐activated protein kinase (MAPK) signaling cascades is considered to play an important role in hepatitis B virus‐mediated hepatocarcinogenesis. Herein, we have identified the regions of HBx that are crucial for activating such signaling cascades in vivo. A truncated mutant incorporating regions C–E (amino acids 58–140) was as effective as the full‐length HBx in activating MAPKs and enhancing activator protein‐1 binding activity. While deletion of region C (amino acids 58–84) or D (amino acids 85–119) led to a drastic loss of function, region E (amino acids 120–140) was dispensable for the activation of signaling cascades. Overall, these findings provide the first evidence for the requirement of domain 58–119 of HBx in transmitting mitogenic signals to the nucleus in vivo.