TY - JOUR
T1 - ATP1B3 protein modulates the restriction of HIV-1 production and nuclear factor K light chain enhancer of activated B cells (NF-κB) activation by BST-2
AU - Nishitsuji, Hironori
AU - Sugiyama, Ryuichi
AU - Abe, Makoto
AU - Takaku, Hiroshi
N1 - Funding Information:
This work was supported in part by a grant-in-aid for science research (C) from the Japan Society for the Promotion of Science (JSPS), Japan; by a grant-in-aid for AIDS research from the Ministry of Health, Labor, and Welfare of Japan; and by a grant from the Strategic Research Foundation grant-aided project for Private Universities from the Ministry of Education, Culture, Sport, Science, and Technology of Japan (MEXT). The authors declare that they have no conflicts of interest with the contents of this article.
PY - 2016/2/26
Y1 - 2016/2/26
N2 - Here, we identify ATP1B3 and fibrillin-1 as novel BST-2-binding proteins. ATP1B3 depletion in HeLa cells (BST-2-positive cells), but not 293T cells (BST-2-negative cells), induced the restriction of HIV-1 production in a BST-2-dependent manner. In contrast, fibrillin-1 knockdown reduced HIV-1 production in 293T and HeLa cells in a BST-2-independent manner. Moreover, NF-κB activation was enhanced by siATP1B3 treatment in HIV-1- and HIV-1ΔVpu-infected HeLa cells. In addition, ATP1B3 silencing induced high level BST-2 expression on the surface of HeLa cells. These results indicate that ATP1B3 is a co-factor that accelerates BST-2 degradation and reduces BST-2-mediated restriction of HIV-1 production and NF-κB activation.
AB - Here, we identify ATP1B3 and fibrillin-1 as novel BST-2-binding proteins. ATP1B3 depletion in HeLa cells (BST-2-positive cells), but not 293T cells (BST-2-negative cells), induced the restriction of HIV-1 production in a BST-2-dependent manner. In contrast, fibrillin-1 knockdown reduced HIV-1 production in 293T and HeLa cells in a BST-2-independent manner. Moreover, NF-κB activation was enhanced by siATP1B3 treatment in HIV-1- and HIV-1ΔVpu-infected HeLa cells. In addition, ATP1B3 silencing induced high level BST-2 expression on the surface of HeLa cells. These results indicate that ATP1B3 is a co-factor that accelerates BST-2 degradation and reduces BST-2-mediated restriction of HIV-1 production and NF-κB activation.
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U2 - 10.1074/jbc.M115.679357
DO - 10.1074/jbc.M115.679357
M3 - Article
C2 - 26694617
AN - SCOPUS:84964588281
VL - 291
SP - 4754
EP - 4762
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 9
ER -