메뉴 건너뛰기




Volumn 63, Issue 3, 2002, Pages 366-375

Valosine containing protein is a substrate of cAMP - Activated boar sperm tyrosine kinase

Author keywords

Capacitation; Gamete biology; Phosphorylation; Spermatozoa

Indexed keywords

CYCLIC AMP; PHOSPHOTYROSINE; PROTEIN; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG; VALOSINE CONTAINING PROTEIN;

EID: 0036836539     PISSN: 1040452X     EISSN: None     Source Type: Journal    
DOI: 10.1002/mrd.10156     Document Type: Article
Times cited : (19)

References (45)
  • 1
    • 0343627933 scopus 로고    scopus 로고
    • Possible redox regulation of sperm motility activation
    • Aitken RJ. 2000. Possible redox regulation of sperm motility activation. J Androl 21:491-496.
    • (2000) J Androl , vol.21 , pp. 491-496
    • Aitken, R.J.1
  • 2
    • 0031890532 scopus 로고    scopus 로고
    • A novel signal transduction cascade in capacitating human spermatozoa characterized by a redox-regulated, cAMP mediated induction of tyrosine phosphorylation
    • Aitken RJ, Harkiss D, Knox W, Paterson M, Irvine DS. 1998. A novel signal transduction cascade in capacitating human spermatozoa characterized by a redox-regulated, cAMP mediated induction of tyrosine phosphorylation. J Cell Sci 111:645-656.
    • (1998) J Cell Sci , vol.111 , pp. 645-656
    • Aitken, R.J.1    Harkiss, D.2    Knox, W.3    Paterson, M.4    Irvine, D.S.5
  • 3
    • 0024444633 scopus 로고
    • Identification of proteins cross-reactive to phosphotyrosine antibodies and of a tyrosine kinase activity in boar spermatozoa
    • Berruti G, Martegani E. 1989. Identification of proteins cross-reactive to phosphotyrosine antibodies and of a tyrosine kinase activity in boar spermatozoa. J Cell Sci 93:667-674.
    • (1989) J Cell Sci , vol.93 , pp. 667-674
    • Berruti, G.1    Martegani, E.2
  • 4
    • 0026558614 scopus 로고
    • Tyrosine protein kinase in boar spermatozoa: Identification and partial characterization
    • Berruti G, Porzio S. 1992. Tyrosine protein kinase in boar spermatozoa: Identification and partial characterization. Biochim Biophys Acta 1118:149-154.
    • (1992) Biochim Biophys Acta , vol.1118 , pp. 149-154
    • Berruti, G.1    Porzio, S.2
  • 5
    • 0030602027 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation in human sperm by a calcium/calmodulin-dependent mechanism: Identification of A kinase anchor proteins as major substrates for tyrosine phosphorylation
    • Carrera A, Moos J, Ning XP, Gerton GL, Tesarik J, Kopf GS, Moss SB. 1996. Regulation of protein tyrosine phosphorylation in human sperm by a calcium/calmodulin-dependent mechanism: Identification of A kinase anchor proteins as major substrates for tyrosine phosphorylation. Dev Biol 180:284-296.
    • (1996) Dev Biol , vol.180 , pp. 284-296
    • Carrera, A.1    Moos, J.2    Ning, X.P.3    Gerton, G.L.4    Tesarik, J.5    Kopf, G.S.6    Moss, S.B.7
  • 6
    • 0034907973 scopus 로고    scopus 로고
    • Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation
    • Dai RM, Li CC. 2001. Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat Cell Biol 3:740-744.
    • (2001) Nat Cell Biol , vol.3 , pp. 740-744
    • Dai, R.M.1    Li, C.C.2
  • 7
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase Co-purified with Ikappa-Balpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha
    • Dai RM, Chen E, Longo DL, Gorbea CM, Li CC. 1998. Involvement of valosin-containing protein, an ATPase Co-purified with Ikappa-Balpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha. J Biol Chem 273:3562-3573.
