Proteolytic cleavage of the cell surface protein p160 is required for detachment of the fertilization envelope in the sea urchin

Developmental Biology
Sheila A Haley, G M Wessel

Abstract

Sea urchin eggs secrete a serine protease activity, CGSP1, at fertilization that is essential for the block to polyspermy. Several targets of this proteolytic activity on the plasma membrane were identified here using a cell surface biotinylation approach. Amino acid microsequencing of one of these proteins led to the identification of a 4.75-kb cDNA clone from a Strongylocentrotus purpuratus ovary cDNA library that encodes a 160-kDa protein called p160. This protein contains five CUB domains and a putative transmembrane domain suggesting that p160 is an integral membrane protein with protein-protein interaction motifs facing the extracellular matrix of the egg. Whole-mount immunolocalization studies demonstrate that p160 is on the surface of the egg, enriched at the tips of microvilli. The protein is removed at fertilization in a protease-dependent manner, and functional assays suggest that p160 serves to link the plasma membrane to the vitelline layer until fertilization. Thus, p160 is a key candidate for a vitelline-layer linker protein, the selective proteolysis of which functions in the block to polyspermy in the sea urchin egg.

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Citations

Jun 1, 2014·Biochemical and Biophysical Research Communications·Nathalie OulhenGary M Wessel
Aug 7, 2009·Molecular Reproduction and Development·Gary M Wessel, Julian L Wong
Aug 30, 2008·Evolution; International Journal of Organic Evolution·Adrianne ProkupekLawrence Harshman
Jun 21, 2011·Molecular Reproduction and Development·A K M Mahbub HasanKen-ichi Sato
Jul 14, 2010·Current Biology : CB·Mark A Johnson
Nov 1, 2006·Developmental Biology·Jia L SongGary M Wessel
Mar 28, 2006·Current Topics in Developmental Biology·Julian L Wong, Gary M Wessel
Jan 22, 2013·Evolution & Development·Nathalie OulhenGary M Wessel

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