• English
    • العربية
  • العربية
  • Login
  • QU
  • QU Library
  •  Home
  • Communities & Collections
  • Help
    • Item Submission
    • Publisher policies
    • User guides
    • FAQs
  • About QSpace
    • Vision & Mission
    • QSpace policies
View Item 
  •   Qatar University Digital Hub
  • Qatar University Institutional Repository
  • Academic
  • Faculty Contributions
  • College of Medicine
  • Medicine Research
  • View Item
  • Qatar University Digital Hub
  • Qatar University Institutional Repository
  • Academic
  • Faculty Contributions
  • College of Medicine
  • Medicine Research
  • View Item
  •      
  •  
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    SPERM FACTORS AND EGG ACTIVATION The structure and function relationship of sperm PLCZ1

    Thumbnail
    View/Open
    SPERM FACTORS AND EGG ACTIVATION. The structure and function relationship of sperm PLCZ1.pdf (3.816Mb)
    Date
    2022-07-01
    Author
    Thanassoulas, Angelos
    Swann, Karl
    Lai, F. Anthony
    Nomikos, Michail
    Metadata
    Show full item record
    Abstract
    In 2002, sperm-specific phospholipase C zeta1 (PLCZ1) was discovered and through these 20 years, it has been established as the predominant sperm oocyte-activating factor. PLCZ1 cRNA expression or direct protein microinjection into mammalian oocytes triggers calcium (Ca2+) oscillations indistinguishable from those observed at fertilization. The imperative role of PLCZ1 in oocyte activation is revealed by the vast number of human mutations throughout the PLCZ1 gene that have been identified and directly linked with certain forms of male infertility due to oocyte activation deficiency. PLCZ1 is the smallest PLC in size, comprising four N-terminal EF-hand domains, followed by X and Y catalytic domains, which are separated by the XY-linker, and ending with a C-terminal C2 domain. The EF hands are responsible for the high Ca2+ sensitivity of PLCZ1. The X and Y catalytic domains are responsible for the catalysis of the phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] substrate to produce the Ca2+-mobilising messenger, inositol 1,4,5-trisphosphate (IP3), while the XY-linker plays multiple roles in the unique mode of PLCZ1 action. Finally, the C2 domain has been proposed to facilitate the anchoring of PLCZ1 to intracellular vesicles through its direct interactions with specific phosphoinositides. This review discusses recent advances in the structure and function relationship of PLCZ1 and the potential binding partners of this important sperm-specific protein in the sperm and oocyte. The unravelling of all the remaining hidden secrets of sperm PLCZ1 should help us to understand the precise mechanism of fertilization, as well as enabling the diagnosis and treatment of currently unknown forms of PLCZ1-linked human infertility.
    URI
    https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85130862796&origin=inward
    DOI/handle
    http://dx.doi.org/10.1530/REP-21-0477
    http://hdl.handle.net/10576/39328
    Collections
    • Medicine Research [‎749‎ items ]

    entitlement


    Qatar University Digital Hub is a digital collection operated and maintained by the Qatar University Library and supported by the ITS department

    Contact Us | Send Feedback
    Contact Us | Send Feedback | QU

     

     

    Home

    Submit your QU affiliated work

    Browse

    All of Digital Hub
      Communities & Collections Publication Date Author Title Subject Type Language Publisher
    This Collection
      Publication Date Author Title Subject Type Language Publisher

    My Account

    Login

    Statistics

    View Usage Statistics

    About QSpace

    Vision & Mission QSpace policies

    Help

    Item Submission Publisher policiesUser guides FAQs

    Qatar University Digital Hub is a digital collection operated and maintained by the Qatar University Library and supported by the ITS department

    Contact Us | Send Feedback
    Contact Us | Send Feedback | QU

     

     

    Video