메뉴 건너뛰기




Volumn 50, Issue 8, 2008, Pages 665-673

Valosin-containing protein/p97 interacts with sperm-activating and sperm-attracting factor (SAAF) in the ascidian egg and modulates sperm-attracting activity

Author keywords

Ciona intestinalis; Fertilization; Sperm attraction; Sperm activating and sperm attracting factor (SAAF); Valosin containing protein p97 Cdc48

Indexed keywords

BETA TUBULIN; BINDING PROTEIN; MGC97756 PROTEIN; PROTEASOME; PROTEASOME ALPHA 2 SUBUNIT; PROTEASOME SUBUNIT Y; PROTEIN; PROTEIN P97; SPERM ACTIVATING AND SPERM ATTRACTING FACTOR; SPERM ACTIVATING AND SPERM ATTRACTING FACTOR BINDING PROTEIN; UNCLASSIFIED DRUG; VALOSIN CONTAINING PROTEIN;

EID: 53149096580     PISSN: 00121592     EISSN: 1440169X     Source Type: Journal    
DOI: 10.1111/j.1440-169X.2008.01064.x     Document Type: Article
Times cited : (12)

References (40)
  • 2
    • 0021438677 scopus 로고
    • Sperm chemotaxis in siphonophores. II. Calcium-dependent asymmetrical movement of spermatozoa induced by the attractant
    • Cosson, M. P., Carre, D. Cosson, J. 1984. Sperm chemotaxis in siphonophores. II. Calcium-dependent asymmetrical movement of spermatozoa induced by the attractant. J. Cell Sci. 68, 163 181.
    • (1984) J. Cell Sci. , vol.68 , pp. 163-181
    • Cosson, M.P.1    Carre, D.2    Cosson, J.3
  • 3
    • 0001438589 scopus 로고
    • Fertilization in the medusan, Spirocodon saltatrix
    • Dan, J. C. 1950. Fertilization in the medusan, Spirocodon saltatrix. Biol. Bull. 99, 412 415.
    • (1950) Biol. Bull. , vol.99 , pp. 412-415
    • Dan, J.C.1
  • 4
    • 4644243461 scopus 로고    scopus 로고
    • Ubiquitin is conjugated by membrane ubiquitin ligase to three sites, including the N terminus, in transmembrane region of mammalian 3-hydroxy-3-methylglutaryl coenzyme a reductase: Implications for sterol-regulated enzyme degradation
    • Doolman, R., Leichner, G. S., Avner, R. Roitelman, J. 2004. Ubiquitin is conjugated by membrane ubiquitin ligase to three sites, including the N terminus, in transmembrane region of mammalian 3-hydroxy-3-methylglutaryl coenzyme A reductase: implications for sterol-regulated enzyme degradation. J. Biol. Chem. 279, 38184 38193.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38184-38193
    • Doolman, R.1    Leichner, G.S.2    Avner, R.3    Roitelman, J.4
  • 5
    • 0033060654 scopus 로고    scopus 로고
    • Sperm chemotaxis
    • Eisenbach, M. 1999. Sperm chemotaxis. Rev. Reprod. 4, 56 66.
    • (1999) Rev. Reprod. , vol.4 , pp. 56-66
    • Eisenbach, M.1
  • 6
    • 0023132635 scopus 로고
    • The role of oocyte maturation in the ontogeny of the fertilization site in the hydrozoan Hydractinia echinata
    • Freeman, G. 1987. The role of oocyte maturation in the ontogeny of the fertilization site in the hydrozoan Hydractinia echinata. Ronxs Arch. Dev. Biol. 196, 83 92.
    • (1987) Ronxs Arch. Dev. Biol. , vol.196 , pp. 83-92
    • Freeman, G.1
  • 7
    • 0020212906 scopus 로고
    • Hydrozoan eggs can only be fertilized at the site of polar body formation
    • Freeman, G. Miller, R. L. 1982. Hydrozoan eggs can only be fertilized at the site of polar body formation. Dev. Biol. 94, 142 152.
    • (1982) Dev. Biol. , vol.94 , pp. 142-152
    • Freeman, G.1    Miller, R.L.2
  • 8
    • 0028685470 scopus 로고
    • A novel biotinylated heterobifunctional cross-linking reagent bearing an aromatic diazirine
    • Hatanaka, Y., Hashimoto, M. Kanaoka, Y. 1994a. A novel biotinylated heterobifunctional cross-linking reagent bearing an aromatic diazirine. Bioorg. Med. Chem. 2, 1367 1373.
    • (1994) Bioorg. Med. Chem. , vol.2 , pp. 1367-1373
    • Hatanaka, Y.1    Hashimoto, M.2    Kanaoka, Y.3
  • 10
    • 40049098664 scopus 로고    scopus 로고
