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Ubiquitin-activating enzyme (UBA1) is required for sperm capacitation, acrosomal exocytosis and sperm-egg coat penetration during porcine fertilization

  1. 1.
    SYSNO ASEP0367613
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleUbiquitin-activating enzyme (UBA1) is required for sperm capacitation, acrosomal exocytosis and sperm-egg coat penetration during porcine fertilization
    Author(s) Yi, Y.-J. (KR)
    Zimmermann, S.W. (US)
    Manandhar, G. (US)
    Odhiambo, J.F. (US)
    Kennedy, C. (US)
    Jonáková, Věra (BTO-N) RID
    Maňásková-Postlerová, Pavla (BTO-N) ORCID
    Sutovsky, M. (US)
    Park, C.-S. (US)
    Sutovsky, P. (US)
    Number of authors10
    Source TitleInternational Journal of Andrology. - : WILEY-BLACKWELL - ISSN 0105-6263
    Roč. 35, č. 2 (2012), s. 196-210
    Number of pages15 s.
    Languageeng - English
    CountryUS - United States
    Keywordsacrosome ; capacitation ; fertilization ; ubiqutin
    Subject RIVCE - Biochemistry
    R&D ProjectsGA303/09/1285 GA ČR - Czech Science Foundation (CSF)
    1M06011 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    NS10009 GA MZd - Ministry of Health (MZ)
    CEZAV0Z50520701 - BTO-N (2007-2013)
    UT WOS000301442200012
    DOI10.1111/j.1365-2605.2011.01217.x.
    AnnotationProtein ubiquitination is covalent post-translational modification that targets proteins for proteolysis by the 26S proteasome. The E1-type ubiquitin-activating enzyme (UBA1) is responsible for the initial step of ubiquitin–protein ligation. Proteasomal proteolysis of ubiquitinated spermatozoa and oocyte proteins occurs during mammalian fertilization. UBA1 was detected in boar sperm-acrosomal extracts by Western blotting (WB) and by IMF in the acrosomal caps. A specific UBA1 inhibitor, PYR-41, altered the outer acrosomal membrane during sperm capacitation and reduced fertilization rates during in vitro fertilization. WB with antiphosphotyrosine antibodies and antibodies against acrosomal proteins SPINK2 (acrosin inhibitor) and AQN1 (spermadhesin) revealed that the capacitationinduced modification of those proteins was altered by PYR-41. It appears that de novo protein ubiquitination involving UBA1 contributes to sperm capacitation and acrosomal function during fertilization.
    WorkplaceInstitute of Biotechnology
    ContactMonika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700
    Year of Publishing2013
Number of the records: 1  

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