메뉴 건너뛰기




Volumn 309, Issue 2, 2007, Pages 236-244

Complexin I is required for mammalian sperm acrosomal exocytosis

Author keywords

Acrosome reaction; Calcium; Egg; Extracellular matrix; Fertilization; Membrane fusion; Oocyte; Secretion; SNARE; Zona pellucida

Indexed keywords

CALCIUM IONOPHORE; CELL MEMBRANE PROTEIN; COMPLEXIN I; COMPLEXIN II; SNARE PROTEIN; UNCLASSIFIED DRUG;

EID: 34548391033     PISSN: 00121606     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ydbio.2007.07.009     Document Type: Article
Times cited : (32)

References (51)
  • 1
    • 0014123988 scopus 로고
    • Membrane vesiculation as a feature of the mammalian acrosome reaction
    • Barros C., Bedford J.M., Franklin L.E., and Austin C.R. Membrane vesiculation as a feature of the mammalian acrosome reaction. J. Cell Biol. 34 (1967) C1-C5
    • (1967) J. Cell Biol. , vol.34
    • Barros, C.1    Bedford, J.M.2    Franklin, L.E.3    Austin, C.R.4
  • 2
    • 0026778460 scopus 로고
    • Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett M.K., Calakos N., and Scheller R.H. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 257 (1992) 255-259
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 4
    • 0031770661 scopus 로고    scopus 로고
    • Cyclodextrin removes cholesterol from mouse sperm and induces capacitation in a protein-free medium
    • Choi Y.H., and Toyoda Y. Cyclodextrin removes cholesterol from mouse sperm and induces capacitation in a protein-free medium. Biol. Reprod. 59 (1998) 1328-1333
    • (1998) Biol. Reprod. , vol.59 , pp. 1328-1333
    • Choi, Y.H.1    Toyoda, Y.2
  • 5
    • 0032555126 scopus 로고    scopus 로고
    • Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly
    • Fasshauer D., Eliason W.K., Brunger A.T., and Jahn R. Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. Biochemistry 37 (1998) 10354-10362
    • (1998) Biochemistry , vol.37 , pp. 10354-10362
    • Fasshauer, D.1    Eliason, W.K.2    Brunger, A.T.3    Jahn, R.4
  • 6
    • 0026090087 scopus 로고
    • Ultrastructural analysis of the acrosome reaction in a population of single guinea pig sperm
    • Flaherty S.P., and Olson G.E. Ultrastructural analysis of the acrosome reaction in a population of single guinea pig sperm. Anat. Rec. 229 (1991) 186-194
    • (1991) Anat. Rec. , vol.229 , pp. 186-194
    • Flaherty, S.P.1    Olson, G.E.2
  • 7
    • 0014857747 scopus 로고
    • The acrosomal region and the acrosome reaction in sperm of the golden hamster
    • Franklin L.E., Barros C., and Fussell E.N. The acrosomal region and the acrosome reaction in sperm of the golden hamster. Biol. Reprod. 3 (1970) 180-200
    • (1970) Biol. Reprod. , vol.3 , pp. 180-200
    • Franklin, L.E.1    Barros, C.2    Fussell, E.N.3
  • 8
    • 2342586760 scopus 로고    scopus 로고
    • Differential messenger RNA expression of complexins in mouse brain
    • Freeman W., and Morton A.J. Differential messenger RNA expression of complexins in mouse brain. Brain Res. Bull. 63 (2004) 33-44
    • (2004) Brain Res. Bull. , vol.63 , pp. 33-44
    • Freeman, W.1    Morton, A.J.2
  • 9
    • 26844542155 scopus 로고    scopus 로고
    • Identification of neuropeptides from the decapod crustacean sinus glands using nanoscale liquid chromatography tandem mass spectrometry
    • Fu Q., Goy M.F., and Li L. Identification of neuropeptides from the decapod crustacean sinus glands using nanoscale liquid chromatography tandem mass spectrometry. Biochem. Biophys. Res. Commun. 337 (2005) 765-778
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 765-778
    • Fu, Q.1    Goy, M.F.2    Li, L.3
  • 10
    • 33746319639 scopus 로고    scopus 로고
    • A clamping mechanism involved in SNARE-dependent exocytosis
    • Giraudo C.G., Eng W.S., Melia T.J., and Rothman J.E. A clamping mechanism involved in SNARE-dependent exocytosis. Science 313 (2006) 676-680
    • (2006) Science , vol.313 , pp. 676-680
    • Giraudo, C.G.1    Eng, W.S.2    Melia, T.J.3    Rothman, J.E.4
  • 11
    • 0141618325 scopus 로고    scopus 로고