    • Molecular characterization of axonemal proteins and signaling molecules responsible for chemoattractant-induced sperm activation in Ciona intestinalis
    • Hozumi, A., Padma, P., Toda, T., Ide, H. Inaba, K. 2008. Molecular characterization of axonemal proteins and signaling molecules responsible for chemoattractant-induced sperm activation in Ciona intestinalis. Cell Motil. Cytoskeleton 65, 249 267.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 249-267
    • Hozumi, A.1    Padma, P.2    Toda, T.3    Ide, H.4    Inaba, K.5
  • 11
    • 2942546538 scopus 로고    scopus 로고
    • Local database and the search program for proteomic analysis of sperm proteins in the ascidian Ciona intestinalis
    • Hozumi, A., Satouh, Y., Ishibe, D. et al. 2004. Local database and the search program for proteomic analysis of sperm proteins in the ascidian Ciona intestinalis. Biochem. Biophys. Res. Commun. 319, 1241 1246.
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 1241-1246
    • Hozumi, A.1    Satouh, Y.2    Ishibe, D.3
  • 12
    • 33744994769 scopus 로고    scopus 로고
    • 2+ increase induces post-fertilization events via MAP kinase dephosphorylation in eggs of the hydrozoan jellyfish Cladonema pacificum
    • 2+ increase induces post-fertilization events via MAP kinase dephosphorylation in eggs of the hydrozoan jellyfish Cladonema pacificum. Dev. Biol. 293, 228 241.
    • (2006) Dev. Biol. , vol.293 , pp. 228-241
    • Kondoh, E.1    Tachibana, K.2    Deguchi, R.3
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0029122698 scopus 로고
    • Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes
    • Latterich, M., Frohlich, K. Schekman, R. 1995. Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes. Cell 82, 885 893.
    • (1995) Cell , vol.82 , pp. 885-893
    • Latterich, M.1    Frohlich, K.2    Schekman, R.3
  • 15
    • 0013915572 scopus 로고
    • Chemotaxis during fertilization in the hydroid Campanularia
    • Miller, R. L. 1966. Chemotaxis during fertilization in the hydroid Campanularia. J. Exp. Zool. 162, 23 44.
    • (1966) J. Exp. Zool. , vol.162 , pp. 23-44
    • Miller, R.L.1
  • 16
    • 84987574097 scopus 로고
    • Site-specific sperm agglutination and the timed release of a sperm chemo-attractant by the egg of the leptomedusan, Orthopyxis caliculata
    • Miller, R. L. 1978. Site-specific sperm agglutination and the timed release of a sperm chemo-attractant by the egg of the leptomedusan, Orthopyxis caliculata. J. Exp. Zool. 205, 385 392.
    • (1978) J. Exp. Zool. , vol.205 , pp. 385-392
    • Miller, R.L.1
  • 17
    • 0001853802 scopus 로고
    • Sperm chemotaxis in the hydromedusae: I. Species-specificity and sperm behavior
    • Miller, R. L. 1979. Sperm chemotaxis in the hydromedusae: I. Species-specificity and sperm behavior. Mar. Biol. 53, 99 114.
    • (1979) Mar. Biol. , vol.53 , pp. 99-114
    • Miller, R.L.1
  • 18
    • 0001338444 scopus 로고
    • Sperm chemotaxis in ascidians
    • Miller, R. L. 1982. Sperm chemotaxis in ascidians. Am. Zool. 22, 827 840.
    • (1982) Am. Zool. , vol.22 , pp. 827-840
    • Miller, R.L.1
  • 19
    • 84993918907 scopus 로고
    • Demonstration of sperm chemotaxis in echinodermata: Asteroidea, Holothuroidea, Ophiuroidea
    • Miller, R. L. 1985a. Demonstration of sperm chemotaxis in echinodermata: Asteroidea, Holothuroidea, Ophiuroidea. J. Exp. Zool. 234, 383 414.
    • (1985) J. Exp. Zool. , vol.234 , pp. 383-414
    • Miller, R.L.1
  • 20
    • 0000513535 scopus 로고
    • Sperm chemo-orientation in metazoa
    • (eds C. B. Metz A. Monroy In. Vol. 2 (eds. pp. Academic Press, New York.
    • Miller, R. L. 1985b. Sperm chemo-orientation in metazoa. In Biology of Fertilization, Vol. 2 (eds C. B. Metz A. Monroy pp. 275 337. Academic Press, New York.
