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Journal articles on the topic 'Foxa'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

LIU, Yuanfang, Wei SHEN, Patricia L. BRUBAKER, Klaus H. KAESTNER, and Daniel J. DRUCKER. "Foxa3 (HNF-3γ) binds to and activates the rat proglucagon gene promoter but is not essential for proglucagon gene expression." Biochemical Journal 366, no. 2 (September 1, 2002): 633–41. http://dx.doi.org/10.1042/bj20020095.

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Members of the Forkhead box a (Foxa) transcription factor family are expressed in the liver, pancreatic islets and intestine and both Foxa1 and Foxa2 regulate proglucagon gene transcription. As Foxa proteins exhibit overlapping DNA-binding specificities, we examined the role of Foxa3 [hepatocyte nuclear factor (HNF)-3γ] in control of proglucagon gene expression. Foxa3 was detected by reverse transcriptase PCR in glucagon-producing cell lines and binds to the rat proglucagon gene G2 promoter element in GLUTag enteroendocrine cells. Although Foxa3 increased rat proglucagon promoter activity in BHK fibroblasts, augmentation of Foxa3 expression did not increase proglucagon promoter activity in GLUTag cells. Furthermore, adenoviral Foxa3 expression did not affect endogenous proglucagon gene expression in islet or intestinal endocrine cell lines. Although Foxa3-/- mice exhibit mild hypoglycaemia during a prolonged fast, the levels of proglucagon-derived peptides and proglucagon mRNA transcripts were comparable in tissues from wild-type and Foxa3-/- mice. These findings identify Foxa3 as a member of the proglucagon gene G2 element binding-protein family that, unlike Foxa1, is not essential for control of islet or intestinal proglucagon gene expression in vivo.

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2

Sharma, Sanjeev K., Ulrike Leinemann, Regine Ratke, Elke Oetjen, Roland Blume, Corinna Dickel, and Willhart Knepel. "Characterization of a novel Foxa (hepatocyte nuclear factor-3) site in the glucagon promoter that is conserved between rodents and humans." Biochemical Journal 389, no. 3 (July 26, 2005): 831–41. http://dx.doi.org/10.1042/bj20050334.

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The pancreatic islet hormone glucagon stimulates hepatic glucose production and thus maintains blood glucose levels in the fasting state. Transcription factors of the Foxa [Fox (forkhead box) subclass A; also known as HNF-3 (hepatocyte nuclear factor-3)] family are required for cell-specific activation of the glucagon gene in pancreatic islet α-cells. However, their action on the glucagon gene is poorly understood. In the present study, comparative sequence analysis and molecular characterization using protein–DNA binding and transient transfection assays revealed that the well-characterized Foxa-binding site in the G2 enhancer element of the rat glucagon gene is not conserved in humans and that the human G2 sequence lacks basal enhancer activity. A novel Foxa site was identified that is conserved in rats, mice and humans. It mediates activation of the glucagon gene by Foxa proteins and confers cell-specific promoter activity in glucagon-producing pancreatic islet α-cell lines. In contrast with previously identified Foxa-binding sites in the glucagon promoter, which bind nuclear Foxa2, the novel Foxa site was found to bind preferentially Foxa1 in nuclear extracts of a glucagon-producing pancreatic islet α-cell line, offering a mechanism that explains the decrease in glucagon gene expression in Foxa1-deficient mice. This site is located just upstream of the TATA box (between −30 and −50), suggesting a role for Foxa proteins in addition to direct transcriptional activation, such as a role in opening the chromatin at the start site of transcription of the glucagon gene.

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3

Yu, Xiuping, Kichiya Suzuki, Yongqing Wang, Aparna Gupta, Renjie Jin, Marie-Claire Orgebin-Crist, and Robert Matusik. "The Role of Forkhead Box A2 to Restrict Androgen-Regulated Gene Expression of Lipocalin 5 in the Mouse Epididymis." Molecular Endocrinology 20, no. 10 (October 1, 2006): 2418–31. http://dx.doi.org/10.1210/me.2006-0008.

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Abstract Murine epididymal retinoic acid-binding protein [or lipocalin 5 (Lcn5)] is synthesized and secreted by the principal cells of the mouse middle/distal caput epididymidis. A 5-kb promoter fragment of the Lcn5 gene can dictate androgen-dependent and epididymis region-specific gene expression in transgenic mice. Here, we reported that the 1.8-kb Lcn5 promoter confers epididymis region-specific gene expression in transgenic mice. To decipher the mechanism that directs transcription, 14 chimeric constructs that sequentially removed 100 bp of 1.8-kb Lcn5 promoter were generated and transfected into epididymal cells and nonepididymal cells. Transient transfection analysis revealed that 1.3 kb promoter fragment gave the strongest response to androgens. Between the 1.2-kb to 1.3-kb region, two androgen receptor (AR) binding sites were identified. Adjacent to AR binding sites, a Foxa2 [Fox (Forkhead box) subclass A] binding site was confirmed by gel shift assay. Similar Foxa binding sites were also found on the promoters of human and rat Lcn5, indicating the Foxa binding site is conserved among species. We previously reported that among the three members of Foxa family, Foxa1 and Foxa3 were absent in the epididymis whereas Foxa2 was detected in epididymal principal cells. Here, we report that Foxa2 displays a region-specific expression pattern along the epididymis: no staining observed in initial segment, light staining in proximal caput, gradiently heavier staining in middle and distal caput, and strongest staining in corpus and cauda, regions with little or no expression of Lcn5. In transient transfection experiments, Foxa2 expression inhibits AR induction of the Lcn5 promoter, which is consistent with the lack of expression of Lcn5 in the corpus and cauda. We conclude that Foxa2 functions as a repressor that restricts AR regulation of Lcn5 to a segment-specific pattern in the epididymis.

