cGMP-dependent Protein Kinase Iβ Physically and Functionally Interacts with the Transcriptional Regulator TFII-I

Casteel, Darren E.; Zhuang, Shunhui; Gudi, Tanima; Tang, Julian W.; Vuica, Milena; Desiderio, Stephen; Pilz, Renate B.

doi:10.1074/jbc.m112332200

Cited by 63 publications

(106 citation statements)

References 70 publications

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“…16,17 Since cGKs and cAKs are highly homologous protein kinase families that possess similar substrate specificities, a similar pathway could be proposed for cGMP. Thus, several studies showed that cGMP-dependent protein kinase could interact with transcription factors such as TFII 18 and NFB. 19 Moreover, cGMP was recently proposed to be involved in other signaling pathways including MAPK1 20 and CaMKinase II cascade.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a cGMP-Response Element in the Guanylyl Cyclase/Natriuretic Peptide Receptor A Gene Promoter

et al. 2004

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Abstract-Previous studies have shown that atrial natriuretic peptide (ANP) can inhibit transcription of its receptor, guanylyl cyclase A, by a mechanism dependent on cGMP and have suggested the presence of a putative cGMP-response element (cGMP-RE) in the Npr1 gene promoter. To localize and characterize the putative cis-acting element, we have subcloned a 1520-bp fragment of the rat Npr1 promoter in an expression vector containing the luciferase reporter gene. Several fragments, generated by exonuclease III-directed deletions, were transiently transfected into cells to measure their promoter activity. Deletion from Ϫ1520 to Ϫ1396 of a 1520-bp-long Npr1 promoter led to a 5-fold increase in luciferase activity. Subsequent deletion to the position Ϫ1307 resulted in a decrease of luciferase activity by 90%. Preincubation of cells with 100 nM of ANP or 100 M 8-bromo-cGMP inhibited luciferase activity of the 1520-bp and 1396-bp-long fragments, but not the activity of the 1307-bp fragment, suggesting that the cGMP-RE is localized between positions Ϫ1396 and Ϫ1307. The cGMP regulatory region was narrowed by gel shift assays and footprinting to position Ϫ1372 to Ϫ1354 from the transcription start site of Npr1 and indicated its interaction with transcriptional factor(s). Cross-competition experiments with mutated oligonucleotides led to the definition of a consensus sequence (Ϫ1372 AaAtRKaNTTCaAcAKTY Ϫ1354) for the novel cGMP-RE, which is conserved in the human (75% identity) and mouse (95% identity) Npr1 promoters. Key Words: cyclic GMP Ⅲ natriuretic peptides Ⅲ receptors, atrial natriuretic factor A trial natriuretic peptide (ANP) is a cardiac hormone with potent effects in the kidney, vasculature, and nervous system. It has vasorelaxant activity in vascular smooth muscle and promotes urinary sodium and water excretion by the kidney (for review, see Reference 1 ). These actions of ANP are brought about via the activation of membrane-bound protein, natriuretic peptide receptor type A (NPR-A), or guanylyl cyclase A. 2-4 NPR-A is a 130-KDa transmembrane protein containing an ANP-binding motif at its extracellular NH 2 terminus and GC activity at its COOH-terminal intracellular domain. 5 Activation of NPR-A leads to the conversion of GTP to the intracellular second messenger cGMP, which is involved in most of the biological responses associated with natriuretic peptides. 2-5 Increased cGMP yields receptor desensitization, resulting in a decrease of ANP-stimulated cGMP synthesis. 6 Receptor preoccupancy appears to be a mechanism of apparent receptor desensitization 7 but transfection experiments with NPR-A cDNA have revealed that early desensitization by ANP pretreatment can be due to dephosphorylation of NPR-A protein. 8 Besides, a previous study demonstrated that NPR-A activity, as well as its mRNA levels, is diminished in a time-and concentration-dependent manner by ANP or by a cell-permeable cGMP analog, 8-bromo-cGMP. 9 Those results suggest transcriptional regulation via a putative cGMPresponse element (cGMP-RE) in the p...

