Structure and function of Pygo in organ development dependent and independent Wnt signalling. (17th July 2020)
- Record Type:
- Journal Article
- Title:
- Structure and function of Pygo in organ development dependent and independent Wnt signalling. (17th July 2020)
- Main Title:
- Structure and function of Pygo in organ development dependent and independent Wnt signalling
- Authors:
- Shi, Yan
Wu, Xiushan
Zhu, Shuoji
Huang, Huanlei
Zhuang, Jian
Yuan, Haiyun
Yuan, Wuzhou
Zhu, Ping - Abstract:
- Abstract : Pygo is a nuclear protein containing two conserved domains, NHD and PHD, which play important roles in embryonic development and carcinogenesis. Pygo was first identified as a core component of the Wnt/β-catenin signalling pathway. However, it has also been reported that the function of Pygo is not always Wnt/β-catenin signalling dependent. In this review, we summarise the functions of both domains of Pygo and show that their functions are synergetic. The PHD domain mainly combines with transcription co-factors, including histone 3 and Bcl9/9l. The NHD domain mainly recruits histone methyltransferase/acetyltransferase (HMT/HAT) to modify lysine 4 of the histone 3 tail (H3K4) and interacts with Chip/LIM-domain DNA-binding proteins (ChiLS) to form enhanceosomes to regulate transcriptional activity. Furthermore, we summarised chromatin modification differences of Pygo in Drosophila (dPygo) and vertebrates, and found that Pygo displayes a chromatin silencing function in Drosophila, while in vertebates, Pygo has a chromatin-activating function due to the two substitution of two amino acid residues. Next, we confirmed the relationship between Pygo and Bcl9/9l and found that Pygo–Bcl/9l are specifically partnered both in the nucleus and in the cytoplasm. Finally, we discuss whether transcriptional activity of Pygo is Wnt/β-catenin dependent during embryonic development. Available information indications that the transcriptional activity of Pygo in embryonic developmentAbstract : Pygo is a nuclear protein containing two conserved domains, NHD and PHD, which play important roles in embryonic development and carcinogenesis. Pygo was first identified as a core component of the Wnt/β-catenin signalling pathway. However, it has also been reported that the function of Pygo is not always Wnt/β-catenin signalling dependent. In this review, we summarise the functions of both domains of Pygo and show that their functions are synergetic. The PHD domain mainly combines with transcription co-factors, including histone 3 and Bcl9/9l. The NHD domain mainly recruits histone methyltransferase/acetyltransferase (HMT/HAT) to modify lysine 4 of the histone 3 tail (H3K4) and interacts with Chip/LIM-domain DNA-binding proteins (ChiLS) to form enhanceosomes to regulate transcriptional activity. Furthermore, we summarised chromatin modification differences of Pygo in Drosophila (dPygo) and vertebrates, and found that Pygo displayes a chromatin silencing function in Drosophila, while in vertebates, Pygo has a chromatin-activating function due to the two substitution of two amino acid residues. Next, we confirmed the relationship between Pygo and Bcl9/9l and found that Pygo–Bcl/9l are specifically partnered both in the nucleus and in the cytoplasm. Finally, we discuss whether transcriptional activity of Pygo is Wnt/β-catenin dependent during embryonic development. Available information indications that the transcriptional activity of Pygo in embryonic development is either Wnt/β-catenin dependent or independent in both tissue-specific and cell-specific-modes. … (more)
- Is Part Of:
- Biochemical Society transactions. Volume 48:Number 4(2020)
- Journal:
- Biochemical Society transactions
- Issue:
- Volume 48:Number 4(2020)
- Issue Display:
- Volume 48, Issue 4 (2020)
- Year:
- 2020
- Volume:
- 48
- Issue:
- 4
- Issue Sort Value:
- 2020-0048-0004-0000
- Page Start:
- 1781
- Page End:
- 1794
- Publication Date:
- 2020-07-17
- Subjects:
- embryonic development -- NHD domain -- PHD domain -- Pygo -- wnt/β-catenin signalling
Biochemistry -- Congresses
572 - Journal URLs:
- https://portlandpress.com/biochemsoctrans ↗
- DOI:
- 10.1042/BST20200393 ↗
- Languages:
- English
- ISSNs:
- 0300-5127
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library HMNTS - ELD Digital store
- Ingest File:
- 14855.xml