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J Biol Chem, Vol. 274, Issue 39, 27981-27988, September 24, 1999
From the Human immunodeficiency virus type 1 (HIV-1) can
establish latent infection following provirus integration into the host
genome. NF-
ERK MAP Kinase Links Cytokine Signals to Activation of Latent
HIV-1 Infection by Stimulating a Cooperative Interaction of AP-1
and NF-
B
§,, and¶
Department of Cancer Immunology and AIDS,
Dana-Farber Cancer Institute, Boston, Massachusetts 02115 and the
Departments of § Pathology and ¶ Neurology, Harvard
Medical School, Boston, Massachusetts 02115
B plays a critical role in activation of HIV-1 gene
expression by cytokines and other stimuli, but the signal transduction
pathways that regulate the switch from latent to productive infection
have not been defined. Here, we show that ERK1/ERK2 mitogen-activated protein kinase (MAPK) plays a central role in linking signals at the
cell surface to activation of HIV-1 gene expression in latently
infected cells. MAPK was activated by cytokines and phorbol 12-myristate 13-acetate in latently infected U1 cells. The induction of
HIV-1 expression by these stimuli was inhibited by PD98059 and U0126,
which are specific inhibitors of MAPK activation. Studies using
constitutively active MEK or Raf kinase mutants demonstrated that MAPK
activates the HIV-1 long terminal repeat (LTR) through the NF-B
sites. Most HIV-1 inducers activated NF-B via a MAPK-independent pathway, indicating that activation of NF-B is not sufficient to
explain the activation of HIV-1 gene expression by MAPK. In contrast,
all of the stimuli activated AP-1 via a MAPK-dependent pathway. NF-B and AP-1 components c-Fos and c-Jun were shown to
physically associate by yeast two-hybrid assays and electrophoretic mobility shift assays. Coexpression of NF-B and c-Fos or c-Jun synergistically transactivated the HIV-1 LTR through the NF-B sites.
These studies suggest that MAPK acts by stimulating AP-1 and a
subsequent physical and functional interaction of AP-1 with NF-B,
resulting in a complex that synergistically transactivates the HIV-1
LTR. These results define a mechanism for signal-dependent activation of HIV-1 replication in latently infected cells and suggest
potential therapeutic strategies for unmasking latent reservoirs of
HIV-1.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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