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4

Bach, Duc-Hiep, Nguyen Long, Thi-Thu-Trang Luu, Nguyen Anh, Sung Kwon, and Sang Lee. "The Dominant Role of Forkhead Box Proteins in Cancer." International Journal of Molecular Sciences 19, no. 10 (October 22, 2018): 3279. http://dx.doi.org/10.3390/ijms19103279.

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Forkhead box (FOX) proteins are multifaceted transcription factors that are significantly implicated in cancer, with various critical roles in biological processes. Herein, we provide an overview of several key members of the FOXA, FOXC, FOXM1, FOXO and FOXP subfamilies. Important pathophysiological processes of FOX transcription factors at multiple levels in a context-dependent manner are discussed. We also specifically summarize some major aspects of FOX transcription factors in association with cancer research such as drug resistance, tumor growth, genomic alterations or drivers of initiation. Finally, we suggest that targeting FOX proteins may be a potential therapeutic strategy to combat cancer.

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5

Gosalia, Nehal, Rui Yang, Jenny L. Kerschner, and Ann Harris. "FOXA2 regulates a network of genes involved in critical functions of human intestinal epithelial cells." Physiological Genomics 47, no. 7 (July 2015): 290–97. http://dx.doi.org/10.1152/physiolgenomics.00024.2015.

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The forkhead box A (FOXA) family of pioneer transcription factors is critical for the development of many endoderm-derived tissues. Their importance in regulating biological processes in the lung and liver is extensively characterized, though much less is known about their role in intestine. Here we investigate the contribution of FOXA2 to coordinating intestinal epithelial cell function using postconfluent Caco2 cells, differentiated into an enterocyte-like model. FOXA2 binding sites genome-wide were determined by ChIP-seq and direct targets of the factor were validated by ChIP-qPCR and siRNA-mediated depletion of FOXA1/2 followed by RT-qPCR. Peaks of FOXA2 occupancy were frequent at loci contributing to gene ontology pathways of regulation of cell migration, cell motion, and plasma membrane function. Depletion of both FOXA1 and FOXA2 led to a significant reduction in the expression of multiple transmembrane proteins including ion channels and transporters, which form a network that is essential for maintaining normal ion and solute transport. One of the targets was the adenosine A2B receptor, and reduced receptor mRNA levels were associated with a functional decrease in intracellular cyclic AMP. We also observed that 30% of FOXA2 binding sites contained a GATA motif and that FOXA1/A2 depletion reduced GATA-4, but not GATA-6 protein levels. These data show that FOXA2 plays a pivotal role in regulating intestinal epithelial cell function. Moreover, that the FOXA and GATA families of transcription factors may work cooperatively to regulate gene expression genome-wide in the intestinal epithelium.

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6

Kohler, Sarah, and Lisa Ann Cirillo. "Stable Chromatin Binding Prevents FoxA Acetylation, Preserving FoxA Chromatin Remodeling." Journal of Biological Chemistry 285, no. 1 (November 5, 2009): 464–72. http://dx.doi.org/10.1074/jbc.m109.063149.

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7

Kanamoto, Naotetsu, Tetsuya Tagami, Yoriko Ueda-Sakane, Masakatsu Sone, Masako Miura, Akihiro Yasoda, Naohisa Tamura, Hiroshi Arai, and Kazuwa Nakao. "Forkhead Box A1 (FOXA1) and A2 (FOXA2) Oppositely Regulate Human Type 1 Iodothyronine Deiodinase Gene in Liver." Endocrinology 153, no. 1 (January 1, 2012): 492–500. http://dx.doi.org/10.1210/en.2011-1310.

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Type 1 iodothyronine deiodinase (D1), a selenoenzyme that catalyzes the bioactivation of thyroid hormone, is expressed mainly in the liver. Its expression and activity are modulated by several factors, but the precise mechanism of its transcriptional regulation remains unclear. In the present study, we have analyzed the promoter of human D1 gene (hDIO1) to identify factors that prevalently increase D1 activity in the human liver. Deletion and mutation analyses demonstrated that a forkhead box (FOX)A binding site and an E-box site within the region between nucleotides −187 and −132 are important for hDIO1 promoter activity in the liver. EMSA demonstrated that FOXA1 and FOXA2 specifically bind to the FOXA binding site and that upstream stimulatory factor (USF) specifically binds to the E-box element. Overexpression of FOXA2 decreased hDIO1 promoter activity, and short interfering RNA-mediated knockdown of FOXA2 increased the expression of hDIO1 mRNA. In contrast, overexpression of USF1/2 increased hDIO1 promoter activity. Short interfering RNA-mediated knockdown of FOXA1 decreased the expression of hDIO1 mRNA, but knockdown of both FOXA1 and FOXA2 restored it. The response of the hDIO1 promoter to USF was greatly attenuated in the absence of FOXA1. Taken together, these results indicate that a balance of FOXA1 and FOXA2 expression modulates hDIO1 expression in the liver.