    • (1998) J Biol Chem , vol.273 , pp. 3562-3573
    • Dai, R.M.1    Chen, E.2    Longo, D.L.3    Gorbea, C.M.4    Li, C.C.5
  • 9
    • 0027510718 scopus 로고
    • Cyclic AMP-dependent phosphorylation of epididymal mouse sperm proteins during capacitation in vitro: Identification of an M(r) 95,000 phosphotyrosine-containing protein
    • Duncan AE, Fraser LR. 1993. Cyclic AMP-dependent phosphorylation of epididymal mouse sperm proteins during capacitation in vitro: Identification of an M(r) 95,000 phosphotyrosine-containing protein. J Reprod Fertil 97:287-299.
    • (1993) J Reprod Fertil , vol.97 , pp. 287-299
    • Duncan, A.E.1    Fraser, L.R.2
  • 10
    • 0028237892 scopus 로고
    • Biochemical characterization of valosin-containing protein, a protein tyrosine kinase substrate in hematopoietic cells
    • Egerton M, Samelson LE. 1994. Biochemical characterization of valosin-containing protein, a protein tyrosine kinase substrate in hematopoietic cells. J Biol Chem 269:11435-11441.
    • (1994) J Biol Chem , vol.269 , pp. 11435-11441
    • Egerton, M.1    Samelson, L.E.2
  • 11
    • 0026660330 scopus 로고
    • VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation
    • Egerton M, Ashe OR, Chen D, Druker BJ, Burgess WH, Samelson LE. 1992. VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation. EMBO J 11:3533-3540.
    • (1992) EMBO J , vol.11 , pp. 3533-3540
    • Egerton, M.1    Ashe, O.R.2    Chen, D.3    Druker, B.J.4    Burgess, W.H.5    Samelson, L.E.6
  • 12
  • 13
    • 0034902491 scopus 로고    scopus 로고
    • Capacitation dependent activation of tyrosine phosphorylation generates two sperm head plasma membrane proteins with high primary binding affinity for the zona pellucida
    • Flesch FM, Wijnand E, van De Lest CH, Colenbrander B, van Golde LM, Gadella BM. 2001. Capacitation dependent activation of tyrosine phosphorylation generates two sperm head plasma membrane proteins with high primary binding affinity for the zona pellucida. Mol Reprod Dev 60:107-115.
    • (2001) Mol Reprod Dev , vol.60 , pp. 107-115
    • Flesch, F.M.1    Wijnand, E.2    Van De Lest, C.H.3    Colenbrander, B.4    Van Golde, L.M.5    Gadella, B.M.6
  • 14
    • 0031049037 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′5′-monophosphate-dependent pathway
    • Galantino-Homer HL, Visconti PE, Kopf GS. 1997. Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′5′-monophosphate-dependent pathway. Biol Reprod 56:707-719.
    • (1997) Biol Reprod , vol.56 , pp. 707-719
    • Galantino-Homer, H.L.1    Visconti, P.E.2    Kopf, G.S.3
  • 15
    • 0033934923 scopus 로고    scopus 로고
    • Progesterone-induced calcium influx in cynomolgus monkey (Macaca fascicularis) spermatozoa
    • Gwathmey T, Blackmore PF, Mahony MC. 2000. Progesterone-induced calcium influx in cynomolgus monkey (Macaca fascicularis) spermatozoa. J Androl 21:534-540.
    • (2000) J Androl , vol.21 , pp. 534-540
    • Gwathmey, T.1    Blackmore, P.F.2    Mahony, M.C.3
  • 16
    • 0031687185 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation in boar sperm through a cAMP-dependent pathway
    • Kalab P, Peknicova J, Geussova G, Moos J. 1998. Regulation of protein tyrosine phosphorylation in boar sperm through a cAMP-dependent pathway. Mol Reprod Dev 51:304-314.
    • (1998) Mol Reprod Dev , vol.51 , pp. 304-314
    • Kalab, P.1    Peknicova, J.2    Geussova, G.3    Moos, J.4
  • 17
    • 0029030462 scopus 로고
    • Mouse sperm adenylyl cyclase: General properties and regulation by the zona pellucida
    • Leclerc P, Kopf GS. 1995. Mouse sperm adenylyl cyclase: General properties and regulation by the zona pellucida. Biol Reprod 52: 1227-1233.
