Expression of activating transcription factor-2, serum response factor and cAMP/Ca response element binding protein in the adult rat brain following generalized seizures, nerve fibre lesion and ultraviolet irradiation

Neuroscience ◽  
1997 ◽  
Vol 81 (1) ◽  
pp. 199-212 ◽  
Author(s):  
T Herdegen ◽  
A Blume ◽  
T Buschmann ◽  
E Georgakopoulos ◽  
C Winter ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Ultraviolet Irradiation ◽  
Serum Response Factor ◽  
Response Factor ◽  
Adult Rat ◽  
Generalized Seizures ◽  
Adult Rat Brain ◽  
Element Binding Protein ◽  
Activating Transcription Factor ◽  
Serum Response

scholarly journals Enhancement of Serum-response Factor-dependent Transcription and DNA Binding by the Architectural Transcription Factor HMG-I(Y)

1998 ◽  
Vol 273 (16) ◽  
pp. 9755-9760 ◽  
Author(s):  
Michael T. Chin ◽  
Andrea Pellacani ◽  
Hong Wang ◽  
Sharon S. J. Lin ◽  
Mukesh K. Jain ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Serum Response Factor ◽  
Response Factor ◽  
Serum Response

scholarly journals The transcription factors Elk-1 and serum response factor interact by direct protein-protein contacts mediated by a short region of Elk-1.

1994 ◽  
Vol 14 (5) ◽  
pp. 3283-3291 ◽  
Author(s):  
P Shore ◽  
A D Sharrocks
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Protein Interactions ◽  
Serum Response Factor ◽  
Specific Protein ◽  
Response Factor ◽  
Protein Protein Interactions ◽  
Amino Acid Peptide ◽  
Necessary And Sufficient ◽  
Serum Response

Transcriptional induction of the c-fos gene in response to epidermal growth factor stimulation is mediated in part by a ternary nucleoprotein complex within the promoter consisting of serum response factor (SRF), p62TCF/Elk-1 and the serum response element (SRE). Both SRF and p62TCF/Elk-1 contact the DNA and bind in a cooperative manner to the SRE. In this study, we demonstrate that SRF and Elk-1 interact directly in the absence of the SRE. A 30-amino-acid peptide from Elk-1 (B-box) is both necessary and sufficient to mediate protein-protein contacts with SRF. Moreover, the Elk-1 B-box is necessary to enable SRF-dependent binding of an alternative ETS domain (from the transcription factor PU.1) to the c-fos SRE. Mutations in either the Elk-1 B-box or the C-terminal half of the SRF DNA-binding domain (coreSRF) which show reduced ability to form ternary complexes also show greatly reduced protein-protein interactions in the absence of the SRE. Our results clearly demonstrate that direct protein-protein interactions between the transcription factors Elk-1 and SRF, in addition to DNA contacts, contribute to the formation of a ternary complex on the c-fos SRE. We discuss the wider applicability of our results in describing specific protein-protein interactions between short well-defined transcription factor domains.

scholarly journals Dual Specificity Phosphatase 5, a Specific Negative Regulator of ERK Signaling, Is Induced by Serum Response Factor and Elk-1 Transcription Factor

PLoS ONE ◽  
2015 ◽  
Vol 10 (12) ◽  
pp. e0145484 ◽  
Author(s):  
Camille Buffet ◽  
Maria-Grazia Catelli ◽  
Karine Hecale-Perlemoine ◽  
Léopoldine Bricaire ◽  
Camille Garcia ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Serum Response Factor ◽  
Negative Regulator ◽  
Erk Signaling ◽  
Response Factor ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity ◽  
Serum Response

Inhibition of c-fos transcription and phosphorylation of the serum response factor by an inhibitor of phospholipase C-type reactions

1990 ◽  
Vol 10 (10) ◽  
pp. 5558-5561
Author(s):  
G Schalasta ◽  
C Doppler
Keyword(s):  
Transcription Factor ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase C ◽  
Transcriptional Activation ◽  
Serum Response Factor ◽  
Response Factor ◽  
Kinase C ◽  
Beta Actin ◽  
Serum Response

Phospholipase C activity is necessary for transcriptional c-fos activation by providing diacylglycerol as an activator of protein kinase C. We found that transcriptional activation of c-fos and the phosphorylation of its major transcription factor were inhibited by tricyclodecan-9-yl xanthogenate, which blocks phospholipase C-type reactions. Transcription of the c-ras and beta-actin genes in the same cells remained unaffected.

scholarly journals Calcium activates serum response factor-dependent transcription by a Ras- and Elk-1-independent mechanism that involves a Ca2+/calmodulin-dependent kinase.

1995 ◽  
Vol 15 (7) ◽  
pp. 3672-3684 ◽  
Author(s):  
C K Miranti ◽  
D D Ginty ◽  
G Huang ◽  
T Chatila ◽  
M E Greenberg
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Growth Factors ◽  
Serum Response Factor ◽  
Active Form ◽  
Response Factor ◽  
Transcriptional Responses ◽  
Pheochromocytoma Cell ◽  
Independent Mechanism ◽  
Serum Response

Enhanced levels of cytoplasmic Ca2+ due to membrane depolarization with elevated levels of KCl or exposure to the Ca2+ ionophore ionomycin stimulate serum response element (SRE)-dependent transcription in the pheochromocytoma cell line PC12. By using altered binding specificity mutants of transcription factors that bind to the SRE, it was demonstrated that in contrast to treatment with purified growth factors, such as nerve growth factor, the serum response factor (SRF), but not Elk-1, mediates Ca(2+)-regulated SRE-dependent transcription. Enhanced levels of cytoplasmic Ca2+ were found to trigger SRE-dependent transcription via a Ras-independent signaling pathway that appears to involve a Ca2+/calmodulin-dependent kinase (CaMK). Overexpression of a constitutively active form of CaMKIV stimulated SRF-dependent transcription. Taken together, these findings indicate that SRF is a versatile transcription factor that, when bound to the SRE, can function by distinct mechanisms and can mediate transcriptional responses to both CaMK- and Ras-dependent signaling pathways.

Sign in / Sign up

Export Citation Format

Share Document