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8

Long, Lingyun, and Brett T. Spear. "FoxA Proteins Regulate H19 Endoderm Enhancer E1 and Exhibit Developmental Changes in Enhancer Binding In Vivo." Molecular and Cellular Biology 24, no. 21 (November 1, 2004): 9601–9. http://dx.doi.org/10.1128/mcb.24.21.9601-9609.2004.

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ABSTRACT Multiple enhancers govern developmental and tissue-specific expression of the H19-Igf2 locus, but factors that bind these elements have not been identified. Using chromatin immunoprecipitation, we have found two FoxA binding sites in the H19 E1 enhancer. Mutating these sites diminishes E1 activity in hepatoma cells. Additional chromatin immunoprecipitations show that FoxA binds to E1 in fetal liver, where H19 is abundantly expressed, but that binding decreases in adult liver, where H19 is no longer transcribed, even though FoxA proteins are present at both times. FoxA proteins are induced when F9 embryonal carcinoma cells differentiate into visceral endoderm (VE) and parietal endoderm (PE). We show that FoxA binds E1 in VE cells, where H19 is expressed, but not in PE cells, where H19 is silent. This correlation between FoxA binding and H19 expression indicates a role for FoxA in regulating H19, including developmental activation in the yolk sac and liver and postnatal repression in the liver. This is the first demonstration of a tissue-specific factor involved in developmental control of H19 expression. These data also indicate that the presence of FoxA proteins is not sufficient for binding but that additional mechanisms must govern the accessibility of FoxA proteins to their cognate binding sites within the H19 E1 enhancer.

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9

Thanan, Raynoo, Waleeporn Kaewlert, Chadamas Sakonsinsiri, Timpika Chaiprasert, Napat Armartmuntree, Duangkamon Muengsaen, Anchalee Techasen, et al. "Opposing Roles of FoxA1 and FoxA3 in Intrahepatic Cholangiocarcinoma Progression." International Journal of Molecular Sciences 21, no. 5 (March 5, 2020): 1796. http://dx.doi.org/10.3390/ijms21051796.

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Cholangiocarcinoma (CCA), a malignancy of biliary epithelium, is related to liver stem cell deregulation. FoxAs are a group of transcription factors that play critical roles in liver stem cell differentiation. In this study, the expression levels of FoxAs (i.e., FoxA1, FoxA2 and FoxA3) were detected in intrahepatic CCA tissues and the functions of FoxAs were studied in CCA cell lines. FoxA1 and FoxA2 were mainly localized in the nuclei of normal bile duct (NBD) cells and some of the cancer cells. Low expression of FoxA1 in CCA tissues (72%) was significantly correlated with poor prognosis. FoxA3 expression of CCA cells was localized in the nucleus and cytoplasm, whereas it was slightly detected in NBDs. High expression of FoxA3 in cancer tissues (61%) was significantly related to high metastasis status. These findings suggest the opposing roles of FoxA1 and FoxA3 in CCA. Moreover, the FoxA1-over-expressing CCA cell line exhibited a significant reduction in proliferative and invasive activities compared to control cells. Knockdown of FoxA3 in CCA cells resulted in a significant decrease in proliferative and invasive activities compared with control cells. Taken together, in CCA, FoxA1 is down-regulated and has tumor suppressive roles, whereas FoxA3 is up-regulated and has oncogenic roles.

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10

Rausa, Francisco M., Yongjun Tan, and Robert H. Costa. "Association between Hepatocyte Nuclear Factor 6 (HNF-6) and FoxA2 DNA Binding Domains Stimulates FoxA2 Transcriptional Activity but Inhibits HNF-6 DNA Binding." Molecular and Cellular Biology 23, no. 2 (January 15, 2003): 437–49. http://dx.doi.org/10.1128/mcb.23.2.437-449.2003.

