All Known In Vivo Functions of the Oct-2 Transcription Factor Require the C-Terminal Protein Domain

Corcoran, Lynn M.; Köentgen, Frank; Dietrich, Wendy; Veale, Margaret F.; Humbert, Patrick O.

doi:10.4049/jimmunol.172.5.2962

Cited by 21 publications

(19 citation statements)

References 59 publications

(66 reference statements)

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“…Nuclear extracts were prepared (Schreiber et al, 1989) and EMSA was performed as previously described (Corcoran et al, 2004). Restriction fragment probes were labeled using [ 32 P]dATP and Klenow DNA polymerase.…”

Section: Methodsmentioning

confidence: 99%

B and T cells collaborate in antiviral responses via IL-6, IL-21, and transcriptional activator and coactivator, Oct2 and OBF-1

Karnowski

Chevrier

Belz

et al. 2012

Journal of Experimental Medicine

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173

198

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Section: Methodsmentioning

confidence: 99%

B and T cells collaborate in antiviral responses via IL-6, IL-21, and transcriptional activator and coactivator, Oct2 and OBF-1

Karnowski

Chevrier

Belz

et al. 2012

Journal of Experimental Medicine

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173

198

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“…An inhibition domain was also identified in the N-terminus of Oct2 (33). The C-terminal domain of Oct2 is required for its in vivo functions (34). Similarly, transactivation domains have also been identified in both the N- and C-termini of Oct4 (35, 36).…”

Section: Structural Characteristics Of Oct Proteinsmentioning

confidence: 99%

Octamer-binding transcription factors: genomics and functions

Zhao¹

2013

Front Biosci

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The Octamer-binding proteins (Oct) are a group of highly conserved transcription factors that specifically bind to the octamer motif (ATGCAAAT) and closely related sequences that are found in promoters and enhancers of a wide variety of both ubiquitously expressed and cell type-specific genes. Oct factors belong to the larger family of POU domain factors that are characterized by the presence of a highly conserved bipartite DNA binding domain, consisting of an amino-terminal specific subdomain (POUS) and a carboxyl-terminal homeo-subdomain (POUH). Eleven Oct proteins have been named (Oct1-11), and currently, eight genes encoding Oct proteins (Oct1, Oct2, Oct3/4, Oct6, Oct7, Oct8, Oct9, and Oct11) have been cloned and characterized. Oct1 and Oct2 are widely expressed in adult tissues, while other Oct proteins are much more restricted in their expression patterns. Oct proteins are implicated in crucial and versatile biological events, such as embryogenesis, neurogenesis, immunity, and body glucose and amino acid metabolism. The aberrant expression and null function of Oct proteins have also been linked to various diseases, including deafness, diabetes and cancer. In this review, I will report both the genomic structure and major functions of individual Oct proteins in physiological and pathological processes.

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“…These will not be discussed here. The Oct2 gene is large, displays complex splicing patterns, and encodes protein isoforms with multiple essential activation domains (20–22). Oct2 is largely localized to the nucleus.…”

Section: Introductionmentioning

confidence: 99%

Oct2 and Obf1 as Facilitators of B:T Cell Collaboration during a Humoral Immune Response

et al. 2014

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The Oct2 protein, encoded by the Pou2f2 gene, was originally predicted to act as a DNA binding transcriptional activator of immunoglobulin (Ig) in B lineage cells. This prediction flowed from the earlier observation that an 8-bp sequence, the “octamer motif,” was a highly conserved component of most Ig gene promoters and enhancers, and evidence from over-expression and reporter assays confirmed Oct2-mediated, octamer-dependent gene expression. Complexity was added to the story when Oct1, an independently encoded protein, ubiquitously expressed from the Pou2f1 gene, was characterized and found to bind to the octamer motif with almost identical specificity, and later, when the co-activator Obf1 (OCA-B, Bob.1), encoded by the Pou2af1 gene, was cloned. Obf1 joins Oct2 (and Oct1) on the DNA of a subset of octamer motifs to enhance their transactivation strength. While these proteins variously carried the mantle of determinants of Ig gene expression in B cells for many years, such a role has not been borne out for them by characterization of mice lacking functional copies of the genes, either as single or as compound mutants. Instead, we and others have shown that Oct2 and Obf1 are required for B cells to mature fully in vivo, for B cells to respond to the T cell cytokines IL5 and IL4, and for B cells to produce IL6 normally during a T cell dependent immune response. We show here that Oct2 affects Syk gene expression, thus influencing B cell receptor signaling, and that Oct2 loss blocks Slamf1 expression in vivo as a result of incomplete B cell maturation. Upon IL4 signaling, Stat6 up-regulates Obf1, indirectly via Xbp1, to enable plasma cell differentiation. Thus, Oct2 and Obf1 enable B cells to respond normally to antigen receptor signals, to express surface receptors that mediate physical interaction with T cells, or to produce and respond to cytokines that are critical drivers of B cell and T cell differentiation during a humoral immune response.

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All Known In Vivo Functions of the Oct-2 Transcription Factor Require the C-Terminal Protein Domain

Cited by 21 publications

References 59 publications

B and T cells collaborate in antiviral responses via IL-6, IL-21, and transcriptional activator and coactivator, Oct2 and OBF-1

B and T cells collaborate in antiviral responses via IL-6, IL-21, and transcriptional activator and coactivator, Oct2 and OBF-1

Octamer-binding transcription factors: genomics and functions

Oct2 and Obf1 as Facilitators of B:T Cell Collaboration during a Humoral Immune Response

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