WW Domain Binding Protein-2, an E6-Associated Protein Interacting Protein, Acts as a Coactivator of Estrogen and Progesterone Receptors

Dhananjayan, Sarath C.; Ramamoorthy, Sivapriya; Khan, Obaid Yusuf; Ismail, Azman; Sun, Jun; Slingerland, Joyce M.; O’Malley, Bert W.; Nawaz, Zafar

doi:10.1210/me.2005-0533

Cited by 73 publications

(100 citation statements)

References 40 publications

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“…25,26 These findings suggest that WBP2 assembles into a transcriptional co-activator complex with YAP/Yki that influences the activity of cognate transcription factors. An alternate possibility is that WBP2 promotes YAP/Yki activity by interfering with SWH pathway-mediated repression of YAP/Yki.…”

Section: Resultsmentioning

confidence: 91%

“…Previously, WBP2 was found to cooperate with YAP to promote ligand-dependent transactivation potential of progesterone and oestrogen receptors. 26 Given that Wbp2 interacts with WW domains of Yki, which are required to promote Yki-dependent gene transcription and tissue growth, we hypothesised that Wbp2 would promote Yki's ability to activate transcription factors. To test this hypothesis, initially we determined whether Wbp2 could activate Yki in two independent luciferase-based transcription assays.…”

Section: Resultsmentioning

confidence: 99%

“…22,23 One such candidate protein was Wbp2, which was previously shown to bind the WW domains of YAP and influence its ability to promote transcription. 25,26 We found that Wbp2 enhances Yki's intrinsic transcriptional co-activator activity and that the ability of Wbp2 to bind and activate Yki was dependent on Yki's WW domains and Wbp2's PY motifs (Figures 2 and 3). Thus, these data are consistent with previous observations that defined a key positive regulatory role of the WW domains of Yki.…”

Section: Discussionmentioning

confidence: 95%

“…Interestingly, WBP2 was one of the first identified YAP-interacting proteins 25 and was previously shown to cooperate with YAP to increase ligand-dependent transactivation of oestrogen and progesterone receptors. 26 However, WBP2 function has never before been investigated in vivo. In this study, we show that the D. melanogaster Wbp2 homologue, CG11009, binds to Yki in a WW domain-and PY motif-dependent manner and can potentiate Yki's transcriptional co-activator function.…”

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confidence: 99%

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Wbp2 cooperates with Yorkie to drive tissue growth downstream of the Salvador–Warts–Hippo pathway

et al. 2011

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The Salvador-Warts-Hippo (SWH) pathway is a key controller of tissue growth in both flies and mammals, and deregulation of pathway activity contributes to tumour formation. The SWH pathway regulates cell growth, proliferation and apoptosis by restricting activity of the Yorkie transcriptional co-activator protein. The proteins that function together with Yorkie to drive transcription and tissue growth are beginning to be revealed and include the Scalloped (Sd), Teashirt (Tsh) and Homothorax (Hth) transcription factors. In this study, we define Wbp2 as a promoter of Yorkie-dependent growth of Drosophila melanogaster tissues. Mammalian WBP2 was previously identified as a protein that interacts with the mammalian Yorkie homologue, Yes-associated protein. WBP2 has been shown to enhance steroid hormone-dependent transcription in cultured cells but its in vivo function has remained obscure. We show that D. melanogaster Wbp2 interacts with Yorkie in a WW domain-and PY motif-dependent manner and that Wbp2 can enhance Yorkie's transcriptional co-activator properties. In vivo, Wbp2 is required for growth of the D. melanogaster wing, and reduction of Wbp2 expression suppresses overgrowth of tissues that lack the warts growth-suppressive gene. Collectively, these studies define an important role for Wbp2 as a downstream component of the SWH tissue growth-control pathway.

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Section: Resultsmentioning

confidence: 91%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 95%

mentioning

confidence: 99%

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Wbp2 cooperates with Yorkie to drive tissue growth downstream of the Salvador–Warts–Hippo pathway

et al. 2011

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“…Many factors equally affect the maximal levels of PR-and GR-mediated gene expression, or V max (McKenna et al, 1999;Giannoukos et al, 2001;Hosohata et al, 2003;Webster et al, 2003;Kino et al, 2004;Zhang et al, 2004;Dong et al, 2005). However, factors that preferentially alter the transactivation of PR vs. GR are being increasingly described (Tan et al, 2000;Fernandes et al, 2003;Metzger et al, 2003;Dhananjayan et al, 2006;Georgiakaki et al, 2006;Sanchez et al, 2007;Zhao et al, 2007). PR is reported to selectively recruit the coactivator SRC-1 and the comodulator CBP to acetylate K5 on histone H4 while GR preferentially recruits TIF2 and then PCAF to histone H3 to cause phosphorylation (S10) and acetylation (K14) and demethylation (K9) .…”