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ABSTRACT In previous studies we used transgenic mice or recombinant adenovirus infection to increase hepatic expression of forkhead box A2 (FoxA2, previously called hepatocyte nuclear factor 3β [HNF-3β]), which caused diminished hepatocyte glycogen levels and reduced expression of glucose homeostasis genes. Because this diminished expression of FoxA2 target genes was associated with reduced levels of the Cut-Homeodomain HNF-6 transcription factor, we conducted the present study to determine whether there is a functional interaction between HNF-6 and FoxA2. Human hepatoma (HepG2) cotransfection assays demonstrated that HNF-6 synergistically stimulated FoxA2 but not FoxA1 or FoxA3 transcriptional activity, and protein-binding assays showed that this protein interaction required the HNF-6 Cut-Homeodomain and FoxA2 winged-helix DNA binding domains. Furthermore, we show that the HNF-6 Cut-Homeodomain sequences were sufficient to synergistically stimulate FoxA2 transcriptional activation by recruiting the p300/CBP coactivator proteins. This was supported by the fact that FoxA2 transcriptional synergy with HNF-6 was dependent on retention of the HNF-6 Cut domain LXXLL sequence, which mediated recruitment of the p300/CBP proteins. Moreover, cotransfection and DNA binding assays demonstrated that increased FoxA2 levels caused a decrease in HNF-6 transcriptional activation of the glucose transporter 2 (Glut-2) promoter by interfering with the binding of HNF-6 to its target DNA sequence. These data suggest that at a FoxA-specific site, HNF-6 serves as a coactivator protein to enhance FoxA2 transcription, whereas at an HNF-6-specific site, FoxA2 represses HNF-6 transcription by inhibiting HNF-6 DNA binding activity. This is the first reported example of a liver-enriched transcription factor (HNF-6) functioning as a coactivator protein to potentiate the transcriptional activity of another liver factor, FoxA2.

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11

Kingsley, Robert A., Rolf Reissbrodt, Wolfgang Rabsch, Julian M. Ketley, Renée M. Tsolis, Paul Everest, Gordon Dougan, Andreas J. Bäumler, Mark Roberts, and Peter H. Williams. "Ferrioxamine-Mediated Iron(III) Utilization bySalmonella enterica." Applied and Environmental Microbiology 65, no. 4 (April 1, 1999): 1610–18. http://dx.doi.org/10.1128/aem.65.4.1610-1618.1999.

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ABSTRACT Utilization of ferrioxamines as sole sources of iron distinguishesSalmonella enterica serotypes Typhimurium and Enteritidis from a number of related species, including Escherichia coli. Ferrioxamine supplements have therefore been used in preenrichment and selection media to increase the bacterial growth rate while selectivity is maintained. We characterized the determinants involved in utilization of ferrioxamines B, E, and G by S. enterica serotype Typhimurium by performing siderophore cross-feeding bioassays. Transport of all three ferric siderophores across the outer membrane was dependent on the FoxA receptor encoded by the Fur-repressible foxA gene. However, only the transport of ferrioxamine G was dependent on the energy-transducing protein TonB, since growth stimulation of a tonB strain by ferrioxamines B and E was observed, albeit at lower efficiencies than in the parental strain. Transport across the inner membrane was dependent on the periplasmic binding protein-dependent ABC transporter complex comprising FhuBCD, as has been reported for other hydroxamate siderophores of enteric bacteria. The distribution of thefoxA gene in the genus Salmonella, as indicated by DNA hybridization studies and correlated with the ability to utilize ferrioxamine E, was restricted to subspecies I, II, and IIIb, and this gene was absent from subspecies IIIa, IV, VI, and VII (formerly subspecies IV) and Salmonella bongori (formerly subspecies V). S. enterica serotype Typhimurium mutants with either a transposon insertion or a defined nonpolar frameshift (+2) mutation in the foxA gene were not able to utilize any of the three ferrioxamines tested. A strain carrying the nonpolar foxAmutation exhibited a significantly reduced ability to colonize rabbit ileal loops compared to the foxA + parent. In addition, a foxA mutant was markedly attenuated in mice inoculated by either the intragastric or intravenous route. Mice inoculated with the foxA mutant were protected against subsequent challenge by the foxA + parent strain.

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12

Kaestner, Klaus H. "The FoxA factors in organogenesis and differentiation." Current Opinion in Genetics & Development 20, no. 5 (October 2010): 527–32. http://dx.doi.org/10.1016/j.gde.2010.06.005.

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13

Maier, Jennifer, and Brian Harfe. "The Foxa family and intervertebral disk formation." Developmental Biology 344, no. 1 (August 2010): 458. http://dx.doi.org/10.1016/j.ydbio.2010.05.185.

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14

Maier, Jennifer, and Brian Harfe. "Foxa transcription factors and the intervertebral disk." Developmental Biology 331, no. 2 (July 2009): 528–29. http://dx.doi.org/10.1016/j.ydbio.2009.05.529.

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15

SCHONEVELD, Onard J. L. M., Ingrid C. GAEMERS, Atze T. DAS, Maarten HOOGENKAMP, Johan RENES, Jan M. RUIJTER, and Wouter H. LAMERS. "Structural requirements of the glucocorticoid-response unit of the carbamoyl-phosphate synthase gene." Biochemical Journal 382, no. 2 (August 24, 2004): 463–70. http://dx.doi.org/10.1042/bj20040471.

