Sperm head membrane reorganisation during capacitation.
The sperm cell has a characteristic polarized morphology and its surface is also highly differentiated into different membrane domains. Junctional protein ring structures seal the surface of the mid-piece from the head and the tail respectively and probably prevent random diffusion of membrane molecules over the protein rings. Despite the absence of such lateral diffusion-preventing structures, the sperm head surface is also highly heterogeneous. Furthermore, lipid and membrane protein ordering is subjected to changes when sperm become capacitated. The forces that maintain the lateral polarity of membrane molecules over the sperm surface, as well as those that cause their dynamic redistribution, are only poorly understood. Nevertheless, it is known that each of the sperm head surface regions has specific roles to allow sperm to fertilize the oocyte: a specific region is devoted to zona pellucida binding, a larger area of the sperm head surface is involved in the acrosome reaction (intracellular fusion), while yet another region is involved in egg plasma membrane binding and fertilization fusion (intercellular membrane fusion). All three events occur in the area of the sperm head where the plasma membrane covers the acrosome. Recently, lipid ordered microdomains (lipid rafts) were discovered in membranes of many biological specimens including sperm. In this review, we cover the latest insights about sperm lipid raft research and discuss how sperm lipid raft dynamics may relate to sperm-zona binding and the zona-induced acrosome reaction.
Gadella
Bart M
BM
Department of Biochemistry and Cell Biology and of Farm Animal Health, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands. B.M.Gadella@uu.nl
Tsai
Pei-Shiue
PS
Boerke
Arjen
A
Brewis
Ian A
IA
D051722:ADAM Proteins / Q000378:metabolism; D000818:Animals; D002784:Cholesterol / Q000378:metabolism; D004822:Epididymis / Q000378:metabolism; D005260:Female; D000072196:Fertilins; D005306:Fertilization; D008297:Male; D008562:Membrane Glycoproteins / Q000378:metabolism; D021962:Membrane Microdomains / Q000378:metabolism; D009865:Oocytes / Q000378:metabolism; D010063:Ovum / Q000378:metabolism; D017434:Protein Structure, Tertiary; D050600:SNARE Proteins / Q000378:metabolism; D029589:Seminal Plasma Proteins / Q000378:metabolism; D013077:Sperm Head / Q000378:metabolism*; D013094:Spermatozoa / Q000378:metabolism*
D008562:Membrane Glycoproteins; D050600:SNARE Proteins; D029589:Seminal Plasma Proteins; C425042:spermadhesin; D002784:Cholesterol; D051722:ADAM Proteins; D000072196:Fertilins