    • (1995) Biol Reprod , vol.52 , pp. 1227-1233
    • Leclerc, P.1    Kopf, G.S.2
  • 18
    • 0029792629 scopus 로고    scopus 로고
    • Cyclic adenosine 3′,5′ monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility
    • Leclerc P, de Lamirande E, Gagnon C. 1996. Cyclic adenosine 3′,5′ monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility. Biol Reprod 55:684-692.
    • (1996) Biol Reprod , vol.55 , pp. 684-692
    • Leclerc, P.1    De Lamirande, E.2    Gagnon, C.3
  • 19
    • 0035027048 scopus 로고    scopus 로고
    • Impact of epididymal maturation on the tyrosine phosphorylation patterns exhibited by rat spermatozoa
    • Lewis B, Aitken RJ. 2001. Impact of epididymal maturation on the tyrosine phosphorylation patterns exhibited by rat spermatozoa. Biol Reprod 64:1545-1556.
    • (2001) Biol Reprod , vol.64 , pp. 1545-1556
    • Lewis, B.1    Aitken, R.J.2
  • 20
    • 0029789196 scopus 로고    scopus 로고
    • Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa
    • Luconi M, Krausz C, Forti G, Baldi E. 1996. Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa. Biol Reprod 55:207-216.
    • (1996) Biol Reprod , vol.55 , pp. 207-216
    • Luconi, M.1    Krausz, C.2    Forti, G.3    Baldi, E.4
  • 21
    • 0031578796 scopus 로고    scopus 로고
    • Identification of the regions of porcine VCP preventing its function in Saccharomyces cerevisiae
    • Madeo F, Schlauer J, Frohlich KU. 1997. Identification of the regions of porcine VCP preventing its function in Saccharomyces cerevisiae. Gene 204:145-151.
    • (1997) Gene , vol.204 , pp. 145-151
    • Madeo, F.1    Schlauer, J.2    Frohlich, K.U.3
  • 22
    • 0031932987 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p
    • Madeo F, Schlauer J, Zischka H, Mecke D, Frohlich KU. 1998. Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p. Mol Biol Cell 9:131-141.
    • (1998) Mol Biol Cell , vol.9 , pp. 131-141
    • Madeo, F.1    Schlauer, J.2    Zischka, H.3    Mecke, D.4    Frohlich, K.U.5
  • 24
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and np14 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer HH, Shorter JG, Seemann J, Pappin D, Warren G. 2000. A complex of mammalian ufd1 and np14 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J 19:2181-2192.
    • (2000) EMBO J , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 25
    • 0020120095 scopus 로고
    • Cold-sensitive cell-division-cycle mutants of yeast: Isolation, properties, and pseudoreversion studies
    • Moir D, Stewart SE, Osmond BC, Botstein D. 1982. Cold-sensitive cell-division-cycle mutants of yeast: Isolation, properties, and pseudoreversion studies. Genetics 100:547-563.
    • (1982) Genetics , vol.100 , pp. 547-563
    • Moir, D.1    Stewart, S.E.2    Osmond, B.C.3    Botstein, D.4
  • 26
    • 0032732658 scopus 로고    scopus 로고
    • Regulation of human sperm capacitation by a cholesterol efflux-stimulated signal transduction pathway leading to protein kinase A-mediated up-regulation of protein tyrosine phosphorylation
    • Osheroff JE, Visconti PE, Valenzuela JP, Travis AJ, Alvarez J, Kopf GS. 1999. Regulation of human sperm capacitation by a cholesterol efflux-stimulated signal transduction pathway leading to protein kinase A-mediated up-regulation of protein tyrosine phosphorylation. Mol Hum Reprod 5:1017-1026.
    • (1999) Mol Hum Reprod , vol.5 , pp. 1017-1026
    • Osheroff, J.E.1    Visconti, P.E.2    Valenzuela, J.P.3    Travis, A.J.4    Alvarez, J.5    Kopf, G.S.6
  • 29
    • 0028930157 scopus 로고
    • Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system
    • Rabouille C, Misteli T, Watson R, Warren G. 1995. Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system. J Cell Biol 129:605-618.
    • (1995) J Cell Biol , vol.129 , pp. 605-618
    • Rabouille, C.1    Misteli, T.2    Watson, R.3    Warren, G.4
  • 30
    • 0034651727 scopus 로고    scopus 로고
    • Membrane fusion proteins are required for oskar mRNA localization in the Drosophila egg chamber
    • Ruden DM, Sollars V, Wang X, Mori D, Alterman M, Lu X. 2000. Membrane fusion proteins are required for oskar mRNA localization in the Drosophila egg chamber. Dev Biol 218:314-325.
