scholarly journals Regulation of ENA1 Na+-ATPase Gene Expression by the Ppz1 Protein Phosphatase Is Mediated by the Calcineurin Pathway

2003 ◽  
Vol 2 (5) ◽  
pp. 937-948 ◽  
Author(s):  
Amparo Ruiz ◽  
Lynne Yenush ◽  
Joaquín Ariño
Keyword(s):  
Gene Expression ◽  
Protein Phosphatase ◽  
Calcineurin Inhibitor ◽  
Salt Tolerant ◽  
Single Region ◽  
Atpase Gene ◽  
Sodium Extrusion ◽  
Increased Activity ◽  
Calcineurin Activity ◽  
Intracellular Alkalinization

ABSTRACT Saccharomyces cerevisiae strains lacking the Ppz1 protein phosphatase are salt tolerant and display increased expression of the ENA1 Na+-ATPase gene, a major determinant for sodium extrusion, while cells devoid of the similar Ppz2 protein do not show these phenotypes. However, a ppz1 ppz2 mutant displays higher levels of ENA1 expression than the ppz1 strain. We show here that the increased activity of the ENA1 promoter in a ppz1 ppz2 mutant maps to two regions: one region located at −751 to −667, containing a calcineurin-dependent response element (CDRE), and one downstream region (−573 to −490) whose activity responds to intracellular alkalinization. In contrast, the increased ENA1 expression in a ppz1 mutant is mediated solely by an intact calcineurin/Crz1 signaling pathway, on the basis that (i) this effect maps to a single region that contains the CDRE and (ii) it is blocked by the calcineurin inhibitor FK506, as well as by deletion of the CNB1 or CRZ1 gene. The calcineurin dependence of the increased ENA1 expression of a ppz1 mutant would suggest that Ppz1 could negatively regulate calcineurin activity. In agreement with this notion, a ppz1 strain is calcium sensitive, and this mutation does not result in a decrease in the calcium hypertolerance of a cnb1 mutant. It has been shown that ENA1 can be induced by alkalinization of the medium and that a ppz1 ppz2 strain has a higher intracellular pH. However, we present several lines of evidence that show that the gene expression profile of a ppz1 mutant does not involve an alkalinization effect. In conclusion, we have identified a novel role for calcineurin, but not alkalinization, in the control of ENA1 expression in ppz1 mutants.

Plasma Membrane Calcium ATPase Gene Expression in Bovine Lens Epithelium

2000 ◽  
Vol 32 (2-3) ◽  
pp. 100-105 ◽  
Author(s):  
Lijun Bian ◽  
Junwen Zeng ◽  
Douglas Borchman ◽  
Christopher A. Paterson
Keyword(s):  
Gene Expression ◽  
Plasma Membrane ◽  
Calcium Atpase ◽  
Lens Epithelium ◽  
Plasma Membrane Calcium Atpase ◽  
Bovine Lens ◽  
Atpase Gene

Protein phosphatase 2A potentiates activity of promoters containing AP-1-binding elements

1993 ◽  
Vol 13 (4) ◽  
pp. 2104-2112
Author(s):  
A S Alberts ◽  
T Deng ◽  
A Lin ◽  
J L Meinkoth ◽  
A Schönthal ◽  
...  
Keyword(s):  
Gene Expression ◽  
Reporter Gene ◽  
Protein Phosphatase ◽  
Signal Transduction Pathways ◽  
Marker Genes ◽  
Direct Mechanism ◽  
Phosphatase 2A ◽  
Beta Galactosidase ◽  
Regulatory Sites

The involvement of serine/threonine protein phosphatases in signaling pathways which modulate the activity of the transcription factor AP-1 was examined. Purified protein phosphatase types 1 (PP1) and 2A (PP2A) were microinjected into cell lines containing stably transfected lacZ marker genes under the control of an enhancer recognized by AP-1. Microinjection of PP2A potentiated serum-stimulated beta-galactosidase expression from the AP-1-regulated promoter. Similarly, transient expression of the PP2A catalytic subunit with c-Jun resulted in a synergistic transactivation of an AP-1-regulated reporter gene. PP2A, but not PP1, potentiated serum-induced c-Jun expression, which has been previously shown to be autoregulated by AP-1 itself. Consistent with these results, PP2A dephosphorylated c-Jun on negative regulatory sites in vitro, suggesting one possible direct mechanism for the effects of PP2A on AP-1 activity. Microinjection of PP2A had no effect on cyclic AMP (cAMP)-induced expression of a reporter gene containing a cAMP-regulated promoter, while PP1 injection abolished cAMP-induced gene expression. Taken together, these results suggest a specific role for PP2A in signal transduction pathways that regulate AP-1 activity and c-Jun expression.