    • Complexin II is essential for normal neurological function in mice
    • Glynn D., Bortnick R.A., and Morton A.J. Complexin II is essential for normal neurological function in mice. Hum. Mol. Genet. 12 (2003) 2431-2448
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2431-2448
    • Glynn, D.1    Bortnick, R.A.2    Morton, A.J.3
  • 12
    • 26444619475 scopus 로고    scopus 로고
    • Profound ataxia in complexin I knockout mice masks a complex phenotype that includes exploratory and habituation deficits
    • Glynn D., Drew C.J., Reim K., Brose N., and Morton A.J. Profound ataxia in complexin I knockout mice masks a complex phenotype that includes exploratory and habituation deficits. Hum. Mol. Genet. 14 (2005) 2369-2385
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2369-2385
    • Glynn, D.1    Drew, C.J.2    Reim, K.3    Brose, N.4    Morton, A.J.5
  • 13
    • 33847212515 scopus 로고    scopus 로고
    • Early motor development is abnormal in complexin 1 knockout mice
    • Glynn D., Sizemore R.J., and Morton A.J. Early motor development is abnormal in complexin 1 knockout mice. Neurobiol. Dis. 25 (2007) 483-495
    • (2007) Neurobiol. Dis. , vol.25 , pp. 483-495
    • Glynn, D.1    Sizemore, R.J.2    Morton, A.J.3
  • 14
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly
    • Hayashi T., McMahon H., Yamasaki S., Binz T., Hata Y., Sudhof T.C., and Niemann H. Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J. 13 (1994) 5051-5061
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1    McMahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Sudhof, T.C.6    Niemann, H.7
  • 16
    • 0036136446 scopus 로고    scopus 로고
    • Synaptotagmin VIII is localized to the mouse sperm head and may function in acrosomal exocytosis
    • Hutt D.M., Cardullo R.A., Baltz J.M., and Ngsee J.K. Synaptotagmin VIII is localized to the mouse sperm head and may function in acrosomal exocytosis. Biol. Reprod. 66 (2002) 50-56
    • (2002) Biol. Reprod. , vol.66 , pp. 50-56
    • Hutt, D.M.1    Cardullo, R.A.2    Baltz, J.M.3    Ngsee, J.K.4
  • 17
    • 20144379204 scopus 로고    scopus 로고
    • Synaptotagmin VI and VIII and syntaxin 2 are essential for the mouse sperm acrosome reaction
    • Hutt D.M., Baltz J.M., and Ngsee J.K. Synaptotagmin VI and VIII and syntaxin 2 are essential for the mouse sperm acrosome reaction. J. Biol. Chem. 280 (2005) 20197-20203
    • (2005) J. Biol. Chem. , vol.280 , pp. 20197-20203
    • Hutt, D.M.1    Baltz, J.M.2    Ngsee, J.K.3
  • 19
    • 0033762859 scopus 로고    scopus 로고
    • Localization of a syntaxin isoform, syntaxin 2, to the acrosomal region of rodent spermatozoa
    • Katafuchi K., Mori T., Toshimori K., and Iida H. Localization of a syntaxin isoform, syntaxin 2, to the acrosomal region of rodent spermatozoa. Mol. Reprod. Dev. 57 (2000) 375-383
    • (2000) Mol. Reprod. Dev. , vol.57 , pp. 375-383
    • Katafuchi, K.1    Mori, T.2    Toshimori, K.3    Iida, H.4
  • 20
    • 0033061672 scopus 로고    scopus 로고
    • Simple histochemical stain for acrosomes on sperm from several species
    • Larson J.L., and Miller D.J. Simple histochemical stain for acrosomes on sperm from several species. Mol. Reprod. Dev. 52 (1999) 445-449
    • (1999) Mol. Reprod. Dev. , vol.52 , pp. 445-449
    • Larson, J.L.1    Miller, D.J.2
  • 21
    • 0030728461 scopus 로고    scopus 로고
    • Sperm from β1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reaction and penetrate the zona pellucida poorly
    • Lu Q., and Shur B.D. Sperm from β1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reaction and penetrate the zona pellucida poorly. Development 124 (1997) 4121-4131
    • (1997) Development , vol.124 , pp. 4121-4131
    • Lu, Q.1    Shur, B.D.2
  • 22
    • 0028880456 scopus 로고
    • Complexins: cytosolic proteins that regulate SNAP receptor function
    • McMahon H.T., Missler M., Li C., and Sudhof T.C. Complexins: cytosolic proteins that regulate SNAP receptor function. Cell 83 (1995) 111-119