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The GRU (glucocorticoid-response unit) within the distal enhancer of the gene encoding carbamoyl-phosphate synthase, which comprises REs (response elements) for the GR (glucocorticoid receptor) and the liver-enriched transcription factors FoxA (forkhead box A) and C/EBP (CCAAT/enhancer-binding protein), and a binding site for an unknown protein denoted P3, is one of the simplest GRUs described. In this study, we have established that the activity of this GRU depends strongly on the positioning and spacing of its REs. Mutation of the P3 site within the 25 bp FoxA–GR spacer eliminated GRU activity, but the requirement for P3 could be overcome by decreasing the length of this spacer to ≤12 bp, by optimizing the sequence of the REs in the GRU, and by replacing the P3 sequence with a C/EBPβ sequence. With spacers of ≤12 bp, the activity of the GRU depended on the helical orientation of the FoxA and GR REs, with highest activities observed at 2 and 12 bp respectively. Elimination of the 6 bp C/EBP–FoxA spacer also increased GRU activity 2-fold. Together, these results indicate that the spatial positioning of the transcription factors that bind to the GRU determines its activity and that the P3 complex, which binds to the DNA via a 75 kDa protein, functions to facilitate interaction between the FoxA and glucocorticoid response elements when the distance between these transcription factors means that they have difficulties contacting each other.

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Wang, Li-Li, Yin-Ling Xiu, Xi Chen, Kai-Xuan Sun, Shuo Chen, Dan-Dan Wu, Bo-Liang Liu, and Yang Zhao. "The transcription factor FOXA1 induces epithelial ovarian cancer tumorigenesis and progression." Tumor Biology 39, no. 5 (May 2017): 101042831770621. http://dx.doi.org/10.1177/1010428317706210.

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FOXA1 (forkhead box A1), a member of the FOXA transcription factor superfamily, plays an important role in tumor occurrence and development. However, the relationship between FOXA1 and ovarian cancer has not been reported. We examined normal ovarian tissue and ovarian cancer tissue and found increased FOXA1 expression in the cancer tissue. 3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide and flow cytometry assays demonstrated that transfection with small interfering RNA to silence FOXA1 (si-FOXA1) in ovarian cancer cell lines decreased cell proliferation and induced apoptosis and S-phase arrest. In addition, si-FOXA1 transfection inhibited cell migration and invasion. Western blotting showed that si-FOXA1 transfection decreased the levels of YY1-associated protein 1, cyclin-dependent kinase 1, cyclin D1, phosphatidylinositol-3 kinase, E2F transcription factor 1, B-cell lymphoma 2, and vascular endothelial growth factor A protein. Based on these results, we suggest that FOXA1 plays a catalytic role in ovarian cancer pathogenesis and development by affecting the expression of the above-mentioned proteins.

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Mirosevich, Janni, Nan Gao, Aparna Gupta, Scott B. Shappell, Richard Jove, and Robert J. Matusik. "Expression and role of Foxa proteins in prostate cancer." Prostate 66, no. 10 (July 1, 2006): 1013–28. http://dx.doi.org/10.1002/pros.20299.

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18

Wolfrum, Christian, David Q. Shih, Satoru Kuwajima, Andrew W. Norris, C. Ronald Kahn, and Markus Stoffel. "Role of Foxa-2 in adipocyte metabolism and differentiation." Journal of Clinical Investigation 112, no. 3 (August 1, 2003): 345–56. http://dx.doi.org/10.1172/jci18698.

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19

Von Stetina, Stephen E., Jennifer Liang, Georgios Marnellos, and Susan E. Mango. "Temporal regulation of epithelium formation mediated by FoxA, MKLP1, MgcRacGAP, and PAR-6." Molecular Biology of the Cell 28, no. 15 (July 15, 2017): 2042–65. http://dx.doi.org/10.1091/mbc.e16-09-0644.

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To establish the animal body plan, embryos link the external epidermis to the internal digestive tract. In Caenorhabditis elegans, this linkage is achieved by the arcade cells, which form an epithelial bridge between the foregut and epidermis, but little is known about how development of these three epithelia is coordinated temporally. The arcade cell epithelium is generated after the epidermis and digestive tract epithelia have matured, ensuring that both organs can withstand the mechanical stress of embryo elongation; mistiming of epithelium formation leads to defects in morphogenesis. Using a combination of genetic, bioinformatic, and imaging approaches, we find that temporal regulation of the arcade cell epithelium is mediated by the pioneer transcription factor and master regulator PHA-4/FoxA, followed by the cytoskeletal regulator and kinesin ZEN-4/MKLP1 and the polarity protein PAR-6. We show that PHA-4 directly activates mRNA expression of a broad cohort of epithelial genes, including junctional factor dlg-1. Accumulation of DLG-1 protein is delayed by ZEN-4, acting in concert with its binding partner CYK-4/MgcRacGAP. Our structure–function analysis suggests that nuclear and kinesin functions are dispensable, whereas binding to CYK-4 is essential, for ZEN-4 function in polarity. Finally, PAR-6 is necessary to localize polarity proteins such as DLG-1 within adherens junctions and at the apical surface, thereby generating arcade cell polarity. Our results reveal that the timing of a landmark event during embryonic morphogenesis is mediated by the concerted action of four proteins that delay the formation of an epithelial bridge until the appropriate time. In addition, we find that mammalian FoxA associates with many epithelial genes, suggesting that direct regulation of epithelial identity may be a conserved feature of FoxA factors and a contributor to FoxA function in development and cancer.

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Le lay, John, and Klaus H. Kaestner. "The Fox Genes in the Liver: From Organogenesis to Functional Integration." Physiological Reviews 90, no. 1 (January 2010): 1–22. http://dx.doi.org/10.1152/physrev.00018.2009.