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Section: Discussionmentioning

confidence: 99%

Characterization of a cGMP-Response Element in the Guanylyl Cyclase/Natriuretic Peptide Receptor A Gene Promoter

et al. 2004

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“…Surprisingly, TFII-I was found to specifically interact with G-kinase Iβ in vitro and in vivo (44). cGMP analogs enhanced association between TFII-I and G-kinase Iβ in the nucleus (44). Importantly, from a regulatory standpoint, G-kinase was shown to phosphorylate TFII-I on two serine residues (S371 and S743) in vitro and in vivo, which potentiated TFII-I dependent transcriptional activation of c-fos.…”

Section: Role Of Tfii-i In G-kinase Pathwaymentioning

confidence: 99%

“…Importantly, from a regulatory standpoint, G-kinase was shown to phosphorylate TFII-I on two serine residues (S371 and S743) in vitro and in vivo, which potentiated TFII-I dependent transcriptional activation of c-fos. Consequently, mutation of these two serine residues resulted in a loss of TFII-I dependent transcriptional activation of cfos (44). Whether the physical and functional interactions between TFII-I and G-kinase Iβ leads to additional interactions of TFII-I with other transcriptional regulators or whether G-kinase Iβ is recruited to the c-fos promoter together with TFII-I remains to be determined.…”

Section: Role Of Tfii-i In G-kinase Pathwaymentioning

confidence: 99%

“…For example, transcriptional regulation of c-fos by nitric oxide and cGMP can occur by nuclear translocation of G-kinase I (43,44). Surprisingly, TFII-I was found to specifically interact with G-kinase Iβ in vitro and in vivo (44). cGMP analogs enhanced association between TFII-I and G-kinase Iβ in the nucleus (44).…”

Section: Role Of Tfii-i In G-kinase Pathwaymentioning

confidence: 99%

“…The resulting transcriptional effects are either positive or negative (43). For example, transcriptional regulation of c-fos by nitric oxide and cGMP can occur by nuclear translocation of G-kinase I (43,44). Surprisingly, TFII-I was found to specifically interact with G-kinase Iβ in vitro and in vivo (44).…”

Section: Role Of Tfii-i In G-kinase Pathwaymentioning

confidence: 99%

See 2 more Smart Citations

Signal-induced functions of the transcription factor TFII-I

Roy

2007

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expres

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We have learned a great deal over the last several years about the molecular mechanisms that govern cell growth, cell division and cell death. Normal cells pass through cell cycle (growth) and divide in response to mitogenic signals that are transduced through their cognate cell surface receptors to the nucleus. Despite the fact that cellular growth and division are mechanistically distinct steps, they are usually coordinately regulated, which is critical for normal cellular proliferation. The precise mechanistic basis for this coordinated regulation is unclear. TFII-I is a unique, signal induced multifunctional transcription factor that is activated upon a variety of signaling pathways and appears to participate in distinct phases of cell growth. For instance, TFII-I is required for growth factorinduced transcriptional activation of the c-fos gene, which is essential for cell cycle entry. Two alternatively spliced isoforms of TFII-I exhibit opposing but necessary functions for mitogen-induced transcriptional activation of c-fos. Besides transcriptional activation of the c-fos proto-oncogene and eventual entry into cell cycle, TFII-I also appears to have a role in later phases of the cell cycle and cell division. Here we discuss how a multitude of signaling inputs target TFII-I isoforms, which may exert their functions in distinct phases of the cell cycle and play a key role in the coordinated regulation of cellular proliferation.

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A multi‐angular mass spectrometric view at cyclic nucleotide dependent protein kinases: In vivo characterization and structure/function relationships

Scholten

Aye

Heck

2008

Mass Spectrometry Reviews

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Mass spectrometry has evolved in recent years to a well-accepted and increasingly important complementary technique in molecular and structural biology. Here we review the many contributions mass spectrometry based studies have made in recent years in our understanding of the important cyclic nucleotide activated protein kinase A (PKA) and protein kinase G (PKG). We both describe the characterization of kinase isozymes, substrate phosphorylation, binding partners and post-translational modifications by proteomics based methodologies as well as their structural and functional properties as revealed by native mass spectrometry, H/D exchange MS and ion mobility. Combining all these mass spectrometry based data with other biophysical and biochemical data has been of great help to unravel the intricate regulation of kinase function in the cell in all its magnificent complexity.

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cGMP-dependent Protein Kinase Iβ Physically and Functionally Interacts with the Transcriptional Regulator TFII-I

Cited by 63 publications

References 70 publications

Characterization of a cGMP-Response Element in the Guanylyl Cyclase/Natriuretic Peptide Receptor A Gene Promoter

Characterization of a cGMP-Response Element in the Guanylyl Cyclase/Natriuretic Peptide Receptor A Gene Promoter

Signal-induced functions of the transcription factor TFII-I

A multi‐angular mass spectrometric view at cyclic nucleotide dependent protein kinases: In vivo characterization and structure/function relationships

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