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.T.1    Missler, M.2    Li, C.3    Sudhof, T.C.4
  • 23
    • 9644289338 scopus 로고    scopus 로고
    • The sperm, a neuron with a tail: 'neuronal' receptors in mammalian sperm
    • Meizel S. The sperm, a neuron with a tail: 'neuronal' receptors in mammalian sperm. Biol. Rev. Camb. Philos. Soc. 79 (2004) 713-732
    • (2004) Biol. Rev. Camb. Philos. Soc. , vol.79 , pp. 713-732
    • Meizel, S.1
  • 24
    • 0034730154 scopus 로고    scopus 로고
    • Calcium-triggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N-ethylmaleimide-sensitive factor
    • Michaut M., Tomes C.N., De Blas G., Yunes R., and Mayorga L.S. Calcium-triggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N-ethylmaleimide-sensitive factor. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 9996-10001
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9996-10001
    • Michaut, M.1    Tomes, C.N.2    De Blas, G.3    Yunes, R.4    Mayorga, L.S.5
  • 25
    • 0033607182 scopus 로고    scopus 로고
    • Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs
    • Nickel W., Weber T., McNew J.A., Parlati F., Sollner T.H., and Rothman J.E. Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 12571-12576
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 12571-12576
    • Nickel, W.1    Weber, T.2    McNew, J.A.3    Parlati, F.4    Sollner, T.H.5    Rothman, J.E.6
  • 26
    • 0035337709 scopus 로고    scopus 로고
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta
    • Nishimura H., Cho C., Branciforte D.R., Myles D.G., and Primakoff P. Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta. Dev. Biol. 233 (2001) 204-213
    • (2001) Dev. Biol. , vol.233 , pp. 204-213
    • Nishimura, H.1    Cho, C.2    Branciforte, D.R.3    Myles, D.G.4    Primakoff, P.5
  • 27
    • 34547125812 scopus 로고    scopus 로고
    • Identification of an ADAM2/ADAM3 complex on the surface of mouse testicular germ cells and cauda epididymal sperm
    • Nishimura H., Myles D.G., and Primakoff P. Identification of an ADAM2/ADAM3 complex on the surface of mouse testicular germ cells and cauda epididymal sperm. J. Biol. Chem. 282 (2007) 17900-17907
    • (2007) J. Biol. Chem. , vol.282 , pp. 17900-17907
    • Nishimura, H.1    Myles, D.G.2    Primakoff, P.3
  • 28
    • 0030810986 scopus 로고    scopus 로고
    • Regulation of membrane stability and the acrosome reaction in mammalian sperm
    • Nolan J.P., and Hammerstedt R.H. Regulation of membrane stability and the acrosome reaction in mammalian sperm. FASEB J. 11 (1997) 670-682
    • (1997) FASEB J. , vol.11 , pp. 670-682
    • Nolan, J.P.1    Hammerstedt, R.H.2
  • 29
    • 0024828306 scopus 로고
    • The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations
    • Oyler G.A., Higgins G.A., Hart R.A., Battenberg E., Billingsley M., Bloom F.E., and Wilson M.C. The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations. J. Cell Biol. 109 (1989) 3039-3052
    • (1989) J. Cell Biol. , vol.109 , pp. 3039-3052
    • Oyler, G.A.1    Higgins, G.A.2    Hart, R.A.3    Battenberg, E.4    Billingsley, M.5    Bloom, F.E.6    Wilson, M.C.7
  • 30
    • 0034733545 scopus 로고    scopus 로고
    • Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions
    • Pabst S., Hazzard J.W., Antonin W., Sudhof T.C., Jahn R., Rizo J., and Fasshauer D. Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions. J. Biol. Chem. 275 (2000) 19808-19818
    • (2000) J. Biol. Chem. , vol.275 , pp. 19808-19818
    • Pabst, S.1    Hazzard, J.W.2    Antonin, W.3    Sudhof, T.C.4    Jahn, R.5    Rizo, J.6    Fasshauer, D.7
  • 31
    • 0037040873 scopus 로고    scopus 로고
    • Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis
    • Pabst S., Margittai M., Vainius D., Langen R., Jahn R., and Fasshauer D. Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis. J. Biol. Chem. 277 (2002) 7838-7848
    • (2002) J. Biol. Chem. , vol.277 , pp. 7838-7848
    • Pabst, S.1    Margittai, M.2    Vainius, D.3    Langen, R.4    Jahn, R.5    Fasshauer, D.6