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Formation and function of the liver are highly controlled, essential processes. Multiple signaling pathways and transcriptional regulatory networks cooperate in this complex system. The evolutionarily conserved FOX, for Forkhead bOX, class of transcriptional regulators is critical to many aspects of liver development and function. The FOX proteins are small, mostly monomeric DNA binding factors containing the so-called winged helix DNA binding motif that distinguishes them from other classes of transcription factors. We discuss the biochemical and genetic roles of Foxa, Foxl1, Foxm1, and Foxo, as these have been shown to regulate many processes throughout the life of the organ, controlling both formation and function of the liver.

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Hirai, Hiroyuki, Tetsuya Tani, and Nobuaki Kikyo. "Structure and functions of powerful transactivators: VP16, MyoD and FoxA." International Journal of Developmental Biology 54, no. 11-12 (2010): 1589–96. http://dx.doi.org/10.1387/ijdb.103194hh.

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22

Friedman, J. R., and K. H. Kaestner. "The Foxa family of transcription factors in development and metabolism." Cellular and Molecular Life Sciences 63, no. 19-20 (August 11, 2006): 2317–28. http://dx.doi.org/10.1007/s00018-006-6095-6.

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23

Lubbers, R. J. M., A. Dilokpimol, J. Visser, and R. P. de Vries. "Aspergillus niger uses the peroxisomal CoA-dependent β-oxidative genes to degrade the hydroxycinnamic acids caffeic acid, ferulic acid, and p-coumaric acid." Applied Microbiology and Biotechnology 105, no. 10 (May 2021): 4199–211. http://dx.doi.org/10.1007/s00253-021-11311-0.

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Abstract Aromatic compounds are important molecules which are widely applied in many industries and are mainly produced from nonrenewable sources. Renewable sources such as plant biomass are interesting alternatives for the production of aromatic compounds. Ferulic acid and p-coumaric acid, a precursor for vanillin and p-vinyl phenol, respectively, can be released from plant biomass by the fungus Aspergillus niger. The degradation of hydroxycinnamic acids such as caffeic acid, ferulic acid, and p-coumaric acid has been observed in many fungi. In A. niger, multiple metabolic pathways were suggested for the degradation of hydroxycinnamic acids. However, no genes were identified for these hydroxycinnamic acid metabolic pathways. In this study, several pathway genes were identified using whole-genome transcriptomic data of A. niger grown on different hydroxycinnamic acids. The genes are involved in the CoA-dependent β-oxidative pathway in fungi. This pathway is well known for the degradation of fatty acids, but not for hydroxycinnamic acids. However, in plants, it has been shown that hydroxycinnamic acids are degraded through this pathway. We identified genes encoding hydroxycinnamate-CoA synthase (hcsA), multifunctional β-oxidation hydratase/dehydrogenase (foxA), 3-ketoacyl CoA thiolase (katA), and four thioesterases (theA-D) of A. niger, which were highly induced by all three tested hydroxycinnamic acids. Deletion mutants revealed that these genes were indeed involved in the degradation of several hydroxycinnamic acids. In addition, foxA and theB are also involved in the degradation of fatty acids. HcsA, FoxA, and KatA contained a peroxisomal targeting signal and are therefore predicted to be localized in peroxisomes. Key points • Metabolism of hydroxycinnamic acid was investigated in Aspergillus niger • Using transcriptome data, multiple CoA-dependent β-oxidative genes were identified. • Both foxA and theB are involved in hydroxycinnamate but also fatty acid metabolism.

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24

Fox, Danny. "Individual concepts and narrow scope illusions." Snippets, no. 37 (December 2019): 30–32. http://dx.doi.org/10.7358/snip-2019-037-foxa.

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25

de-Leon, Smadar Ben-Tabou, and Eric H. Davidson. "The endoderm specification, a view from the foxa cis-regulatory modules." Developmental Biology 331, no. 2 (July 2009): 435. http://dx.doi.org/10.1016/j.ydbio.2009.05.178.

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26

Zhao, Yongbing, and Zhaoyu Li. "Interplay of estrogen receptors and FOXA factors in the liver cancer." Molecular and Cellular Endocrinology 418 (December 2015): 334–39. http://dx.doi.org/10.1016/j.mce.2015.01.043.

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27

Báumler, Andreas J., and Klaus Hantke. "Ferrioxamine uptake in Yersinia enterocolitica: characterization of the receptor protein FoxA." Molecular Microbiology 6, no. 10 (May 1992): 1309–21. http://dx.doi.org/10.1111/j.1365-2958.1992.tb00852.x.

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28

Kaestner, Klaus H. "The Hepatocyte Nuclear Factor 3 (HNF3 or FOXA) Family in Metabolism." Trends in Endocrinology & Metabolism 11, no. 7 (September 2000): 281–85. http://dx.doi.org/10.1016/s1043-2760(00)00271-x.

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29

Lee, Catherine S., Joshua R. Friedman, James T. Fulmer, and Klaus H. Kaestner. "The initiation of liver development is dependent on Foxa transcription factors." Nature 435, no. 7044 (June 2005): 944–47. http://dx.doi.org/10.1038/nature03649.

