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Science 22 September 1995:
Vol. 269. no. 5231, pp. 1718 - 1721
DOI: 10.1126/science.7569899
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Articles

Science, Vol 269, Issue 5231, 1718-1721
Copyright © 1995 by American Association for the Advancement of Science

articles

Activation of a G protein complex by aggregation of beta-1,4-galactosyltransferase on the surface of sperm

X Gong, DH Dubois, DJ Miller, and BD Shur

Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030, USA.

Fertilization is initiated by the species-specific binding of sperm to the extracellular coat of the egg. One sperm receptor for the mouse egg is beta-1,4-galactosyltransferase (GalTase), which binds O-linked oligosaccharides on the egg coat glycoprotein ZP3. ZP3 binding induces acrosomal exocytosis through the activation of a pertussis toxin-sensitive heterotrimeric guanine nucleotide-binding protein (G protein). The cytoplasmic domain of sperm surface GalTase bound to and activated a heterotrimeric G protein complex that contained the Gi alpha subunit. Aggregation of GalTase by multivalent ligands elicited G protein activation. Sperm from transgenic mice that overexpressed GalTase had higher rates of G protein activation than did wild-type sperm, which rendered transgenic sperm hypersensitive to their ZP3 ligand. Thus, the cytoplasmic domain of cell surface GalTase appears to enable it to function as a signal-transducing receptor for extracellular oligosaccharide ligands.


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