Two distinct forms of active transcription factor CREB (cAMP response element binding protein).

Berkowitz, Laura A.; Gilman, Michael

doi:10.1073/pnas.87.14.5258

Cited by 118 publications

(58 citation statements)

References 26 publications

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“…Yamamoto et al (35) found that CREB341 is more active than CREB327 in stimulating transcription from the somatostatin gene CRE. However, in two other studies the presence of the cc peptide did not result in increased CREB activity (34,36). Therefore, the functional significance of the cc peptide is still unclear.…”

Section: Regulation Of Gene Transcription By Protein Kinase A-specifimentioning

confidence: 99%

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

Vallejo

1994

J Neuroendocrinology

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Section: Regulation Of Gene Transcription By Protein Kinase A-specifimentioning

confidence: 99%

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

Vallejo

1994

J Neuroendocrinology

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“…The membrane was detected with anti-phosphorylated CREB (Upstate Biotechnology) or anti-CREB (25) using ECL reagents (Amersham). The doublet of CREB corresponding to CREB341 and CREB327 was previously reported (70). pCREB, CREB phosphorylated at Ser 133 .…”

Section: Synergistic Effect Of Erk P38 Mapk and Ca 2ϩ On Creb Transmentioning

confidence: 99%

Multiple Signals Required for Cyclic AMP-Responsive Element Binding Protein (CREB) Binding Protein Interaction Induced by CD3/CD28 Costimulation

Shih²,

Lai

2001

The Journal of Immunology

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The optimal activation of cAMP-responsive element binding protein (CREB), similar to the full activation of T lymphocytes, requires the stimulation of both CD3 and CD28. Using a reporter system to detect interaction of CREB and CREB-binding protein (CBP), in this study we found that CREB binds to CBP only by engagement of both CD3 and CD28. CD3/CD28-promoted CREB-CBP interaction was dependent on p38 mitogen-activated protein kinase (MAPK) and calcium/calmodulin-dependent protein kinase (CaMK) IV in addition to the previously identified extracellular signal-regulated kinase pathway. Extracellular signal-regulated kinase, CaMKIV, and p38 MAPK were also the kinases involved in CREB Ser133 phosphorylation induced by CD3/CD28. A reconstitution experiment illustrated that optimum CREB-CBP interaction and CREB trans-activation were attained when these three kinase pathways were simultaneously activated in T cells. Our results demonstrate that coordinated activation of different kinases leads to full activation of CREB. Notably, CD28 ligation activated p38 MAPK and CaMKIV, the kinases stimulated by CD3 engagement, suggesting that CD28 acts by increasing the activation extent of p38 MAPK and CaMKIV. These results support the model of a minimum activation threshold for CREB-CBP interaction that can be reached only when both CD3 and CD28 are stimulated.

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“…In addition, we also tested a modified form of NF-KB p65, NF-KB p65mLZ, containing a point mutation in a recently VOL. 13,1993 described leucine zipper-like structure (73). For comparison of the effects of rat C/EBPP on KB enhancer-dependent gene expression, the amounts of transfected expression vectors for NF-KB proteins were adjusted to obtain similar levels of induced CAT activity.…”

mentioning

confidence: 99%

“…The mouse c-Jun, human c-Fos, and human CREB pCMV4T expression vectors contain full-length coding sequences of the corresponding T7 polymerase-driven vectors (13,69,70) cloned downstream of the CMV immediate-early-region promoter. The wild-type Myb expression vector (pRmb3SVneo) and the corresponding frameshift control pJTmyb-fs have been described elsewhere (25).…”

mentioning

confidence: 99%

Functional and physical associations between NF-kappa B and C/EBP family members: a Rel domain-bZIP interaction.

Stein¹,

Cogswell²,

Baldwin³

1993

Mol. Cell. Biol.

500

340

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NF-KB and C/EBP represent distinct families of transcription factors that target unique DNA enhancer elements. The heterodimeric NF-KB complex is composed of two subunits, a 50-and a 65-kDa protein. All members of the NF-cB family, including the product of the proto-oncogene c-rel, are characterized by their highly homologous -300-amino-acid N-terminal region. This Rel homology domain mediates DNA binding, dimerization, and nuclear targeting of these proteins. C/EBP contains the bZIP region, which is characterized by two motifs in the C-terminal half of the protein: a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. The C/EBP family consists of several related proteins, C/EBPa, C/EBP3, C/EBP-y, and C/EBP8, that form homodimers and that form heterodimers with each other. We now demonstrate the unexpected cross-coupling of members of the NF-cB family with three members of the C/EBP family. NF-cB p65, p50, and Rel functionally synergize with C/EBPa, C/EBPf3, and C/EBP8. This cross-coupling results in the inhibition of promoters with KB enhancer motifs and in the synergistic stimulation of promoters with C/EBP binding sites. These studies demonstrate that NF-KB augments gene expression mediated by a multimerized c-fos serum response element in the presence of C/EBP. We show a direct physical association of the bZIP region of C/EBP with the Rel homology domain of NF-KB. The cross-coupling of NF-cB with C/EBP highlights a mechanism of gene regulation involving an interaction between distinct transcription factor families.Transcriptional regulation of gene expression is controlled by factors that bind to specific DNA sequences. Many of these factors can be classified into distinct families based on common structural motifs. These families include the homeodomain family (30), the zinc finger proteins (26, 46), the leucine zipper family (49,84), and the helix-loop-helix family (59, 60). Many of these transcription factors bind to their cognate DNA motifs as homodimers and, moreover, there are multiple examples of heterodimer formation within the same family of transcription factors. However, there is growing evidence that these dimerization motifs are also involved in interactions between transcription factors from different families. Examples are the interaction of the Jun leucine zipper region with the helix-loop-helix motif of MyoD (12) (24,42,74,87). This cross-coupling between different families might lead to the formation of novel transcription factor complexes displaying altered biological activities.The transcription factor NF-KB binds to KB enhancer motifs found in a variety of genes in response to various signals (5 and references therein, 35, 51). NF-KB DNA binding activity typically involves two subunits, a 50-kDa protein (17, 31, 45) and a 65-kDa protein (63,72). NF-KB p50 and NF-KB p65 share a highly homologous 300-residue N-terminal region. This region is also found in the products of the proto-oncogene c-rel and of the dorsal maternal effect gene of Drosophila mela...

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Two distinct forms of active transcription factor CREB (cAMP response element binding protein).

Cited by 118 publications

References 26 publications

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

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

Multiple Signals Required for Cyclic AMP-Responsive Element Binding Protein (CREB) Binding Protein Interaction Induced by CD3/CD28 Costimulation

Functional and physical associations between NF-kappa B and C/EBP family members: a Rel domain-bZIP interaction.

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