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Gamete membrane microdomains and their associated molecules in fertilization signaling

Fertilization is the fundamental system of biological reproduction in many organisms, including animals, plants, and algae. A growing body of knowledge has emerged to explain how fertilization and activation of development are accomplished. Studies on the molecular mechanisms of fertilization are in...

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Published in:Molecular reproduction and development 2011-10, Vol.78 (10-11), p.814-830
Main Authors: Hasan, A.K.M. Mahbub, Fukami, Yasuo, Sato, Ken-ichi
Format: Article
Language:English
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Summary:Fertilization is the fundamental system of biological reproduction in many organisms, including animals, plants, and algae. A growing body of knowledge has emerged to explain how fertilization and activation of development are accomplished. Studies on the molecular mechanisms of fertilization are in progress for a wide variety of multicellular organisms. In this review, we summarize recent findings and debates about the long‐standing questions concerning fertilization: how egg and sperm become competent for their interaction with each other, how the binding and fusion of these gamete cells are made possible, and how the fertilized eggs initiate development to a newborn. We will focus on the structure and function of the membrane microdomains (MDs) of egg and sperm that may serve as a platform or signaling center for the aforementioned cellular functions. In particular, we provide evidence that MDs of eggs from the African clawed frog, Xenopus laevis, play a pivotal role in receiving extracellular signals from fertilizing sperm and then transmitting them to the egg cytoplasm, where the tyrosine kinase Src is present and responsible for the subsequent signaling events collectively called egg activation. The presence of a new signaling axis involving uroplakin III, an MD‐associated transmembrane protein, and Src in this system will be highlighted and discussed. Mol. Reprod. Dev. 78:814–830, 2011. © 2011 Wiley Periodicals, Inc.
ISSN:1040-452X
1098-2795
1098-2795
DOI:10.1002/mrd.21336