  • 32
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin D.J., Hojrup P., and Bleasby A.J. Rapid identification of proteins by peptide-mass fingerprinting. Curr. Biol. 3 (1993) 327-332
    • (1993) Curr. Biol. , vol.3 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 37
    • 0018502644 scopus 로고
    • An ultrastructural study of epididymal mouse spermatozoa binding to zonae pellucidae in vitro: sequential relationship to the acrosome reaction
    • Saling P.M., Sowinski J., and Storey B.T. An ultrastructural study of epididymal mouse spermatozoa binding to zonae pellucidae in vitro: sequential relationship to the acrosome reaction. J. Exp. Zool. 209 (1979) 229-238
    • (1979) J. Exp. Zool. , vol.209 , pp. 229-238
    • Saling, P.M.1    Sowinski, J.2    Storey, B.T.3
  • 39
    • 0038050215 scopus 로고    scopus 로고
    • Regulated exocytosis and SNARE function (Review)
    • Sollner T.H. Regulated exocytosis and SNARE function (Review). Mol. Membr. Biol. 20 (2003) 209-220
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 209-220
    • Sollner, T.H.1
  • 43
    • 33748605056 scopus 로고    scopus 로고
    • A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis
    • Tang J., Maximov A., Shin O.H., Dai H., Rizo J., and Sudhof T.C. A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell 126 (2006) 1175-1187
    • (2006) Cell , vol.126 , pp. 1175-1187
    • Tang, J.1    Maximov, A.2    Shin, O.H.3    Dai, H.4    Rizo, J.5    Sudhof, T.C.6
  • 46
    • 0033613867 scopus 로고    scopus 로고
    • Cholesterol efflux-mediated signal transduction in mammalian sperm. β-Cyclodextrins initiate transmembrane signaling leading to an increase in protein tyrosine phosphorylation and capacitation
    • Visconti P.E., Galantino-Homer H., Ning X., Moore G.D., Valenzuela J.P., Jorgez C.J., Alvarez J.G., and Kopf G.S. Cholesterol efflux-mediated signal transduction in mammalian sperm. β-Cyclodextrins initiate transmembrane signaling leading to an increase in protein tyrosine phosphorylation and capacitation. J. Biol. Chem. 274 (1999) 3235-3242
    • (1999) J. Biol. Chem. , vol.274 , pp. 3235-3242
    • Visconti, P.E.1    Galantino-Homer, H.2    Ning, X.3    Moore, G.D.4    Valenzuela, J.P.5    Jorgez, C.J.6    Alvarez, J.G.7    Kopf, G.S.8
  • 47
    • 0022642621 scopus 로고
    • Relationship between calcium binding sites and membrane fusion during the acrosome reaction induced by ionophore in ram spermatozoa
    • Watson P.F., and Plummer J.M. Relationship between calcium binding sites and membrane fusion during the acrosome reaction induced by ionophore in ram spermatozoa. J. Exp. Zool. 238 (1986) 113-118
    • (1986) J. Exp. Zool. , vol.238 , pp. 113-118
    • Watson, P.F.1    Plummer, J.M.2
  • 49
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E., and Neill J.D. (Eds), Raven Press, New York
    • Yanagimachi R. Mammalian fertilization. In: Knobil E., and Neill J.D. (Eds). Physiology of Reproduction. 2nd Edition (1994), Raven Press, New York A189-A317
    • (1994) Physiology of Reproduction. 2nd Edition
    • Yanagimachi, R.1
  • 50
    • 0034106739 scopus 로고    scopus 로고
    • Rab3A triggers the acrosome reaction in permeabilized human spermatozoa
    • Yunes R., Michaut M., Tomes C., and Mayorga L.S. Rab3A triggers the acrosome reaction in permeabilized human spermatozoa. Biol. Reprod. 62 (2000) 1084-1089
    • (2000) Biol. Reprod. , vol.62 , pp. 1084-1089
    • Yunes, R.1    Michaut, M.2    Tomes, C.3    Mayorga, L.S.4
  • 51
    • 34247566489 scopus 로고    scopus 로고
    • Dynamin 2 associates with complexins and is found in the acrosomal region of mammalian sperm
    • Zhao L., Shi X., Li L., and Miller D.J. Dynamin 2 associates with complexins and is found in the acrosomal region of mammalian sperm. Mol. Reprod. Dev. 74 (2007) 750-757
    • (2007) Mol. Reprod. Dev. , vol.74 , pp. 750-757
    • Zhao, L.1    Shi, X.2    Li, L.3    Miller, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.