Disease relevance of BATF

• In this study, we identified BATF as a cellular gene that is up-regulated dramatically within 24 h following the infection of established and primary human B cells with EBV [1].
• Northern blot analysis of polyadenylated mRNA isolated from a variety of human tissues and established cell lines indicates that the 1.0 kilobase B-ATF mRNA is expressed differentially, with the strongest hybridization detected in lung and in Raji Burkitt's lymphoma [2].
• A novel cellular gene, SFA-2, was isolated by differential hybridization of a cDNA library, using probes obtained from an adult T-cell leukemia cell line in comparison with normal CD4+ T cells and MOLT-4 cell line [3].

High impact information on BATF

• Intriguingly, the induction of AP-1 activity by LPS in precursor B cells and primary dendritic cells fully depends on the IKK/NF-kappaB pathway, which promotes expression of several AP-1 family members, including JunB, JunD, and B-ATF [4].
• In this study, we show that Tg BATF targets the majority of Valpha14Jalpha281 (Valpha14i(7)) NKT cells, regardless of CD4 expression and Vbeta gene usage [5].
• As a population, BATF-expressing NKT cells are TCRbeta/CD3epsilon(low), but express normal levels of CD69, suggesting a failure to expand appropriately following selection [5].
• Interaction studies in vitro and in vivo show that the leucine zipper of B-ATF mediates dimerization with members of the Jun family of proteins [6].
• Stable expression of B-ATF in C3H10T1/2 cells does not reduce cell viability, but does result in a reduced cellular growth rate when compared to controls [6].

Biological context of BATF

• Given that 40% of mammalian bZIP transcription factors contain a residue analogous to serine-43 of BATF in their DNA binding domains, the phosphorylation event described here represents a mechanism that is potentially applicable to the regulation of many bZIP proteins [7].
• The identification of BATF as a cellular target of EBV provides important new information on how programs of viral and cellular gene expression may be coordinated to promote viral latency and control lytic-cycle entry [1].
• The transactivation of BATF is mediated by EBNA2 in a B-cell-specific manner and is duplicated in non-EBV-infected B cells by the expression of mammalian Notch proteins [1].
• A potential role for BATF in promoting EBV latency is supported by studies in which BATF was shown to negatively impact the expression of a BZLF1 reporter gene and to reduce the frequency of lytic replication in latently infected cells [1].
• A new member of the ATF/CREB family of transcription factors, called B-ATF, has been isolated from a cDNA library prepared from Epstein-Barr virus stimulated human B cells [2].

Anatomical context of BATF

• Frequency-dependent changes in modulus and phase of BATF and RATF were attributable to wave travel and reflection in the upper limb [8].
• SFA-2, a novel bZIP transcription factor induced by human T-cell leukemia virus type I, is highly expressed in mature lymphocytes [3].

Associations of BATF with chemical compounds

• To model phosphorylation of the BATF DNA binding domain, serine-43 was replaced by an aspartate residue [7].
• In the present study, we demonstrate that BATF is phosphorylated in vivo on multiple serine and threonine residues and at least one tyrosine residue [7].
• There was no significant difference in BATF under control conditions and with nitroglycerine; hence results were pooled [8].
• Jun/B-ATF dimers display similar DNA binding profiles as Jun/Fos dimers, with a bias toward binding TRE (12-O-tetradecanolyphorbol-13-acetate-response element) over CRE (cyclic AMP-response element) DNA sites [6].
• The N-terminal region of SFA-2 is rich in serine and contains a consensus sequence for casein kinase II phosphorylation [3].

Physical interactions of BATF

• These data demonstrate that phosphorylation of serine-43 converts BATF from a DNA binding into a non-DNA binding inhibitor of AP-1 activity [7].
• IFP 35 forms complexes with B-ATF, a member of the AP1 family of transcription factors [9].

Regulatory relationships of BATF

• EBNA2 and activated Notch induce expression of BATF [1].

Other interactions of BATF

• Interestingly, BATF(S43D) functions like wild-type BATF to reduce AP-1-mediated gene transcription, despite the observed inability of the BATF(S43D):Jun heterodimer to bind DNA [7].

Analytical, diagnostic and therapeutic context of BATF

• Northern blot analysis reveals that the human B-ATF gene is expressed most highly in hematopoietic tissues [6].

References