Regulation of aquaporin-2 abundance by TAZ in the kidney collecting duct cells
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ABSTRACT:
PROVIDER: PRJNA1148532 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR30260800_1.fastq.gz | Fastqsanger.gz | |||
| SRR30260800_2.fastq.gz | Fastqsanger.gz | |||
| SRR30260801_1.fastq.gz | Fastqsanger.gz | |||
| SRR30260801_2.fastq.gz | Fastqsanger.gz | |||
| SRR30260802_1.fastq.gz | Fastqsanger.gz |
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Project description:Background: The transcriptional coactivator with a PDZ-binding motif (TAZ), a downstream effector of the Hippo signaling pathway, regulates the expression of target genes by acting as a transcription cofactor. TAZ knockout (KO) mice exhibit polycystic kidneys and polyuria. This study aimed to investigate the role of TAZ in vasopressin-induced AQP2 regulation. Methods: 1) TAZ knockdown mediated by siRNA in mpkCCDc11 cells; 2) qRT-PCR, semiquantitative immunoblotting, and immunocytochemistry of AQP2; and 3) Next Generation Sequencing (NGS) in mpkCCDc11 cells, a mouse collecting duct cell line. Results: Endogenous expression of AQP2 was induced in mpkCCDc11 cells by treatment with dDAVP (10-9 M) treatment. Treatment with dDAVP (10-9 M) for 24 h increased AQP2 mRNA (12,608 ± 177% of control) and AQP2 protein levels (287 ± 15%). On the contrary, the increase induced by dDAVP in AQP2 mRNA (9,240 ± 241% of the control) and protein levels (215 ± 23%) was significantly reduced in TAZ-KD cells. TonEBP protein levels remained unchanged in TAZ-KD cells. NGS identified several potential AQP2 transcription factors (TF), including Klf6, Irf3, Cebpb, and Nr4a1, selected based on previous in silico database analysis. Among these, Nr4a1 was chosen for further investigation due to its significantly reduced expression of mRNA in TAZ-KD cells, as confirmed by qRT-PCR. Conclusion: TAZ appears to affect dDAVP-induced AQP2 trafficking through mechanisms not mediated by the cAMP/PKA pathway, suggesting the involvement of other non-canonical pathways. TAZ may also regulate AQP2 abundance, potentially through interaction with several transcription factors, including Nr4a1.
2024-09-30 | GSE274937 | GEO
Project description:Phosphorylation of the aquaporin-2 (AQP2) water channel at four COOH-terminal serines plays a central role in the regulation of water permeability of the renal collecting duct. The level of phosphorylation at these sites is determined by a balance between phosphorylation by protein kinases and dephosphorylation by phosphatases. The phosphatases that dephosphorylate AQP2 have not been identified. Here, we use large-scale data integration techniques to identify serine-threonine phosphatases likely to interact with AQP2 in renal collecting duct principal cells. As a first step, we have created a comprehensive list of 38 S/T phosphatase catalytic subunits present in the mammalian genome. Then we used Bayes’ theorem to integrate available information from large-scale data sets from proteomic and transcriptomic studies in order to rank the known S/T phosphatases with regard to the likelihood that they interact with AQP2 in renal collecting duct cells. To broaden the analysis, we have generated new proteomic data (LC-MS/MS) identifying 4538 distinct proteins including 22 S/T phosphatases in cytoplasmic fractions from native inner medullary collecting duct cells from rats. The official gene symbols corresponding to the top-ranked phosphatases (common names in parentheses) were: Ppp1cb (PP1-beta), Ppm1g (PP2C), Ppp1ca (PP1-alpha), Ppp3ca (PP2-B or calcineurin), Ppp2ca (PP2A-alpha), Ppp1cc (PP1-gamma), Ppp2cb (PP2A-beta), Ppp6c (PP6C) and Ppp5c (PP5). This ranking correlates well with results of prior reductionist studies of ion and water channels in renal collecting duct cells.
2018-10-26 | PXD005488 | Pride
Project description:Vasopressin is the major hormone that regulates renal water excretion. It does so by binding to a receptor in renal collecting duct cells, triggering signaling pathways that ultimately regulate the abundance, location, and activity of the water channel protein aquaporin 2. We took an advantage of quantitative large scale proteomic technologies and oligonucleotide microarrays to quantify steady state changes in protein and transcript abundances in response to vasopressin in a collecting duct cell line, mpkCCD clone 11 (Yu et al. PNAS 2009, 106:2441-2446). This cell line originally developed by Alan Vandewalle’s group recapitulates vasopressin-mediated AQP2 expression and phosphorylation as seen in native colleting duct cells.
2010-12-09 | GSE19938 | GEO
Project description:In mammals, the peptide hormone vasopressin controls renal water excretion, largely through regulation of the molecular water channel aquaporin-2 (AQP2) in the renal collecting duct. Regulatory mechanisms of AQP2 show: 1) short-term regulation by membrane trafficking; and 2) long-term regulation involving vasopressin-induced changes in the abundance of the aquaporin-2 protein. Vasopressin activates a G protein-coupled receptor (V2R) increasing cyclic AMP and activating protein kinase PKA. Crebbp and Ep300 are known targets of PKA. They are histone acetyltransferases that acetylate histone H3 lysine-27, a histone mark associated with open chromatin and increased transcription (Tie F et al. Development 2009). The translocation of CREBBP and Ep300 into the nucleus in response to vasopressin in the collecting duct cells, predicts that vasopressin, working through PKA, may increase histone H3K27 acetylation of some genes. We tested this by performing ChIP-Seq for this modification.
