PTB-associated Splicing Factor (PSF) Functions as a Repressor of STAT6-mediated Igϵ Gene Transcription by Recruitment of HDAC1

Dong, Lijie; Zhang, Xinyu; Fu, Xiao; Zhang, Xianzhi; Gao, Xingjie; Zhu, Mengyu; Wang, Xinting; Yang, ZhenXia; Jensen, Ole N.; Saarikettu, Juha; Yao, Zhi; Silvennoinen, Olli; Yang, Jie

doi:10.1074/jbc.m110.168377

Cited by 21 publications

(17 citation statements)

References 37 publications

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“…It indicates that different domains of Tudor-SN protein may recruit different protein complexes to play different roles. In line with this concept, we have demonstrated that Tudor-SN functions as a transcriptional co-activator of STAT6 via interaction with the SNlike domains (12,15), whereas the TSN domain is involved in the spliceosome assembly and accelerates the kinetics of precursor-messenger RNA (pre-mRNA) splicing (13). However, the precise molecular mechanism underlying the involvement of Tudor-SN in pre-mRNA processing has not been fully elucidated.…”

mentioning

confidence: 72%

Tudor Staphylococcal Nuclease (Tudor-SN) Participates in Small Ribonucleoprotein (snRNP) Assembly via Interacting with Symmetrically Dimethylated Sm Proteins

Gao

Zhao

et al. 2012

Journal of Biological Chemistry

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Background: Human Tudor staphylococcal nuclease (Tudor-SN) is involved in the snRNP assembly. Results: The efficient formation of Tudor-SN⅐SmB complex requires binding orientation of the methylated ligand and the specific binding pocket. Conclusion: Tudor-SN takes part in regulating pre-mRNA splicing via the recruitment of U5 snRNP and the association of Sm protein.Significance: The mechanism underlying the involvement of Tudor-SN in regulating snRNP biogenesis was revealed.

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confidence: 72%

Tudor Staphylococcal Nuclease (Tudor-SN) Participates in Small Ribonucleoprotein (snRNP) Assembly via Interacting with Symmetrically Dimethylated Sm Proteins

Gao

Zhao

et al. 2012

Journal of Biological Chemistry

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“…For example, PSF and p54nrb, in addition to their roles in facilitating RNA splicing, have been shown to function as transcriptional repressors for several nuclear receptors including progesterone receptor and androgen receptor29. Further study has indicated that PSF plays a role in repression of STAT6-mediated transcription through recruitment of the HDAC complex30. It has been reported that splicing factors such as PGC-1, CoAA, and CAPERs potentially coactivate the transcriptional activity of nuclear receptors313233.…”

Section: Discussionmentioning

confidence: 99%

LUC7L3/CROP inhibits replication of hepatitis B virus via suppressing enhancer II/basal core promoter activity

Ito

Sun

et al. 2016

Sci Rep

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The core promoter of hepatitis B virus (HBV) genome is a critical region for transcriptional initiation of 3.5 kb, pregenome and precore RNAs and for the viral replication. Although a number of host-cell factors that potentially regulate the viral promoter activities have been identified, the molecular mechanisms of the viral gene expression, in particular, regulatory mechanisms of the transcriptional repression remain elusive. In this study, we identified LUC7 like 3 pre-mRNA splicing factor (LUC7L3, also known as hLuc7A or CROP) as a novel interacting partner of HBV enhancer II and basal core promoter (ENII/BCP), key elements within the core promoter, through the proteomic screening and found that LUC7L3 functions as a negative regulator of ENII/BCP. Gene silencing of LUC7L3 significantly increased expression of the viral genes and antigens as well as the activities of ENII/BCP and core promoter. In contrast, overexpression of LUC7L3 inhibited their activities and HBV replication. In addition, LUC7L3 possibly contributes to promotion of the splicing of 3.5 kb RNA, which may also be involved in negative regulation of the pregenome RNA level. This is the first to demonstrate the involvement of LUC7L3 in regulation of gene transcription and in viral replication.

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“…We have previously reported that Tudor-SN is capable of enhancing histone acetyltransferase activity via recruitment of CREB-binding protein (CBP) to STAT6 (15). Very recently we also identified PSF as a repressor of STAT6-mediated transcription that functions through recruitment of histone deacetylase (HDAC) to the STAT6 transcriptional complex (24). We thus investigated whether a lack of Tudor-SN in MEF cells affects histone acetylation.…”

Section: Observed In Mef-ko Cells (Upper Panel) Statistical Analysismentioning

confidence: 99%

Tudor-SN, a Novel Coactivator of Peroxisome Proliferator-activated Receptor γ Protein, Is Essential for Adipogenesis

Duan¹,

Zhao

et al. 2014

Journal of Biological Chemistry

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Background: Tudor-SN has been observed in lipid droplets, but its role in lipid homeostasis remains unclear. Results: Tudor-SN and PPAR␥ are both regulated by C/EBP␤ during adipogenesis and significantly influence the regulation of PPAR␥ target genes. Conclusion: Tudor-SN functions as a co-activator of PPAR␥ in adipogenesis. Significance: The study has elucidated a new functional mechanism for the regulation of adipogenesis.

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PTB-associated Splicing Factor (PSF) Functions as a Repressor of STAT6-mediated Igϵ Gene Transcription by Recruitment of HDAC1

Cited by 21 publications

References 37 publications

Tudor Staphylococcal Nuclease (Tudor-SN) Participates in Small Ribonucleoprotein (snRNP) Assembly via Interacting with Symmetrically Dimethylated Sm Proteins

Tudor Staphylococcal Nuclease (Tudor-SN) Participates in Small Ribonucleoprotein (snRNP) Assembly via Interacting with Symmetrically Dimethylated Sm Proteins

LUC7L3/CROP inhibits replication of hepatitis B virus via suppressing enhancer II/basal core promoter activity

Tudor-SN, a Novel Coactivator of Peroxisome Proliferator-activated Receptor γ Protein, Is Essential for Adipogenesis

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