Regulation of oligopeptide transporter (Pept-1) in experimental diabetes

2002 ◽  
Vol 283 (1) ◽  
pp. G133-G138 ◽  
Author(s):  
Archana Gangopadhyay ◽  
Manikkavasagar Thamotharan ◽  
Siamak A. Adibi
Keyword(s):  
Gene Expression ◽  
Intestinal Mucosa ◽  
Brush Border Membrane ◽  
Experimental Diabetes ◽  
Maximal Velocity ◽  
Gene Expressions ◽  
Oligopeptide Transporter ◽  
Uncontrolled Diabetes ◽  
Increased Activity ◽  
Menten Constant

The knowledge of expression and biology of the intestinal oligopeptide transporter (Pept-1) in a metabolic disorder such as diabetes may have nutritional and pharmacological implications. To study this problem, rats were made diabetic by streptozotocin injection, and Western and Northern blot analyses and nuclear run-on assay were used to determine the protein and gene expressions of Pept-1 and its rate of transcription, respectively. Uncontrolled diabetes for 96 h increased the activity of Pept-1 in the brush-border membrane of intestinal mucosa. Studies of Michaelis-Menten constant, maximal velocity, and protein expression of Pept-1 indicated that an increase in the abundance of this transporter was responsible for the increased activity. Studies of the gene expression showed that uncontrolled diabetes increased the abundance of mRNA encoding Pept-1 without altering its rate of transcription. Lastly, studies of the specificity of the above effect showed that uncontrolled diabetes similarly affected the protein and gene expressions of Pept-1 located in the kidney. In conclusion, the data show that 1) uncontrolled diabetes has a tropic effect on Pept-1 and 2) the effect is systemic, and its molecular mechanism appears to be an increase in the stabilization of mRNA encoding Pept-1.

scholarly journals Differential expression of protein phosphatase PPM1B and multiple protein phosphatase regulatory subunits in glioblastoma.

2020 ◽  
Author(s):  
Shahan Mamoor
Keyword(s):  
Gene Expression ◽  
Brain Tissue ◽  
Protein Phosphatase ◽  
Treatment Options ◽  
Normal Brain ◽  
Regulatory Subunits ◽  
Gene Expression Information ◽  
Multiple Protein ◽  
Substrate Phosphorylation ◽  
Public Dataset

Glioblastoma multiforme is an aggressive brain cancer with few treatment options and poor survival outcomes (1, 2). We used a public dataset (3) containing the gene expression information of tumors from 17 patients diagnosed with glioblastoma and compared it to the gene expression information from the non-cancerous, healthy brain tissue from 8 individuals as a reference control, to understand what is most different between the transcriptional behavior of glioblastoma tumors relative to the tissue it arises from. We found that protein phosphatase PPM1B and three protein phosphatase regulatory subunits were among the genes whose expression was most different between glioblastoma tumors and “normal” brain tissue. The fact that multiple phosphatase regulatory genes are expressed at significantly lower levels in glioblastoma tumors suggests that alteration of substrate phosphorylation might be an important event in glioblastoma formation, maintenance or progression.

scholarly journals The full-length transcriptome of Spartina alterniflora reveals the complexity of high salt tolerance in monocotyledonous halophyte

2019 ◽  
Author(s):  
Wenbin Ye ◽  
Taotao Wang ◽  
Wei Wei ◽  
Shuaitong Lou ◽  
Faxiu Lan ◽  
...  
Keyword(s):  
Gene Expression ◽  
Salt Stress ◽  
Alternative Splicing ◽  
Salt Tolerance ◽  
Protein Kinases ◽  
Spartina Alterniflora ◽  
High Salt ◽  
Full Length ◽  
Salt Tolerant ◽  
High Salt Tolerance