2018-01-02 | GSE95007 | GEO
Project description:The gene encoding the aquaporin-2 water channel is regulated transcriptionally in response to vasopressin. In the renal collecting duct, vasopressin stimulates the nuclear translocation and phosphorylation (at Ser552) of β-catenin, a multifunctional protein that can act as a transcriptional co-regulator in the nucleus. The purpose of this study was to identify β-catenin interacting proteins in nuclei of rat inner medullary collecting duct (IMCD) cells using both experimental and computational approaches. We used chromatin immunoprecipitation coupled to mass spectrometry (ChIP-MS) in nuclei isolated from rat IMCD suspensions to identify β-catenin interacting proteins. We reproducibly (n=4) identified 43 β-catenin binding proteins, which included a number of known β-catenin binding partners as well as novel interacting proteins. Multiple proteins involved in transcriptional regulation were identified (Taf1, Jup, Tdrd3, Cdh1, Cenpj, and several histones). Many of the identified β-catenin binding partners were found in prior studies to translocate to the nucleus in response to vasopressin. There was one DNA-binding transcription factor (TF), viz. Taf1, part of the RNA-polymerase II pre-initiation complex. To identify sequence-specific TFs that may interact with β-catenin but are expressed at abundance levels too low to be detected by MS, Bayes’ Theorem was used to integrate data from several information sources. The analysis identified several TFs with potential binding sites in the Aqp2 gene promoter that could interact with β-catenin in the regulation of Aqp2 gene transcription viz. Jun, Junb, Jund, Atf1, Atf2, Mef2d, Usf1, Max, Pou2f1, and Rxra. The findings provide information necessary for modeling the transcriptional response to vasopressin.
2018-10-26 | PXD005792 | Pride
Project description:Vasopressin is the major hormone that regulates renal water excretion. It does so by binding to a receptor in renal collecting duct cells, triggering signaling pathways that ultimately regulate the abundance, location, and activity of the water channel protein aquaporin 2. We took an advantage of quantitative large scale proteomic technologies and oligonucleotide microarrays to quantify steady state changes in protein and transcript abundances in response to vasopressin in a collecting duct cell line, mpkCCD clone 11 (Yu et al. PNAS 2009, 106:2441-2446). This cell line originally developed by Alan Vandewalle’s group recapitulates vasopressin-mediated AQP2 expression and phosphorylation as seen in native colleting duct cells. The mpkCCD cells were grown on membrane supports to permit polarization. Once transepithelial resistance reached 5kohm per centimeter square and higher, the cells were exposed to the vasopressin V2 receptor analog, dDAVP, at a physiological concentration, 0.1nM, for 5 days. Control experiments were done with cells exposed to vehicle alone. Total RNA was harvested and processed for transcript expression analysis using Affymetrix GeneChip Mouse Genome 430 2.0 Arrays. Each experimental treatment, vehicle and dDAVP, was repeated 3 times.
2010-12-09 | E-GEOD-19938 | biostudies-arrayexpress
Project description:Vasopressin controls water excretion by regulating the water channel protein, aquaporin 2. Vasopressin acts in the renal collecting duct by binding to a G-protein coupled receptor and activating protein kinase A (PKA). Signaling events beyond PKA are largely unknown. Ultra-deep phosphoproteomic analysis of collecting duct cells isolated from rat kidneys identified and quantified 10,738 phosphorylation sites. Vasopressin significantly altered the abundance of only 219 of these phosphorylation sites, suggesting a highly selective effect on cell signaling. The regulated sites were mapped to cellular processes shown in prior studies to be involved in aquaporin-2 regulation. The mapping and full data set was used to create an online data resource to guide future studies.
2020-05-25 | PXD011245 | Pride
Project description:Early stages of ureteral obstruction are marked by polyuria with impaired urinary concentrating ability, associated with loss of aquaporin-2 (AQP2) expression. Most mechanistic work in unilateral ureteral obstruction (UUO) models has been done at relatively late time points, making it difficult to discriminate the early effect on collecting ducts (CDs) in gene expression. Here, we use single-tubule RNA-Seq to identity signaling pathways at earlier time points after UUO in rat models.
2022-07-20 | GSE174289 | GEO
Project description:Early molecular events mediating loss of aquaporin-2 in kidney collecting duct during ureteral obstruction
| PRJNA729109 | ENA
Project description:Vasopressin, a peptide hormone, controls renal water excretion, largely through regulation of water channel aquaporin-2 (AQP2) in the renal collecting duct. There are two regulatory mechanisms of AQP2: 1) short-term regulation by membrane trafficking of AQP2; and 2) long-term regulation involving vasopressin-induced changes of protein abundance of AQP2 through regulation of gene transcription and protein half-life. Vasopressin binds a G protein-coupled receptor (V2R) activating a cyclic AMP/protein kinase A (PKA) signaling pathway. Sequentially, after activation of cAMP/PKA signaling, many of transcription factors involve gene transcription process. cAMP-response element binding protein (CREB) and cAMP-responsive transcription factor C/EBP beta are potential candidates for vaopressin-mediated regulation of Aqp2 gene transcription proviously reported. In the present study, genome-wide binding sites for two b-ZIP transcription factors CREB and C/EBP beta were identified in vasopressin-responsive mouse collecting duct mpkCCD cells using ChIP-Seq.
2018-03-26 | GSE98076 | GEO