Membrane interactions of the putative fusion peptide (MFalphaP) from fertilin-alpha, the mouse sperm protein complex involved in fertilization

References

• Almeida, E. A. C., Huovila, A.-P. J., Sutherland, A. E., Stephens, L. E., Calarco, P. G., Shaw, L. M., Mercurio, A. M., Sonnenberg, A., Primakoff, P., Myles, D. G. and White, J. M., 1995, Mouse egg integrin a6b1 functions as a sperm receptor. Cell, 81, 1095 - 1104.
   Google Scholar
• Bigler, D., Chen, M., Waters, S. and White, J. M., 1997, A model for sperm- egg binding based on ADAMs and integrins. Trends in Cell Biology, 7, 220 - 225.
   Google Scholar
• Blobel, C. P., Myles, D. G., Primakoff, P. and White, J. M., 1990, Proteolytic processing of a protein involved in sperm- egg fusion correlates with acquisition of fertilization competence. Journal of Cell Biology, 111, 69 - 78.
   PubMedGoogle Scholar
• Blobel, C. P., Wolfsberg, T. G., Turch, C. W., Myles, D. G., Primakoff, P. and White, J. M., 1992, A potential fusion peptide and an integrin ligand domain in a protein active in sperm- egg fusion. Nature, 356, 248 - 252.
   PubMed Web of Science ®Google Scholar
• Byler, D. M. and Susi, H., 1986, Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers, 25, 469 - 487.
   PubMed Web of Science ®Google Scholar
• Chen, H. and Sampson, N. S., 1999, Mediation of sperm- egg fusion: evidence that mouse egg alpha6b1 integrin is the receptor for sperm fertilinb. Chemical Biology, 6, 1 - 10.
   Google Scholar
• Chen, M. S., Almeida, E. A. C., Huovila, A.-P. J., Takahashi, Y., Shaw, L. M., Mercurio, A. M. and White, J. M., 1999, Evidence that distinct states of the integrin 61 interact with laminin and an ADAM. Journal of Cell Biology, 144, 549 - 561.
   Google Scholar
• Cho, C. H., Bunch, D. O., Faure, J. E., Goulding, E. H., Eddy, E. M., Primakoff, P., and Myles, D. G., 1998, Fertilization defects in sperm from mice lacking fertilin beta. Science, 281, 1857 - 1859.
   PubMed Web of Science ®Google Scholar
• Cowan, A. E. and Myles, D. G., 1993, Biogenesis of surface domains during spermiogenesis in the guinea pig. Developmental Biology, 155, 124 - 133.
   Google Scholar
• Cowan, A. E., Myles, D. G. and Koppel, D. E., 1987, Lateral diffusion of the PH-20 protein on guinea pig sperm: evidence that barriers to diffusion maintain plasma membrane domains in mammalian sperm. Journal of Cell Biology, 104, 917 - 923.
   Google Scholar
• Evans, J. P., Kopf, G. S. and Schultz, R. M., 1997a, Characterization of the binding of recombinant mouse sperm fertilin beta subunit to mouse eggs: evidence for adhesive activity via an egg beta 1 integrin-mediated interaction. Developmental Biology, 187, 79 - 83.
   Google Scholar
• Evans, J. P., Schultz, R. M. and Kopf, G. S., 1997b, Characterization of the binding of recombinant mouse sperm fertilin alpha subunit to mouse eggs: evidence for function as a cell adhesion molecule in sperm- egg binding. Developmental Biology, 187, 94 - 106.
   Google Scholar
• Gadella, B. M., Lopes Cardozo, M., van Golde, L. M., Colenbrander, B. and Gadella, T. W., 1995, Glycolipid migration from the apical to the equatorial subdomains of the sperm head plasma membrane precedes the acrosome reaction. Journal of Cell Science, 108, 935 - 946.
   PubMed Web of Science ®Google Scholar
• Golding, C. A. and O’Shea, P., 1995, The interactions of signal sequences with membranes. Biochemical Society Transactions, 23, 971 - 976.
   PubMedGoogle Scholar
• Golding, C. A., Senior, S., Wilson, M. T. and O’Shea, P., 1996, Time resolution of binding and membrane insertion of a mitochondrial signal peptide: correlation with structural changes and evidence for cooperativity. Biochemistry, 35, 10931- 10937.
   Google Scholar
• Harrison, R. A., Ashworth, P. J. and Miller, N. G., 1996, Bicarbonate/ CO2, an effector of capacitation, induces a rapid and reversible change in the lipid architecture of boar sperm plasma membranes. Molecular Reproduction and Development, 45, 378 - 391.
   PubMed Web of Science ®Google Scholar
• Hope, M. J., Bally, M. B., Webb, G. and Cullis, P. R., 1985, Production of large unilamellar vesicles by a rapid extrusion procedure. Characterisation of size distribution, trapped volume and ability to maintain a membrane potential. Biochimica et Biophysica Acta, 812, 55 - 65.
