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  1. Article: Yki stability and activity are regulated by Ca

    Zhai, Chaojun / Wang, Yunfeng / Qi, Shenao / Yang, Muhan / Wu, Shian

    Journal of genetics and genomics = Yi chuan xue bao

    2024  

    Abstract: Yorkie (Yki) is a key effector of the Hippo pathway that activates the expression of targets by associating with the transcription factor Scalloped (Sd). Various upstream signals, such as cell polarity and mechanical cues, control transcriptional ... ...

    Abstract Yorkie (Yki) is a key effector of the Hippo pathway that activates the expression of targets by associating with the transcription factor Scalloped (Sd). Various upstream signals, such as cell polarity and mechanical cues, control transcriptional programs by regulating Yki activity. Searching for Yki regulatory factors has far-reaching significance for studying the Hippo pathway in animal development and human diseases. In this study, we identify Calpain-A (CalpA) and Calpain-B (CalpB), two calcium (Ca
    Language English
    Publishing date 2024-04-23
    Publishing country China
    Document type Journal Article
    ZDB-ID 2374568-X
    ISSN 1873-5533 ; 1673-8527
    ISSN (online) 1873-5533
    ISSN 1673-8527
    DOI 10.1016/j.jgg.2024.04.011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: C‐terminal–mediated homodimerization of Expanded is critical for its ability to promote Hippo signalling in Drosophila

    Wang, Guiping / Zhai, Chaojun / Ji, Xiaohui / Wang, Enlin / Zhao, Shanshan / Qian, Chenxi / Yu, Dongyue / Wang, Yunfeng / Wu, Shian

    FEBS letters. 2022 July, v. 596, no. 13

    2022  

    Abstract: Hippo signalling plays key role in tissue growth and homeostasis, and its dysregulation is implicated in various human diseases. Expanded (Ex) is an important upstream activator of Hippo signalling; however, how Ex activates Hippo signalling is still ... ...

    Abstract Hippo signalling plays key role in tissue growth and homeostasis, and its dysregulation is implicated in various human diseases. Expanded (Ex) is an important upstream activator of Hippo signalling; however, how Ex activates Hippo signalling is still poorly understood. Here, we demonstrate that Ex forms a homodimer via C‐terminal interaction, and that the ExC2 region (912–1164 aa) is sufficient and essential for Ex dimerization. Functional analysis shows that ExC2 is required for Ex to promote the phosphorylation and inactivation of Yki in Drosophila cells. Further in vivo analysis shows that ExC2 is important for Ex to control Drosophila tissue growth. Our study, thus, uncovers a novel mechanism whereby Ex homodimerization mediates its full activation to promote Hippo signalling in growth control.
    Keywords Drosophila ; dimerization ; homeostasis ; humans ; phosphorylation
    Language English
    Dates of publication 2022-07
    Size p. 1628-1638.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note JOURNAL ARTICLE
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14332
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2005/702: Show issues
    Z 5.4: Show issues

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  3. Article ; Online: C-terminal-mediated homodimerization of Expanded is critical for its ability to promote Hippo signalling in Drosophila.

    Wang, Guiping / Zhai, Chaojun / Ji, Xiaohui / Wang, Enlin / Zhao, Shanshan / Qian, Chenxi / Yu, Dongyue / Wang, Yunfeng / Wu, Shian

    FEBS letters

    2022  Volume 596, Issue 13, Page(s) 1628–1638

    Abstract: Hippo signalling plays key role in tissue growth and homeostasis, and its dysregulation is implicated in various human diseases. Expanded (Ex) is an important upstream activator of Hippo signalling; however, how Ex activates Hippo signalling is still ... ...

    Abstract Hippo signalling plays key role in tissue growth and homeostasis, and its dysregulation is implicated in various human diseases. Expanded (Ex) is an important upstream activator of Hippo signalling; however, how Ex activates Hippo signalling is still poorly understood. Here, we demonstrate that Ex forms a homodimer via C-terminal interaction, and that the ExC2 region (912-1164 aa) is sufficient and essential for Ex dimerization. Functional analysis shows that ExC2 is required for Ex to promote the phosphorylation and inactivation of Yki in Drosophila cells. Further in vivo analysis shows that ExC2 is important for Ex to control Drosophila tissue growth. Our study, thus, uncovers a novel mechanism whereby Ex homodimerization mediates its full activation to promote Hippo signalling in growth control.
    MeSH term(s) Animals ; Dimerization ; Drosophila/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins/genetics ; Protein Serine-Threonine Kinases/genetics ; Signal Transduction
    Chemical Substances Drosophila Proteins ; Intracellular Signaling Peptides and Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2022-03-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14332
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 282: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: The SCF ubiquitin ligase Slimb controls Nerfin-1 turnover in Drosophila.

