A family of C/EBP-related proteins capable of forming covalently linked leucine zipper dimers in vitro.

Williams, Simon C.; Cantwell, Carrie A.; Johnson, Peter F.

doi:10.1101/gad.5.9.1553

Cited by 565 publications

(458 citation statements)

References 60 publications

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“…(VP16)GBF-F was slightly more active than (C/EBP␤)GBF-F in this assay, probably due to the fact that the VP16 activation domain is more potent than that of C/EBP␤. The decrease in transactivation potential at high C/EBP␤ activation domain concentration has been observed previously (35). The activation of novel cis-elements by GBF-F in concert with C/EBP␤ suggests the possible use of this molecule in regulating genes containing this chimeric site.…”

Section: Gbf-f In Conjunction With C/ebp Activate a Chimeric Site Crementioning

confidence: 48%

“…Eukaryotic Activator Protein Expression Plasmids: Murine Sarcoma Virus Promoter-The eukaryotic expression plasmids for the three C/EBP family members, pMEX C/EBP␣, pMEX C/EBP␤, and pMEX C/EBP␦, are driven by the murine sarcoma virus promoter and have been described elsewhere (35). In order to monitor the presence of C/EBP␣ in transfected cells, we introduced either the flag (DYKDDDK) or the hemagglutinin (YPYDVPDYA) epitope at the NH 2 terminus of C/EBP␣ by inserting oligonucleotides into the non-unique NcoI site of pMEX C/EBP␣.…”

Section: Methodsmentioning

confidence: 99%

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Design of a C/EBP-specific, Dominant-negative bZIP Protein with Both Inhibitory and Gain-of-function Properties

Olive

Williams

Dezan

et al. 1996

Journal of Biological Chemistry

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We have developed a bZIP protein, GBF-F, with both dominant-negative (DN) and gain-of-function properties. GBF-F is a chimera consisting of two components: the DNA binding (basic) region from the plant bZIP protein GBF-1 (GBF) and a leucine zipper (F) designed to preferentially heterodimerize with the C/EBP␣ leucine zipper. Biochemical studies show that GBF-F preferentially forms heterodimers with C/EBP␣ and thus binds a chimeric DNA sequence composed of the half-sites recognized by the C/EBP and GBF basic regions. Transient transfections in HepG2 hepatoma cells show that both components of GBF-F are necessary for inhibition of C/EBP␣ transactivation. When the C/EBP␣ leucine zipper is replaced with that of either GCN4 or VBP, the resulting protein can transactivate a C/EBP cis-element but is not inhibited by GBF-F, indicating that the specificity of dominant-negative action is determined by the leucine zipper. All known members of the C/EBP family contain similar leucine zipper regions and are inhibited by GBF-F. GBF-F also exhibits gain-of-function properties, since, with the essential cooperation of a C/EBP family member, it can transactivate a promoter containing the chimeric C/EBPͦGBF site. This protein therefore has potential utility both as a dominant-negative inhibitor of C/EBP function and as an activator protein with novel DNA sequence specificity.

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Section: Gbf-f In Conjunction With C/ebp Activate a Chimeric Site Crementioning

confidence: 48%

Section: Methodsmentioning

confidence: 99%

Design of a C/EBP-specific, Dominant-negative bZIP Protein with Both Inhibitory and Gain-of-function Properties

Olive

Williams

Dezan

et al. 1996

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Another family of bZip transcription factors is that of Fos-and Jun-related oncoproteins, that modulate cell division and phorbol esther/protein kinase-Cdependent transcription by binding to the CRE-related AP-1 binding site ( 7 ) . The third family of bZip proteins is that of CAAT-box/enhancer binding proteins (C/EBP) ( 8,9), that bind to CAAT-box and related enhancer motifs and regulate the expression of many genes in terminally differentiated cells or in response to cytokines. These families are defined by virtue of similarities in the structures of their bZip domains, their capability to associate as homodimers, or heterodimers with other members of the same family, and their selective binding to specific DNA sequences (Table 1 ).…”

Section: Cre-binding Proteins Share a Common Structurementioning

confidence: 99%

Transcriptional Control of Gene Expression by cAMP‐Response Element Binding Proteins

Vallejo

1994

J Neuroendocrinology

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“…Members of the C/EBP family (C/EBP␣, C/EBP␤, Ig/EBP, C/EBP␦, and C/EBPε) recognize a common DNA-binding sequence and display similar dimerization specificities (4,9,24). Although tissue expression patterns of these members often overlap, recent studies using gene knockout analysis of C/EBPs in mice revealed that C/EBPs differ significantly in their physiological functions and in their downstream target genes.…”

mentioning

confidence: 99%

C/EBPβ, When Expressed from the C/ebpα Gene Locus, Can Functionally Replace C/EBPα in Liver but Not in Adipose Tissue

Chen

Johnson

et al. 2000

Molecular and Cellular Biology

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Knockout of C/EBP␣ causes a severe loss of liver function and, subsequently, neonatal lethality in mice. By using a gene replacement approach, we generated a new C/EBP␣-null mouse strain in which C/EBP␤, in addition to its own expression, substituted for C/EBP␣ expression in tissues. The homozygous mutant mice C/ebp␣ ␤/␤ are viable and fertile and show none of the overt liver abnormalities found in the previous C/EBP␣-null mouse line. Levels of hepatic PEPCK mRNA are not different between C/ebp␣ ␤/␤ and wild-type mice. However, despite their normal growth rate, C/ebp␣ ␤/␤ mice have markedly reduced fat storage in their white adipose tissue (WAT). Expression of two adipocyte-specific factors, adipsin and leptin, is significantly reduced in the WAT of C/ebp␣ ␤/␤ mice. In addition, expression of the non-adipocyte-specific genes for transferrin and cysteine dioxygenase is reduced in WAT but not in liver. Our study demonstrates that when expressed from the C/ebp␣ gene locus, C/EBP␤ can act for C/EBP␣ to maintain liver functions during development. Moreover, our studies with the C/ebp␣ ␤/␤ mice provide new insights into the nonredundant functions of C/EBP␣ and C/EBP␤ on gene regulation in WAT.

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A family of C/EBP-related proteins capable of forming covalently linked leucine zipper dimers in vitro.

Cited by 565 publications

References 60 publications

Design of a C/EBP-specific, Dominant-negative bZIP Protein with Both Inhibitory and Gain-of-function Properties

Design of a C/EBP-specific, Dominant-negative bZIP Protein with Both Inhibitory and Gain-of-function Properties

Transcriptional Control of Gene Expression by cAMP‐Response Element Binding Proteins

C/EBPβ, When Expressed from the C/ebpα Gene Locus, Can Functionally Replace C/EBPα in Liver but Not in Adipose Tissue

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