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    Comparative analysis of FKBP family protein: Evaluation, structure, and function in mammals and Drosophila melanogaster

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    Author
    Ghartey-Kwansah, G.
    Li, Z.
    Feng, R.
    Date
    2018
    Journal
    BMC Developmental Biology
    Publisher
    BioMed Central Ltd.
    Type
    Article
    
    Metadata
    Show full item record
    See at
    https://dx.doi.org/10.1186/s12861-018-0167-3
    Abstract
    Background: FK506-binding proteins (FKBPs) have become the subject of considerable interest in several fields, leading to the identification of several cellular and molecular pathways in which FKBPs impact prenatal development and pathogenesis of many human diseases. Main body: This analysis revealed differences between how mammalian and Drosophila FKBPs mechanisms function in relation to the immunosuppressant drugs, FK506 and rapamycin. Differences that could be used to design insect-specific pesticides. (1) Molecular phylogenetic analysis of FKBP family proteins revealed that the eight known Drosophila FKBPs share homology with the human FKBP12. This indicates a close evolutionary relationship, and possible origination from a common ancestor. (2) The known FKBPs contain FK domains, that is, a prolyl cis/trans isomerase (PPIase) domain that mediates immune suppression through inhibition of calcineurin. The dFKBP59, CG4735/Shutdown, CG1847, and CG5482 have a Tetratricopeptide receptor domain at the C-terminus, which regulates transcription and protein transportation. (3) FKBP51 and FKBP52 (dFKBP59), along with Cyclophilin 40 and protein phosphatase 5, function as Hsp90 immunophilin co-chaperones within steroid receptor-Hsp90 heterocomplexes. These immunophilins are potential drug targets in pathways associated with normal physiology and may be used to treat a variety of steroid-based diseases by targeting exocytic/endocytic cycling and vesicular trafficking. (4) By associating with presinilin, a critical component of the Notch signaling pathway, FKBP14 is a downstream effector of Notch activation at the membrane. Meanwhile, Shutdown associates with transposons in the PIWI-interacting RNA pathway, playing a crucial role in both germ cells and ovarian somas. Mutations in or silencing of dFKBPs lead to early embryonic lethality in Drosophila. Therefore, further understanding the mechanisms of FK506 and rapamycin binding to immunophilin FKBPs in endocrine, cardiovascular, and neurological function in both mammals and Drosophila would provide prospects in generating unique, insect specific therapeutics targeting the above cellular signaling pathways. Conclusion: This review will evaluate the functional roles of FKBP family proteins, and systematically summarize the similarities and differences between FKBP proteins in Drosophila and Mammals. Specific therapeutics targeting cellular signaling pathways will also be discussed. Copyright 2018 The Author(s).
    Sponsors
    This work was supported by the National Natural Science Foundation of China (#31371256/31571273/31771277), the Ministry of Science and Technology of China (#2015CB943100), the National Department of Education Central Universities Research Fund (#GK20130100/201701005/ GERP-17-45), US Maryland Stem Cell Research Fund (2009MSCRFE008300), the Foreign Distinguished Scientist Program from the National Department of Education (#MS2014SXSF038), and the Outstanding Doctoral Thesis fund (#X2014YB02/X2015YB05).
    Keyword
    FK506-binding protein
    Hsp90
    Inositol 1, 4, 5-trisphosphate
    Notch
    Peptidyl-prolyl isomerase
    Phospholipase C
    Ryanodine receptor
    Tetratricopetide receptor
    Transient receptor potential
    Identifier to cite or link to this item
    https://www.scopus.com/inward/record.uri?eid=2-s2.0-85044518112&doi=10.1186%2fs12861-018-0167-3&partnerID=40&md5=e1a19096b041607f170f5b0b5b516468; http://hdl.handle.net/10713/9654
    ae974a485f413a2113503eed53cd6c53
    10.1186/s12861-018-0167-3
    Scopus Count
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    UMB Open Access Articles 2018

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