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30

Panowski, Siler H., Suzanne Wolff, Hugo Aguilaniu, Jenni Durieux, and Andrew Dillin. "PHA-4/Foxa mediates diet-restriction-induced longevity of C. elegans." Nature 447, no. 7144 (May 2007): 550–55. http://dx.doi.org/10.1038/nature05837.

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31

Kornreich-Leshem, Hagit, Carmit Ziv, Elzbieta Gumienna-Kontecka, Rina Arad-Yellin, Yona Chen, Mourad Elhabiri, Anne-Marie Albrecht-Gary, Yitzhak Hadar, and Abraham Shanzer. "Ferrioxamine B Analogues: Targeting the FoxA Uptake System in the PathogenicYersiniaenterocolitica." Journal of the American Chemical Society 127, no. 4 (February 2005): 1137–45. http://dx.doi.org/10.1021/ja035182m.

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32

Gaudet, J. "Regulation of Organogenesis by the Caenorhabditis elegans FoxA Protein PHA-4." Science 295, no. 5556 (February 1, 2002): 821–25. http://dx.doi.org/10.1126/science.1065175.

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33

Reizel, Yitzhak, Ashleigh Morgan, Long Gao, Jonathan Schug, Sarmistha Mukherjee, Meilín Fernández García, Greg Donahue, Joseph A. Baur, Kenneth S. Zaret, and Klaus H. Kaestner. "FoxA-dependent demethylation of DNA initiates epigenetic memory of cellular identity." Developmental Cell 56, no. 5 (March 2021): 602–12. http://dx.doi.org/10.1016/j.devcel.2021.02.005.

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34

Minoo, Parviz, Lingyan Hu, Yiming Xing, Nian Ling Zhu, Hongyan Chen, Min Li, Zea Borok, and Changgong Li. "Physical and Functional Interactions between Homeodomain NKX2.1 and Winged Helix/Forkhead FOXA1 in Lung Epithelial Cells." Molecular and Cellular Biology 27, no. 6 (January 12, 2007): 2155–65. http://dx.doi.org/10.1128/mcb.01133-06.

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ABSTRACT NKX2.1 is a homeodomain transcription factor that controls development of the brain, lung, and thyroid. In the lung, Nkx2.1 is expressed in a proximo-distal gradient and activates specific genes in phenotypically distinct epithelial cells located along this axis. The mechanisms by which NKX2.1 controls its target genes may involve interactions with other transcription factors. We examined whether NKX2.1 interacts with members of the winged-helix/forkhead family of FOXA transcription factors to regulate two spatially and cell type-specific genes, SpC and Ccsp. The results show that NKX2.1 interacts physically and functionally with FOXA1. The nature of the interaction is inhibitory and occurs through the NKX2.1 homeodomain in a DNA-independent manner. On SpC, which lacks a FOXA1 binding site, FOXA1 attenuates NKX2.1-dependent transcription. Inhibition of FOXA1 by small interfering RNA increased SpC mRNA, demonstrating the in vivo relevance of this finding. In contrast, FOXA1 and NKX2.1 additively activate transcription from Ccsp, which includes both NKX2.1 and FOXA1 binding sites. In electrophoretic mobility shift assays, the GST-FOXA1 fusion protein interferes with the formation of NKX2.1 transcriptional complexes by potentially masking the latter's homeodomain DNA binding function. These findings suggest a novel mode of selective gene regulation by proximo-distal gradient distribution of and functional interactions between forkhead and homeodomain transcription factors.

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35

Dal-Pra, Sophie, Christine Thisse, and Bernard Thisse. "FoxA transcription factors are essential for the development of dorsal axial structures." Developmental Biology 350, no. 2 (February 2011): 484–95. http://dx.doi.org/10.1016/j.ydbio.2010.12.018.

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36

Koinuma, Satoshi, Yoshihiko Umesono, Kenji Watanabe, and Kiyokazu Agata. "Planaria FoxA (HNF3) homologue is specifically expressed in the pharynx-forming cells." Gene 259, no. 1-2 (December 2000): 171–76. http://dx.doi.org/10.1016/s0378-1119(00)00426-1.

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37

Liu, Y., and M. Lehmann. "Genes and biological processes controlled by the Drosophila FOXA orthologue Fork head." Insect Molecular Biology 17, no. 2 (April 2008): 91–101. http://dx.doi.org/10.1111/j.1365-2583.2007.00785.x.

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38

Mirosevich, Janni, Nan Gao, and Robert J. Matusik. "Expression of Foxa transcription factors in the developing and adult murine prostate." Prostate 62, no. 4 (July 23, 2004): 339–52. http://dx.doi.org/10.1002/pros.20131.

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39

Huang, Ying, Xin Wang, Zhigang Cui, Yuhuan Yang, Yuchun Xiao, Liuying Tang, Biao Kan, Jianguo Xu, and Huaiqi Jing. "Possible use of ail and foxA polymorphisms for detecting pathogenic Yersinia enterocolitica." BMC Microbiology 10, no. 1 (2010): 211. http://dx.doi.org/10.1186/1471-2180-10-211.