    • (1985) Biology of Fertilization , pp. 275-337
    • Miller, R.L.1
  • 21
    • 21344456775 scopus 로고    scopus 로고
    • Activation of motility and chemotaxis in the spermatozoa: From invertebrates to humans
    • Morisawa, M. Yoshida, M. 2005. Activation of motility and chemotaxis in the spermatozoa: from invertebrates to humans. Reprod. Med. Biol. 4, 101 114.
    • (2005) Reprod. Med. Biol. , vol.4 , pp. 101-114
    • Morisawa, M.1    Yoshida, M.2
  • 22
    • 0041696649 scopus 로고    scopus 로고
    • Synthesis of endogenous sperm-activating and attracting factor isolated from ascidian Ciona intestinalis
    • Oishi, T., Tuchikawa, H., Murata, M., Yoshida, M. Morisawa, M. 2003. Synthesis of endogenous sperm-activating and attracting factor isolated from ascidian Ciona intestinalis. Tetrahedron Lett. 44, 6387 6389.
    • (2003) Tetrahedron Lett. , vol.44 , pp. 6387-6389
    • Oishi, T.1    Tuchikawa, H.2    Murata, M.3    Yoshida, M.4    Morisawa, M.5
  • 23
    • 0035949509 scopus 로고    scopus 로고
    • Allurin, a 21-kDa sperm chemoattractant from Xenopus egg jelly, is related to mammalian sperm-binding proteins
    • Olson, J. H., Xiang, X., Ziegert, T. et al. 2001. Allurin, a 21-kDa sperm chemoattractant from Xenopus egg jelly, is related to mammalian sperm-binding proteins. Proc. Natl Acad. Sci. USA 98, 11205 11210.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11205-11210
    • Olson, J.H.1    Xiang, X.2    Ziegert, T.3
  • 24
    • 31544453323 scopus 로고    scopus 로고
    • Establishment of animal-vegetal polarity during maturation in ascidian oocytes
    • Prodon, F., Chenevert, J. Sardet, C. 2006. Establishment of animal-vegetal polarity during maturation in ascidian oocytes. Dev. Biol. 290, 297 311.
    • (2006) Dev. Biol. , vol.290 , pp. 297-311
    • Prodon, F.1    Chenevert, J.2    Sardet, C.3
  • 25
    • 33750872805 scopus 로고    scopus 로고
    • Increase in multidrug transport activity is associated with oocyte maturation in sea stars
    • Roepke, T. A., Hamdoun, A. M. Cherr, G. N. 2006. Increase in multidrug transport activity is associated with oocyte maturation in sea stars. Dev. Growth Differ. 48, 559 573.
    • (2006) Dev. Growth Differ. , vol.48 , pp. 559-573
    • Roepke, T.A.1    Hamdoun, A.M.2    Cherr, G.N.3
  • 26
    • 33748987082 scopus 로고    scopus 로고
    • 2+ exchanger modulates the flagellar wave pattern for the regulation of motility activation and chemotaxis in the ascidian spermatozoa
    • 2+ exchanger modulates the flagellar wave pattern for the regulation of motility activation and chemotaxis in the ascidian spermatozoa. Cell Motil. Cytoskeleton 63, 623 632.
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 623-632
    • Shiba, K.1    Marian, T.2    Krasznai, Z.3    Baba, S.A.4    Morisawa, M.5    Yoshida, M.6
  • 27
    • 24944591120 scopus 로고    scopus 로고
    • Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase
    • Song, B. L., Sever, N. Debose-Boyd, R. A. 2005. Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. Mol. Cell 19, 829 840.
    • (2005) Mol. Cell , vol.19 , pp. 829-840
    • Song, B.L.1    Sever, N.2    Debose-Boyd, R.A.3
  • 28
    • 0037049466 scopus 로고    scopus 로고
    • VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo
    • Uchiyama, K., Jokitalo, E., Kano, F. et al. 2002. VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo. J. Cell Biol. 159, 855 866.
    • (2002) J. Cell Biol. , vol.159 , pp. 855-866
    • Uchiyama, K.1    Jokitalo, E.2    Kano, F.3
  • 29
    • 17044386675 scopus 로고    scopus 로고
    • P97/p47-Mediated biogenesis of Golgi and ER
    • Uchiyama, K. Kondo, H. 2005. p97/p47-Mediated biogenesis of Golgi and ER. J. Biochem. 137, 115 119.
    • (2005) J. Biochem. , vol.137 , pp. 115-119