Section: Introductionmentioning

confidence: 99%

Differential modulation of glucocorticoid and progesterone receptor transactivation

Szapary

Song

et al. 2008

Molecular and Cellular Endocrinology

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The determinants of the different biological activities of progesterone receptors (PRs) vs. glucocorticoid receptors (GRs), which bind to the same DNA sequences, remain poorly understood. The mechanisms by which differential expression of a common target gene can be achieved by PR and GR include unequal agonist steroid concentrations for half maximal induction (EC 50 ) and dissimilar amounts of residual partial agonist activity for antisteroids in addition to the more common changes in total gene induction, or V max . Several factors are known to alter some or all of these three parameters for GR-regulated gene induction and some (i.e., the corepressors NCoR and SMRT) modulate the EC 50 and partial agonist activity for GR and PR induction of the same gene in opposite directions. The current study demonstrates that other factors (GME, GMEB-2, Ubc9, and STAMP) can also differentially interact with PRs and GRs or alter several of the above induction parameters under otherwise identical conditions. These results support the hypothesis that the modulation of EC 50 , partial agonist activity, and V max by a given factor is not limited to one receptor in a specific cell line. Furthermore, the number of factors that unequally modulate PR and GR induction parameters is now greatly expanded, thereby increasing the possible mechanisms for differential gene regulation by PRs vs. GRs.

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Variation of gene expression of fatty acid acyl CoA reductase associated with wax secretion of a scale insect, Ericerus pela, and identification of its regulation factors through the accessible chromatin analyses and yeast one‐hybrid

Fu,

Shi,

et al. 2024

Arch Insect Biochem Physiol

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The Chinese white wax scale insect (CWWSI), Ericerus pela, can secret an amount of wax equivalent to their body weight. Previous studies demonstrated the fatty acyl‐CoA reductase (far3) plays a pivotal role in wax secretion of CWWSI. The high expression of far3 is crucial for the massive wax secretion. However, the transcription regulation of far3 was not clear. To identify regulatory factors that control the expression of far3, the assay for transposase‐accessible chromatin (ATAC) and yeast one‐hybrid (Y1H) were carried out in this study. The ATAC sequencing of the CWWSI at the early wax‐secretion stage ATAC‐seq resulted in 22.75 GB raw data, generated 75,827,225 clean reads and revealed 142,771 peaks. There was one significant peak in the 3 kb upstream regulation regions. The peak sequence is located between −1000 and −670 bp upstream of the far3 transcription start site, spanning a length of 331 bp. This peak sequence served as bait for creating the pAbAi‐peak recombinant vector, used in Y1H screenings to identify proteins interacting with far3 gene. The results indicate a successful CWWSI cDNA library construction with a capacity of 1.2 × 107 colony forming unit, a 95.8% recombination rate, and insert sizes between 1,000 and 2,000 bp. Self‐activation tests established that 100 ng/mL of AbA effectively inhibited bait vector self‐activation. Finally, a total of 88 positive clones were selected. After sequencing and removal of duplication, 63 unique clones were obtained from these screened colonies. By aligning the clone sequences with full‐length transcriptome and genome of CWWSI, the full‐length coding sequences of these clones were obtained. BlastX analysis identified a transcription factor, nuclear transcription factor Y beta, and two co‐activators, cAMP‐response‐element‐binding‐protein‐binding protein and WW domain binding protein 2. Reverse transcription quantitative polymerase chain reaction analysis confirmed that their expression patterns were consistent with the developmental stages preceding wax secretion and matched the wax secretion characteristics during ovulation periods. These results are beneficial for further research into the regulatory mechanisms of wax secretion of CWWSI.

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WW Domain Binding Protein-2, an E6-Associated Protein Interacting Protein, Acts as a Coactivator of Estrogen and Progesterone Receptors

Cited by 73 publications

References 40 publications

Wbp2 cooperates with Yorkie to drive tissue growth downstream of the Salvador–Warts–Hippo pathway

Wbp2 cooperates with Yorkie to drive tissue growth downstream of the Salvador–Warts–Hippo pathway

Differential modulation of glucocorticoid and progesterone receptor transactivation

Variation of gene expression of fatty acid acyl CoA reductase associated with wax secretion of a scale insect, Ericerus pela, and identification of its regulation factors through the accessible chromatin analyses and yeast one‐hybrid

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