    • (2000) Dev Biol , vol.218 , pp. 314-325
    • Ruden, D.M.1    Sollars, V.2    Wang, X.3    Mori, D.4    Alterman, M.5    Lu, X.6
  • 31
    • 0027943759 scopus 로고
    • Tyrosine phosphorylation of VCP, the mammalian homologue of the Saccharomyces cerevisiae CDC48 protein, is unusually sensitive to stimulation by sodium vanadate and hydrogen peroxide
    • Schulte RJ, Campbell MA, Fischer WH, Sefton BM. 1994. Tyrosine phosphorylation of VCP, the mammalian homologue of the Saccharomyces cerevisiae CDC48 protein, is unusually sensitive to stimulation by sodium vanadate and hydrogen peroxide. J Immunol 153: 5465-5472.
    • (1994) J Immunol , vol.153 , pp. 5465-5472
    • Schulte, R.J.1    Campbell, M.A.2    Fischer, W.H.3    Sefton, B.M.4
  • 32
    • 0033024113 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation of flagellar proteins in hamster sperm hyperactivation
    • Si Y, Okuno M. 1999. Role of tyrosine phosphorylation of flagellar proteins in hamster sperm hyperactivation. Biol Reprod 61:240-246.
    • (1999) Biol Reprod , vol.61 , pp. 240-246
    • Si, Y.1    Okuno, M.2
  • 34
    • 0035012044 scopus 로고    scopus 로고
    • A putative, ubiquitin-dependent mechanism for the recognition and elimination of defective spermatozoa in the mammalian epididymis
    • Sutovsky P, Moreno R, Ramalho-Santos J, Dominko T, Thompson WE, Schatten G. 2001. A putative, ubiquitin-dependent mechanism for the recognition and elimination of defective spermatozoa in the mammalian epididymis. J Cell Sci 114:1665-1667.
    • (2001) J Cell Sci , vol.114 , pp. 1665-1667
    • Sutovsky, P.1    Moreno, R.2    Ramalho-Santos, J.3    Dominko, T.4    Thompson, W.E.5    Schatten, G.6
  • 35
    • 0034887719 scopus 로고    scopus 로고
    • Capacitation is associated with tyrosine phosphorylation and tyrosine kinase-like activity of pig sperm proteins
    • Tardif S, Dube C, Chevalier S, Bailey JL. 2001. Capacitation is associated with tyrosine phosphorylation and tyrosine kinase-like activity of pig sperm proteins. Biol Reprod 65:784-792.
    • (2001) Biol Reprod , vol.65 , pp. 784-792
    • Tardif, S.1    Dube, C.2    Chevalier, S.3    Bailey, J.L.4
  • 36
    • 0032817012 scopus 로고    scopus 로고
    • Relationship between sperm motility and the processing and tyrosine phosphorylation of two human sperm fibrous sheath proteins, pro-hAKAP82 and hAKAP82
    • Turner RM, Eriksson RL, Gerton GL, Moss SB. 1999. Relationship between sperm motility and the processing and tyrosine phosphorylation of two human sperm fibrous sheath proteins, pro-hAKAP82 and hAKAP82. Mol Hum Reprod 5:816-824.
    • (1999) Mol Hum Reprod , vol.5 , pp. 816-824
    • Turner, R.M.1    Eriksson, R.L.2    Gerton, G.L.3    Moss, S.B.4
  • 37
    • 0035030573 scopus 로고    scopus 로고
    • Protein tyrosine phosphorylation in sperm during gamete interaction in the mouse: The influence of glucose
    • Urner F, Leppens-Luisier G, Sakkas D. 2001. Protein tyrosine phosphorylation in sperm during gamete interaction in the mouse: The influence of glucose. Biol Reprod 64:1350-1357.
