Repression of Transcription by WT1-BASP1 Requires the Myristoylation of BASP1 and the PIP2-Dependent Recruitment of Histone Deacetylase

Toska, Eneda; Campbell, Hayley; Shandilya, Jayasha; Goodfellow, Sarah J.; Shore, Paul; Medler, Kathryn F.; Roberts, Stefan G. E.

doi:10.1016/j.celrep.2012.08.005

Cited by 70 publications

(149 citation statements)

References 36 publications

(56 reference statements)

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“…BASP1 binding to PIP2 was shown to be required for the interaction with HDAC1, which resulted in the recruitment of HDAC1 to the promoter of WT1-targeted genes to repress transcription of Pol II (Toska et al, 2012). Here we report for the first time the presence of PIP2 in the transcription complex on the promoter during Pol I transcription.…”

Section: Pip2 Co-localizes With Rrna Nascent Transcripts In Nucleolimentioning

confidence: 71%

“…The presence of PIP2 on the Pol II promoter was recently shown by Toska et al (Toska et al, 2012). BASP1 binding to PIP2 was shown to be required for the interaction with HDAC1, which resulted in the recruitment of HDAC1 to the promoter of WT1-targeted genes to repress transcription of Pol II (Toska et al, 2012).…”

Section: Pip2 Co-localizes With Rrna Nascent Transcripts In Nucleolimentioning

confidence: 99%

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Involvement of PIP2 in RNA Polymerase I transcription

Yıldırım

Castaño

Sobol

et al. 2013

Journal of Cell Science

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SummaryRNA polymerase I (Pol I) transcription is essential for the cell cycle, growth and protein synthesis in eukaryotes. In the present study, we found that phosphatidylinositol 4,5-bisphosphate (PIP2) is a part of the protein complex on the active ribosomal promoter during transcription. PIP2 makes a complex with Pol I and the Pol I transcription factor UBF in the nucleolus. PIP2 depletion reduces Pol I transcription, which can be rescued by the addition of exogenous PIP2. In addition, PIP2 also binds directly to the pre-rRNA processing factor fibrillarin (Fib), and co-localizes with nascent transcripts in the nucleolus. PIP2 binding to UBF and Fib modulates their binding to DNA and RNA, respectively. In conclusion, PIP2 interacts with a subset of Pol I transcription machinery, and promotes Pol I transcription.

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Section: Pip2 Co-localizes With Rrna Nascent Transcripts In Nucleolimentioning

confidence: 71%

Section: Pip2 Co-localizes With Rrna Nascent Transcripts In Nucleolimentioning

confidence: 99%

Involvement of PIP2 in RNA Polymerase I transcription

Yıldırım

Castaño

Sobol

et al. 2013

Journal of Cell Science

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“…BASP1 specifically binds PI(4,5)P(2) in the nucleus. This leads to binding of the BASP1/ PI(4,5)P(2) complex to the promoter regions of Wilms tumor 1 target genes, recruitment of the histone deacetylase HDAC1, and results in repression of transcription[40]. …”

Section: N-myristoylationmentioning

confidence: 99%

Fatty acylation of proteins: The long and the short of it

Resh

2016

Progress in Lipid Research

238

235

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Long, short and medium chain fatty acids are covalently attached to hundreds of proteins. Each fatty acid confers distinct biochemical properties, enabling fatty acylation to regulate intracellular trafficking, subcellular localization, protein-protein and protein-lipid interactions. Myristate and palmitate represent the most common fatty acid modifying groups. New insights into how fatty acylation reactions are catalyzed, and how fatty acylation regulates protein structure and function continue to emerge. Myristate is typically linked to an N-terminal glycine, but recent studies reveal that lysines can also be myristoylated. Enzymes that remove N-terminal myristoyl-glycine or myristate from lysines have now been identified. DHHC proteins catalyze S-palmitoylation, but the mechanisms that regulate substrate recognition by individual DHHC family members remain to be determined. New studies continue to reveal thioesterases that remove palmitate from S-acylated proteins. Another area of rapid expansion is fatty acylation of the secreted proteins Hedgehog, Wnt and Ghrelin, by Hhat, Porcupine and GOAT, respectively. Understanding how these membrane bound O-acyl transferases recognize their protein and fatty acyl CoA substrates is an active area of investigation, and is punctuated by the finding that these enzymes are potential drug targets in human diseases.

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“…Antibodies were: anti-WT1 [89 (Toska et al, 2012); 1:50], anti-WT1 (C-19; sc192; 1:50), anti-SHH (sc-9024; 1:50), anti-GAP43 (sc10786; 1:50) from Santa Cruz Biotechnology, anti-Troma1 from Developmental Studies Hybridoma Bank (Iowa City, IA, USA; 1:50), anti-LEF1 (C1285; 1:50; from Signal Transduction), anti-SOX2 (AB97959; 1:50), anti-BMP4 (AB155033; 1:50), anti-WT1 (AB89901; 1:50) and anti-PTCH1 (AB53715; 1:50) from Abcam. Secondary antibodies were purchased from Jackson ImmunoResearch.…”

Section: Immunocytochemistrymentioning

confidence: 99%

WT1 regulates the development of the posterior taste field

et al. 2014

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Despite the importance of taste in determining nutrient intake, our understanding of the processes that control the development of the peripheral taste system is lacking. Several early regulators of taste development have been identified, including sonic hedgehog, bone morphogenetic protein 4 and multiple members of the Wnt/β-catenin signaling pathway. However, the regulation of these factors, including their induction, remains poorly understood. Here, we identify a crucial role for the Wilms' tumor 1 protein (WT1) in circumvallate (CV) papillae development. WT1 is a transcription factor that is important in the normal development of multiple tissues, including both the olfactory and visual systems. In mice, WT1 expression is detectable by E12.5, when the CV taste placode begins to form. In mice lacking WT1, the CV fails to develop normally and markers of early taste development are dysregulated compared with wild type. We demonstrate that expression of the WT1 target genes Lef1, Ptch1 and Bmp4 is significantly reduced in developing tongue tissue derived from Wt1 knockout mice and that, in normal tongue, WT1 is bound to the promoter regions of these genes. Moreover, siRNA knockdown of WT1 in cultured taste cells leads to a reduction in the expression of Lef1 and Ptch1. Our data identify WT1 as a crucial transcription factor in the development of the CV through the regulation of multiple signaling pathways that have established roles in the formation and patterning of taste placodes.

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Repression of Transcription by WT1-BASP1 Requires the Myristoylation of BASP1 and the PIP2-Dependent Recruitment of Histone Deacetylase

Cited by 70 publications

References 36 publications

Involvement of PIP2 in RNA Polymerase I transcription

Involvement of PIP2 in RNA Polymerase I transcription

Fatty acylation of proteins: The long and the short of it

WT1 regulates the development of the posterior taste field

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