    Lin, Xiaohui / Wang, Feng / Li, Yuanpei / Zhai, Chaojun / Wang, Guiping / Zhang, Xiaoting / Gao, Yang / Yi, Tao / Sun, Dan / Wu, Shian

    Biochemical and biophysical research communications

    2017  Volume 495, Issue 1, Page(s) 629–633

    Abstract: The C2H2 type zinc-finger transcription factor Nerfin-1 expresses dominantly in Drosophila nervous system and plays an important role in early axon guidance decisions and preventing neurons dedifferentiation. Recently, increasing reports indicated that ... ...

    Abstract The C2H2 type zinc-finger transcription factor Nerfin-1 expresses dominantly in Drosophila nervous system and plays an important role in early axon guidance decisions and preventing neurons dedifferentiation. Recently, increasing reports indicated that INSM1 (homologue to nerfin-1 in mammals) is a useful marker for prognosis of neuroendocrine tumors. The dynamic expression of Nerfin-1 is regulated post-transcriptionally by multiple microRNAs; however, its post-translational regulation is still unclear. Here we showed that the protein turnover of Nerfin-1 is regulated by Slimb, the substrate adaptor of SCF
    MeSH term(s) Animals ; Cell Cycle Proteins/metabolism ; Drosophila/metabolism ; Drosophila Proteins/metabolism ; Gene Expression Regulation, Developmental/physiology ; Metabolic Clearance Rate ; SKP Cullin F-Box Protein Ligases/metabolism ; Transcription Factors/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination/physiology
    Chemical Substances Cell Cycle Proteins ; Drosophila Proteins ; Transcription Factors ; nerfin-1 protein, Drosophila ; slmb protein, Drosophila ; SKP Cullin F-Box Protein Ligases (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2017-11-14
    Publishing country United States
    Document type Journal Article
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2017.11.090
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Usp10 Modulates the Hippo Pathway by Deubiquitinating and Stabilizing the Transcriptional Coactivator Yorkie.

    Gao, Yang / Zhang, Xiaoting / Xiao, Lijuan / Zhai, Chaojun / Yi, Tao / Wang, Guiping / Wang, Enlin / Ji, Xiaohui / Hu, Liangchang / Shen, Guangshuang / Wu, Shian

    International journal of molecular sciences

    2019  Volume 20, Issue 23

    Abstract: The Hippo signaling pathway is an evolutionarily conserved regulator that plays important roles in organ size control, homeostasis, and tumorigenesis. As the key effector of the Hippo pathway, Yorkie (Yki) binds to transcription factor Scalloped (Sd) and ...

    Abstract The Hippo signaling pathway is an evolutionarily conserved regulator that plays important roles in organ size control, homeostasis, and tumorigenesis. As the key effector of the Hippo pathway, Yorkie (Yki) binds to transcription factor Scalloped (Sd) and promotes the expression of target genes, leading to cell proliferation and inhibition of apoptosis. Thus, it is of great significance to understand the regulatory mechanism for Yki protein turnover. Here, we provide evidence that the deubiquitinating enzyme ubiquitin-specific protease 10 (Usp10) binds Yki to counteract Yki ubiquitination and stabilize Yki protein in
    MeSH term(s) Animals ; Cell Line ; Cytoplasm/metabolism ; Drosophila Proteins/analysis ; Drosophila Proteins/metabolism ; Drosophila melanogaster/cytology ; Drosophila melanogaster/metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Nuclear Proteins/analysis ; Nuclear Proteins/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Proteolysis ; Signal Transduction ; Trans-Activators/analysis ; Trans-Activators/metabolism ; Ubiquitin-Specific Proteases ; Ubiquitination
    Chemical Substances Drosophila Proteins ; Intracellular Signaling Peptides and Proteins ; Nuclear Proteins ; Trans-Activators ; Yki protein, Drosophila ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; hpo protein, Drosophila (EC 2.7.11.1) ; Ubiquitin-Specific Proteases (EC 3.4.19.12) ; Usp10 protein, Drosophila (EC 3.4.19.12) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2019-11-29
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms20236013
    Database MEDical Literature Analysis and Retrieval System OnLINE

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