ABSTRACTSpartina alterniflora (Spartina) is the only halophyte in the salt marsh. However, the molecular basis of its high salt tolerance remains elusive. In this study, we used PacBio full-length single molecule long-read sequencing and RNA-seq to elucidate the transcriptome dynamics of high salt tolerance in Spartina by salt-gradient experiments (0, 350, 500 and 800 mM NaCl). We systematically analyzed the gene expression diversity and deciphered possible roles of ion transporters, protein kinases and photosynthesis in salt tolerance. Moreover, the co-expression network analysis revealed several hub genes in salt stress regulatory networks, including protein kinases such as SaOST1, SaCIPK10 and three SaLRRs. Furthermore, high salt stress affected the gene expression of photosynthesis through down-regulation at the transcription level and alternative splicing at the post-transcriptional level. In addition, overexpression of two Spartina salt-tolerant genes SaHSP70-I and SaAF2 in Arabidopsis significantly promoted the salt tolerance of transgenic lines. Finally, we built the SAPacBio website for visualizing the full-length transcriptome sequences, transcription factors, ncRNAs, salt-tolerant genes, and alternative splicing events in Spartina. Overall, this study sheds light on the high salt tolerance mechanisms of monocotyledonous-halophyte and demonstrates the potential of Spartina genes for engineering salt-tolerant plants.

Plasma-membrane H+-ATPase gene expression is regulated by NaCl in cells of the halophyte Atriplex nummularia L.

Planta ◽  
1993 ◽  
Vol 190 (4) ◽  
Author(s):  
Xiaomu Niu ◽  
Jian-Kang Zhu ◽  
MeenaL. Narasimhan ◽  
RayA. Bressan ◽  
PaulM. Hasegawa
Keyword(s):  
Gene Expression ◽  
Plasma Membrane ◽  
Atpase Gene ◽  
Atriplex Nummularia ◽  
In Cells

Cadmium effect on vacuolar H+-ATPase gene expression in the roots of barley seedlings of different age

2012 ◽  
Vol 60 (1) ◽  
pp. 55-59 ◽  
Author(s):  
N. M. Kaznina ◽  
A. F. Titov ◽  
L. V. Topchieva ◽  
G. F. Laidinen ◽  
Yu. V. Batova
Keyword(s):  
Gene Expression ◽  
Atpase Gene

Calcineurin Regulates Synaptic Plasticity and Nociceptive Transmissionat the Spinal Cord Level

2021 ◽  
pp. 107385842110468
Author(s):  
Yuying Huang ◽  
Shao-Rui Chen ◽  
Hui-Lin Pan
Keyword(s):  
Spinal Cord ◽  
Neuropathic Pain ◽  
Protein Phosphatase ◽  
Transient Receptor Potential ◽  
Calcineurin Inhibitors ◽  
Receptor Potential ◽  
Transient Receptor Potential Channels ◽  
Negative Feedback Regulation ◽  
Spinal Cord Level ◽  
Calcineurin Activity

Calcineurin, the predominant Ca2+/calmodulin-dependent serine/threonine protein phosphatase (also known as protein phosphatase 2B), is highly expressed in immune T cells and the nervous system, including the dorsal root ganglion and spinal cord. It controls synaptic transmission and plasticity by maintaining the appropriate phosphorylation status of many ion channels present at presynaptic and postsynaptic sites. As such, normal calcineurin activity in neurons and synapses is mainly involved in negative feedback regulation in response to increased neuronal activity and intracellular Ca2+ levels. Calcineurin inhibitors (e.g., cyclosporine and tacrolimus) are widely used as immunosuppressants in tissue and organ transplantation recipients and for treating autoimmune diseases but can cause severe pain in some patients. Furthermore, diminished calcineurin activity at the spinal cord level may play a major role in the transition from acute to chronic neuropathic pain after nerve injury. Restoring calcineurin activity at the spinal cord level produces long-lasting pain relief in animal models of neuropathic pain. In this article, we provide an overview of recent studies on the critical roles of calcineurin in regulating glutamate NMDA and AMPA receptors, voltage-gated Ca2+ channels, potassium channels, and transient receptor potential channels expressed in the spinal dorsal horn and primary sensory neurons.

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