   PubMed Web of Science ®Google Scholar
• Huovila, A,-P., Almeida, E. A. C. and White, J., 1996, ADAMS and cell fusion. Current Opinion in Cell Biology, 8, 692 - 699.
   Google Scholar
• Jones, R., Shalgi, R., Hoyland, J. and Phillips, D. M., 1990, Topographical rearrangement of a plasma - membrane antigen during capacitation of rat spermatozoa in vitro. Developmenal Biology, 139, 349 - 362.
   Google Scholar
• Martin, I. and Ruysschaert, J.-M., 1997, Comparison of lipid vesicle fusion induced by the putative fusion peptide of fertilin (a protein active in sperm- egg fusion) and the NH2-terminal domain of the HIV2 gp41. FEBS Letters, 405, 351 - 355.
   Google Scholar
• Martin, I., Epand, R. M. and Ruysschaert, J. M., 1998, Structural properties of the putative fusion peptide of fertilin, a protein active in sperm- egg fusion, upon interaction with the lipid bilayer. Biochemistry, 37, 17030- 17039.
   Google Scholar
• Muga, A., Neugebauer, W., Tomoko, H. and Surewicz, W. K., 1994, Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm- egg fusion. Biochemistry, 33, 4444- 4448.
   PubMed Web of Science ®Google Scholar
• Myles, D. G. and Primakoff, P., 1984, Localized surface antigens of guinea pig sperm migrate to new regions prior to fertilization. Journal of Cell Biology, 99, 1634- 1641.
   PubMedGoogle Scholar
• Myles, D. G. and Primakoff, P., 1997, Why did the sperm cross the cumulus? To get to the oocyte. Functions of the sperm surface proteins PH-20 and fertilin in arriving at, and fusing with, the egg. Biological Reproduction, 56, 320 - 327.
   Google Scholar
• Niidome, T., Kimura, M., Chiba, T., Ohmori, N., Mihara, H. and Aoyagi, H., 1997, Membrane interaction of synthetic peptides related to the putative fusogenic region of PH-30 alpha, a protein in sperm- egg fusion. Journal of Peptide Research, 49, 563 - 569.
   Google Scholar
• Perry, A. C. F., Jones, R. and Hall, L., 1995, Analysis of transcripts encoding novel members of the mammalian metalloprotease-like, disintegrin-like, cysteine-rich (mdc) protein family and their expression in reproductive and nonreproductive monkey tissues. Biochemical Journal, 312, 239 - 244.
   PubMedGoogle Scholar
• Phelps, B. M., Primakoff, P., Koppel, D. E., Low, M. G. and Myles, D. G., 1988, Restricted lateral diffusion of ph-20, a pi-anchored sperm membrane-protein. Science, 240, 1780- 1782.
   Google Scholar
• Primakoff, P. and Myles, D. G., 1983, A map of the guinea pig sperm surface constructed with monoclonal antibodies. Developmental Biology, 98, 417 - 428.
   PubMed Web of Science ®Google Scholar
• Primakoff, P., Hyatt, H. and Tredick-Kline, J., 1987, Identification and purification of a sperm surface protein with a potential role in sperm- egg fusion. Journal of Cell Biology, 104, 141 - 149.
   PubMed Web of Science ®Google Scholar
• Snell, W. J. and White, J. M., 1996, The molecules of mammalian fertilization. Cell, 85, 629 - 637.
   PubMedGoogle Scholar
• Wall, J., Ayoub, F. and O’Shea, P., 1995a, The interactions of macromolecules with the mammalian cell surface. Journal of Cell Science, 108, 2673- 2682.
   Google Scholar
• Wall, J., Golding, C. A., Van Veen, M. and O’Shea, P., 1995b, The use of fluoresceinphosphatidylethanolamine (FPE) as a real-time probe for peptide-membrane interactions. Molecular Membrane Biology, 12, 183 - 192.
   PubMed Web of Science ®Google Scholar
• Wassarman, P. M., 1995, Towards the molecular mechanisms for gamete adhesion and fusion during mammalian fertilization. Current Opinion in Cell Biology, 7, 658 - 664.
   Google Scholar
• White, J. M., 1992, Membrane-fusion. Science, 258, 917 - 924.
   PubMed Web of Science ®Google Scholar
• Wolfe, C. Cladera, J. and O’Shea,P., 1998, Amino acid sequences which promote and prevent the binding and membrane insertion of surface-active peptides: comparison of melittin and promelittin. Molecular Membrane Biology, 15, 221 - 227.
   Google Scholar
• Wolfsberg, T. G., Primakoff, P., Myles, D. G. and White, J. M., 1995a, ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. Journal of Cell Biology, 131, 275 - 278.
   PubMed Web of Science ®Google Scholar
• Wolfsberg, T. G., Straight, P. D., Gerene, R. L., Huovila, A.-P. J., Primakoff, P., Myles, D. G. and White, J. M., 1995b, ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metallopro- tease domain. Developmental Biology, 169, 378 - 383.
   PubMed Web of Science ®Google Scholar