Document Detail


Preferentially localized dynein and perinuclear dynactin associate with nuclear pore complex proteins to mediate genomic union during mammalian fertilization.
MedLine Citation:
PMID:  14600259     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Fertilization is complete once the parental genomes unite, and requires the migration of the egg nucleus to the sperm nucleus (female and male pronuclei, respectively) on microtubules within the inseminated egg. Neither the molecular mechanism of pronucleus binding to microtubules nor the role of motor proteins in regulating pronuclear motility has been fully characterized, and the failure of zygotic development in some patients suggests that they contribute to human infertility. Based on the minus-end direction of female pronuclear migration, we propose a role for cytoplasmic dynein and dynactin in associating with the pronuclear envelope and mediating genomic union. Our results show that dynein intermediate and heavy chains preferentially concentrate around the female pronucleus, whereas dynactin subunits p150Glued, p50 and p62 localize to the surfaces of both pronuclei. Transfection of antibodies against dynein and dynactin block female pronuclear migration in zygotes. Both parthenogenetic activation in oocytes and microtubule depolymerization in zygotes significantly reduce the localization of dynein to the female pronucleus but do not inhibit the pronuclear association of dynactin. When immunoprecipitated from zygotes, p150Glued associates with nuclear pore complex proteins, as well as the intermediate filament vimentin and dynein. Antibodies against nucleoporins and vimentin inhibit pronuclear apposition when transfected into zygotes. We conclude that preferentially localized dynein and perinuclear dynactin associate with the nuclear pore complex and vimentin and are required to mediate genomic union. These data suggest a model in which dynein accumulates and binds to the female pronucleus on sperm aster microtubules, where it interacts with dynactin, nucleoporins and vimentin.
Authors:
Christopher Payne; Vanesa Rawe; João Ramalho-Santos; Calvin Simerly; Gerald Schatten
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of cell science     Volume:  116     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2003 Dec 
Date Detail:
Created Date:  2003-11-05     Completed Date:  2004-06-09     Revised Date:  2014-09-09    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  4727-38     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Cattle / physiology
Cell Nucleus / metabolism
Dyneins / metabolism*
Female
Fertilization / genetics*
Genomics
Macaca mulatta / physiology
Male
Microtubule-Associated Proteins / metabolism*
Microtubules / metabolism
Models, Molecular
Nuclear Pore Complex Proteins / metabolism*
Oocytes / metabolism
Protein Subunits / metabolism*
Spermatozoa / metabolism
Zygote / metabolism
Grant Support
ID/Acronym/Agency:
R00 HD055330/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/Microtubule-Associated Proteins; 0/Nuclear Pore Complex Proteins; 0/Protein Subunits; 144198-36-7/dynactin; EC 3.6.4.2/Dyneins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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