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40

Ao, W. "Environmentally Induced Foregut Remodeling by PHA-4/FoxA and DAF-12/NHR." Science 305, no. 5691 (September 17, 2004): 1743–46. http://dx.doi.org/10.1126/science.1102216.

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41

Bryzgalov, L. O., N. I. Ershov, D. Yu Oshchepkov, V. I. Kaledin, and T. I. Merkulova. "Detection of target genes of FOXA transcription factors involved in proliferation control." Biochemistry (Moscow) 73, no. 1 (January 2008): 70–75. http://dx.doi.org/10.1134/s0006297908010100.

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42

Ionescu, Andreia, Elena Kozhemyakina, Claudia Nicolae, Klaus H. Kaestner, Bjorn R. Olsen, and Andrew B. Lassar. "FoxA Family Members Are Crucial Regulators of the Hypertrophic Chondrocyte Differentiation Program." Developmental Cell 22, no. 5 (May 2012): 927–39. http://dx.doi.org/10.1016/j.devcel.2012.03.011.

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43

Iacobazzi, Vito, Vittoria Infantino, Faustino Bisaccia, Alessandra Castegna, and Ferdinando Palmieri. "Role of FOXA in mitochondrial citrate carrier gene expression and insulin secretion." Biochemical and Biophysical Research Communications 385, no. 2 (July 2009): 220–24. http://dx.doi.org/10.1016/j.bbrc.2009.05.030.

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44

Prokai, D., A. Moehlman, K. Chapman, J. Chaudhary, A. Pudasaini, and F. Hamra. "Pioneering roles for FOXA transcription factors in rat stem and progenitor spermatogonia." Fertility and Sterility 110, no. 4 (September 2018): e307. http://dx.doi.org/10.1016/j.fertnstert.2018.07.865.

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45

Pochareddy, Sirisha, and Howard J. Edenberg. "Identification of a FOXA-dependent enhancer of human alcohol dehydrogenase 4 (ADH4)." Gene 460, no. 1-2 (July 2010): 1–7. http://dx.doi.org/10.1016/j.gene.2010.03.013.

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46

Holmfeldt, Per, Miguel Ganuza, Himangi Marathe, Bing He, Trent Hall, Guolian Kang, Joseph Moen, et al. "Functional screen identifies regulators of murine hematopoietic stem cell repopulation." Journal of Experimental Medicine 213, no. 3 (February 15, 2016): 433–49. http://dx.doi.org/10.1084/jem.20150806.

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Understanding the molecular regulation of hematopoietic stem and progenitor cell (HSPC) engraftment is paramount to improving transplant outcomes. To discover novel regulators of HSPC repopulation, we transplanted >1,300 mice with shRNA-transduced HSPCs within 24 h of isolation and transduction to focus on detecting genes regulating repopulation. We identified 17 regulators of HSPC repopulation: Arhgef5, Armcx1, Cadps2, Crispld1, Emcn, Foxa3, Fstl1, Glis2, Gprasp2, Gpr56, Myct1, Nbea, P2ry14, Smarca2, Sox4, Stat4, and Zfp521. Knockdown of each of these genes yielded a loss of function, except in the cases of Armcx1 and Gprasp2, whose loss enhanced hematopoietic stem cell (HSC) repopulation. The discovery of multiple genes regulating vesicular trafficking, cell surface receptor turnover, and secretion of extracellular matrix components suggests active cross talk between HSCs and the niche and that HSCs may actively condition the niche to promote engraftment. We validated that Foxa3 is required for HSC repopulating activity, as Foxa3−/− HSC fails to repopulate ablated hosts efficiently, implicating for the first time Foxa genes as regulators of HSPCs. We further show that Foxa3 likely regulates the HSC response to hematologic stress. Each gene discovered here offers a window into the novel processes that regulate stable HSPC engraftment into an ablated host.

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Pandit, Awadhesh, Vaibhav Jain, Neeraj Kumar, and Arnab Mukhopadhyay. "PHA-4/FOXA-regulated microRNA feed forward loops during Caenorhabditis elegans dietary restriction." Aging 6, no. 10 (October 31, 2014): 835–51. http://dx.doi.org/10.18632/aging.100697.

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48

Reizel, Yitzhak, Ashleigh Morgan, Long Gao, Yemin Lan, Elisabetta Manduchi, Eric L. Waite, Amber W. Wang, Andrew Wells, and Klaus H. Kaestner. "Collapse of the hepatic gene regulatory network in the absence of FoxA factors." Genes & Development 34, no. 15-16 (June 19, 2020): 1039–50. http://dx.doi.org/10.1101/gad.337691.120.

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49

Heslop, James A., and Stephen A. Duncan. "FoxA factors: the chromatin key and doorstop essential for liver development and function." Genes & Development 34, no. 15-16 (August 1, 2020): 1003–4. http://dx.doi.org/10.1101/gad.340570.120.

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50

Updike, Dustin L., and Susan E. Mango. "Temporal Regulation of Foregut Development by HTZ-1/H2A.Z and PHA-4/FoxA." PLoS Genetics 2, no. 9 (September 29, 2006): e161. http://dx.doi.org/10.1371/journal.pgen.0020161.

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