    • Uchiyama, K.1    Kondo, H.2
  • 30
    • 0026487058 scopus 로고
    • Human P-glycoprotein transports cortisol, aldosterone, and dexamethasone, but not progesterone
    • Ueda, K., Okamura, N., Hirai, M. et al. 1992. Human P-glycoprotein transports cortisol, aldosterone, and dexamethasone, but not progesterone. J. Biol. Chem. 267, 24248 24252.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24248-24252
    • Ueda, K.1    Okamura, N.2    Hirai, M.3
  • 31
    • 1642309633 scopus 로고    scopus 로고
    • Molecular perspectives on p97-VCP: Progress in understanding its structure and diverse biological functions
    • Wang, Q., Song, C. Li, C. C. 2004. Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions. J. Struct. Biol. 146, 44 57.
    • (2004) J. Struct. Biol. , vol.146 , pp. 44-57
    • Wang, Q.1    Song, C.2    Li, C.C.3
  • 32
    • 0022372552 scopus 로고
    • Chemotaxis of Arbacia punctulata spermatozoa to resact, a peptide from the egg jelly layer
    • Ward, G. E., Brokaw, C. J., Garbers, D. L. Vacquier, V. D. 1985. Chemotaxis of Arbacia punctulata spermatozoa to resact, a peptide from the egg jelly layer. J. Cell Biol. 101, 2324 2329.
    • (1985) J. Cell Biol. , vol.101 , pp. 2324-2329
    • Ward, G.E.1    Brokaw, C.J.2    Garbers, D.L.3    Vacquier, V.D.4
  • 33
    • 0242635839 scopus 로고    scopus 로고
    • P97, a protein coping with multiple identities
    • Woodman, P. G. 2003. p97, a protein coping with multiple identities. J. Cell Sci. 116, 4283 4290.
    • (2003) J. Cell Sci. , vol.116 , pp. 4283-4290
    • Woodman, P.G.1
  • 34
    • 33749236210 scopus 로고    scopus 로고
    • Diverse functions with a common regulator: Ubiquitin takes command of an AAA ATPase
    • Ye, Y. 2006. Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase. J. Struct. Biol. 156, 29 40.
    • (2006) J. Struct. Biol. , vol.156 , pp. 29-40
    • Ye, Y.1
  • 35
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H. H. Rapoport, T. A. 2001. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414, 652 656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 36
    • 0027213435 scopus 로고
    • Sperm chemotaxis during the process of fertilization in the ascidians Ciona savignyi and Ciona intestinalis
    • Yoshida, M., Inaba, K. Morisawa, M. 1993. Sperm chemotaxis during the process of fertilization in the ascidians Ciona savignyi and Ciona intestinalis. Dev. Biol. 157, 497 506.
    • (1993) Dev. Biol. , vol.157 , pp. 497-506
    • Yoshida, M.1    Inaba, K.2    Morisawa, M.3
  • 38
    • 0037069393 scopus 로고    scopus 로고
    • A chemoattractant for ascidian spermatozoa is a sulfated steroid
    • Yoshida, M., Murata, M., Inaba, K. Morisawa, M. 2002. A chemoattractant for ascidian spermatozoa is a sulfated steroid. Proc. Natl Acad. Sci. USA 99, 14 831 14 836.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14831-14836
    • Yoshida, M.1    Murata, M.2    Inaba, K.3    Morisawa, M.4
  • 39
    • 0028587687 scopus 로고
    • Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum of rat liver
    • Zhang, L., Ashendel, C. L., Becker, G. W. Morre, D. J. 1994. Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum of rat liver. J. Cell Biol. 127, 1871 1883.
    • (1994) J. Cell Biol. , vol.127 , pp. 1871-1883
    • Zhang, L.1    Ashendel, C.L.2    Becker, G.W.3    Morre, D.J.4
  • 40
    • 0033855808 scopus 로고    scopus 로고
    • VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells
    • Zhang, H., Wang, Q., Kajino, K. Greene, M. I. 2000. VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells. DNA Cell Biol. 19, 253 263.
    • (2000) DNA Cell Biol. , vol.19 , pp. 253-263
    • Zhang, H.1    Wang, Q.2    Kajino, K.3    Greene, M.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.