    • (2001) Biol Reprod , vol.64 , pp. 1350-1357
    • Urner, F.1    Leppens-Luisier, G.2    Sakkas, D.3
  • 38
    • 0034076243 scopus 로고    scopus 로고
    • A role for phosphorylation of glycogen synthase kinase-3alpha in bovine sperm motility regulation
    • Vijayaraghavan S, Mohan J, Gray H, Khatra B, Carr DW. 2000. A role for phosphorylation of glycogen synthase kinase-3alpha in bovine sperm motility regulation. Biol Reprod 62:1647-1654.
    • (2000) Biol Reprod , vol.62 , pp. 1647-1654
    • Vijayaraghavan, S.1    Mohan, J.2    Gray, H.3    Khatra, B.4    Carr, D.W.5
  • 39
    • 0031778295 scopus 로고    scopus 로고
    • Regulation of protein phosphorylation during sperm capacitation
    • Visconti PE, Kopf GS. 1998. Regulation of protein phosphorylation during sperm capacitation. Biol Reprod 59:1-6.
    • (1998) Biol Reprod , vol.59 , pp. 1-6
    • Visconti, P.E.1    Kopf, G.S.2
  • 40
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti PE, Bailey JL, Moore GD, Pan D, Olds-Clarke P, Kopf GS. 1995a. Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation. Development 121:1129-1137.
    • (1995) Development , vol.121 , pp. 1129-1137
    • Visconti, P.E.1    Bailey, J.L.2    Moore, G.D.3    Pan, D.4    Olds-Clarke, P.5    Kopf, G.S.6
  • 41
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti PE, Moore GD, Bailey JL, Leclerc P, Connors SA, Pan D, Olds-Clarke P, Kopf GS. 1995b. Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 121:1139-1150.
    • (1995) Development , vol.121 , pp. 1139-1150
    • Visconti, P.E.1    Moore, G.D.2    Bailey, J.L.3    Leclerc, P.4    Connors, S.A.5    Pan, D.6    Olds-Clarke, P.7    Kopf, G.S.8
  • 42
    • 0033570112 scopus 로고    scopus 로고
    • Cholesterol efflux-mediated signal transduction in mammalian sperm: Cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation
    • Visconti PE, Ning X, Fornes MW, Alvarez JG, Stein P, Connors SA, Kopf GS. 1999a. Cholesterol efflux-mediated signal transduction in mammalian sperm: Cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation. Dev Biol 214:429-443.
    • (1999) Dev Biol , vol.214 , pp. 429-443
    • Visconti, P.E.1    Ning, X.2    Fornes, M.W.3    Alvarez, J.G.4    Stein, P.5    Connors, S.A.6    Kopf, G.S.7
  • 43
    • 0032985619 scopus 로고    scopus 로고
    • Roles of bicarbonate, cAMP, and protein tyrosine phosphorylation on capacitation and the spontaneous acrosome reaction of hamster sperm
    • Visconti PE, Stewart-Savage J, Blasco A, Battaglia L, Miranda P, Kopf GS, Tezon JG. 1999b. Roles of bicarbonate, cAMP, and protein tyrosine phosphorylation on capacitation and the spontaneous acrosome reaction of hamster sperm. Biol Reprod 61:76-84.
    • (1999) Biol Reprod , vol.61 , pp. 76-84
    • Visconti, P.E.1    Stewart-Savage, J.2    Blasco, A.3    Battaglia, L.4    Miranda, P.5    Kopf, G.S.6    Tezon, J.G.7
  • 44
    • 0032828238 scopus 로고    scopus 로고
    • Responses of monkey epididymal sperm of different maturational status to second messengers mediating protein tyrosine phosphorylation, acrosome reaction, and motility
    • Yeung CH, Weinbauer GF, Cooper TG. 1999. Responses of monkey epididymal sperm of different maturational status to second messengers mediating protein tyrosine phosphorylation, acrosome reaction, and motility. Mol Reprod Dev 54:194-202.
    • (1999) Mol Reprod Dev , vol.54 , pp. 194-202
    • Yeung, C.H.1    Weinbauer, G.F.2    Cooper, T.G.3
  • 45
    • 0033580911 scopus 로고    scopus 로고
    • Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1
    • Zhang SH, Liu J, Kobayashi R, Tonks NK. 1999. Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1. J Biol Chem 274: 17806-17812.
    • (1999) J Biol Chem , vol.274 , pp. 17806-17812
    • Zhang, S.H.1    Liu, J.2    Kobayashi, R.3    Tonks, N.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.