Protein kinase A inhibits lysophosphatidic acid induction of serum response factor via alterations in the actin cytoskeleton

2004 ◽  
Vol 16 (10) ◽  
pp. 1141-1151 ◽  
Author(s):  
Giang Huong Nguyen ◽  
Robert French ◽  
Harish Radhakrishna
Keyword(s):  
Protein Kinase ◽  
Actin Cytoskeleton ◽  
Protein Kinase A ◽  
Lysophosphatidic Acid ◽  
Serum Response Factor ◽  
Response Factor ◽  
Serum Response ◽  
Kinase A

scholarly journals Protein Kinase N1 control of androgen-responsive serum response factor action provides rationale for novel prostate cancer treatment strategy

Oncogene ◽  
2019 ◽  
Vol 38 (23) ◽  
pp. 4496-4511
Author(s):  
Varadha Balaji Venkadakrishnan ◽  
Adam D. DePriest ◽  
Sangeeta Kumari ◽  
Dhirodatta Senapati ◽  
Salma Ben-Salem ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Protein Kinase ◽  
Cancer Treatment ◽  
Treatment Strategy ◽  
Serum Response Factor ◽  
Response Factor ◽  
Prostate Cancer Treatment ◽  
Serum Response

scholarly journals A Pathogenic Relationship Between a Regulator of the Actin Cytoskeleton and Serum Response Factor

Genetics ◽  
2010 ◽  
Vol 186 (1) ◽  
pp. 147-157 ◽  
Author(s):  
Angela M. Verdoni ◽  
Keaton J. Schuster ◽  
Brian S. Cole ◽  
Akihiro Ikeda ◽  
Winston W. Kao ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Serum Response Factor ◽  
Response Factor ◽  
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 Neurokinin B Induces c-fos Transcription via Protein Kinase C and Activation of Serum Response Factor and Elk-1 in Immortalized GnRH Neurons

Endocrinology ◽  
2014 ◽  
Vol 155 (10) ◽  
pp. 3909-3919 ◽  
Author(s):  
Christine A. Glidewell-Kenney ◽  
Crystal Trang ◽  
Paul P. Shao ◽  
Navarre Gutierrez-Reed ◽  
Adaku M. Uzo-Okereke ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Serum Response Factor ◽  
Response Factor ◽  
Gnrh Neuron ◽  
Serum Response Element ◽  
Neurokinin B ◽  
Response Element ◽  
Kinase C ◽  
Serum Response

Abstract Mutations in neurokinin B (NKB) and its receptor, NK3R, were identified in human patients with hypogonadotropic hypogonadism, a disorder characterized by lack of puberty and infertility. Further studies have suggested that NKB acts at the level of the hypothalamus to control GnRH neuron activity, either directly or indirectly. We recently reported that treatment with senktide, a NK3R agonist, induced GnRH secretion and expression of c-fos mRNA in GT1-7 cells. Here, we map the responsive region in the murine c-fos promoter to between −400 and −200 bp, identify the signal transducer and activator of transcription (STAT) (−345) and serum response element (−310) sites as required for induction, a modulatory role for the Ets site (−318), and show that induction is protein kinase C dependent. Using gel shift and Gal4 assays, we further show that phosphorylation of Elk-1 leads to binding to DNA in complex with serum response factor at serum response element and Ets sites within the c-fos promoter. Thus, we determine molecular mechanisms involved in NKB regulation of c-fos induction, which may play a role in modulation of GnRH neuron activation.

scholarly journals Protein Kinase Cδ Blocks Immediate-Early Gene Expression in Senescent Cells by Inactivating Serum Response Factor

2004 ◽  
Vol 24 (16) ◽  
pp. 7298-7311 ◽  
Author(s):  
Keith Wheaton ◽  
Karl Riabowol
Keyword(s):  
Gene Expression ◽  
Protein Kinase ◽  
Serum Response Factor ◽  
Immediate Early Gene ◽  
Early Gene ◽  
Immediate Early ◽  
Response Factor ◽  
Serum Response

ABSTRACT Fibroblasts lose the ability to replicate in response to growth factors and become unable to express growth-associated immediate-early genes, including c-fos and egr-1, as they become senescent. The serum response factor (SRF), a major transcriptional activator of immediate-early gene promoters, loses the ability to bind to the serum response element (SRE) and becomes hyperphosphorylated in senescent cells. We identify protein kinase C delta (PKCδ) as the kinase responsible for inactivation of SRF both in vitro and endogenously in senescent cells. This is due to a higher level of PKCδ activity as cells age, production of the PKCδ catalytic fragment, and its nuclear localization in senescent but not in low-passage-number cells. The phosphorylation of T160 of SRF by PKCδ in vitro and in vivo led to loss of SRF DNA binding activity. Both the PKCδ inhibitor rottlerin and ectopic expression of a dominant negative form of PKCδ independently restored SRE-dependent transcription and immediate-early gene expression in senescent cells. Modulation of PKCδ activity in vivo with rottlerin or bistratene A altered senescent- and young-cell morphology, respectively. These observations support the idea that the coordinate transcriptional inhibition of several growth-associated genes by PKCδ contributes to the senescent phenotype.

Serum response factor: master regulator of the actin cytoskeleton and contractile apparatus

2007 ◽  
Vol 292 (1) ◽  
pp. C70-C81 ◽  
Author(s):  
Joseph M. Miano ◽  
Xiaochun Long ◽  
Keigi Fujiwara
Keyword(s):  
Transcription Factor ◽  
Actin Cytoskeleton ◽  
Target Genes ◽  
Serum Response Factor ◽  
Cellular Growth ◽  
Cellular Migration ◽  
Actin Dynamics ◽  
Response Factor ◽  
Master Regulator ◽  
Serum Response

Serum response factor (SRF) is a highly conserved and widely expressed, single copy transcription factor that theoretically binds up to 1,216 permutations of a 10-base pair cis element known as the CArG box. SRF-binding sites were defined initially in growth-related genes. Gene inactivation or knockdown studies in species ranging from unicellular eukaryotes to mice have consistently shown loss of SRF to be incompatible with life. However, rather than being critical for proliferation and growth, these genetic studies point to a crucial role for SRF in cellular migration and normal actin cytoskeleton and contractile biology. In fact, recent genomic studies reveal nearly half of the >200 SRF target genes encoding proteins with functions related to actin dynamics, lamellipodial/filopodial formation, integrin-cytoskeletal coupling, myofibrillogenesis, and muscle contraction. SRF has therefore emerged as a dispensable transcription factor for cellular growth but an absolutely essential orchestrator of actin cytoskeleton and contractile homeostasis. This review summarizes the recent genomic and genetic analyses of CArG-SRF that support its role as an ancient, master regulator of the actin cytoskeleton and contractile machinery.

Sign in / Sign up

Export Citation Format

Share Document