Abstract
Basic leucine zipper (bZIP) transcription factors (TFs) govern diverse cellular processes and cell fate decisions. The hallmark of the leucine zipper domain is the heptad repeat, with leucine residues at every seventh position in the domain. These leucine residues enable homo- and heterodimerization between ZIP domain α-helices, generating coiled-coil structures that stabilize interactions between adjacent DNA-binding domains and target DNA substrates. Several cancer-causing viruses encode viral bZIP TFs, including human T-cell leukemia virus (HTLV), hepatitis C virus (HCV) and the herpesviruses Marek’s disease virus (MDV), Epstein–Barr virus (EBV) and Kaposi’s sarcoma-associated herpesvirus (KSHV). Here, we provide a comprehensive review of these viral bZIP TFs and their impact on viral replication, host cell responses and cell fate.
Highlights
Basic leucine zipper transcription factors (TFs) govern diverse cellular processes and cell fate decisions
Because K-Basic leucine zipper (bZIP) is a viral E3 small ubiquitin-like modifier (SUMO) ligase that displays SUMO2/3 specificity, and because SUMO2/3 are the preferred substrates for K-replication and transcription activator (Rta)-mediated ubiquitination and subsequent proteasomal degradation, KSHV basic leucine zipper (K-bZIP) and K-Rta may work in concert to regulate cellular protein levels during lytic replication to create an optimal environment for Kaposi’s sarcoma-associated herpesvirus (KSHV) replication
HTLV-1 bZIP factor (HBZ) heterodimerizes with CREB1 to repress the transcriptional activation of the cell cycle-regulating cyclin D1 in 293T cells at a cAMP response elements (CREs) site located in the cyclin D1 promoter
Summary
TFs residues stabilize dimer formation [6]). A well-studied example of a heterodimeric bZIP TF complex is the activator-protein 1 (AP-1). AP-1 Complexes complex, which comprises members of the Jun, Fos, ATF, and Maf families of bZIP proteins [1]. AP-1 activity is regulated post-translationally by phosphorylation and to serine and threonine residues by O-linked glycosylation [14]. Together, these foundational [13]. C/EBPα/c-Jun and C/EBPα/c-Fos heterodimers potently drive monocyte differentiation in mouse bone marrow mononuclear cells compared to weaker C/EBPα homodimers and c-Jun/c-Fos heterodimers [27] Together, these studies of C/EBP complexes have reinforced the idea that heterodimer formation diversifies the transcriptional output of bZIP TFs
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