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Volumn 61, Issue 2, 1999, Pages 335-342

Conservation and function of a bovine sperm A-kinase anchor protein homologous to mouse AKAP82

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; UNCLASSIFIED DRUG;

EID: 0032764209     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod61.2.335     Document Type: Article
Times cited : (46)

References (36)
  • 1
    • 0003164230 scopus 로고
    • Mammalian spermatozoa: Structure and assembly of the tail
    • Gagnon C (ed.), Boca Raton, FL: CRC Press
    • Oko R, Clermont Y. Mammalian spermatozoa: structure and assembly of the tail. In: Gagnon C (ed.), Controls of Sperm Motility: Biological and Clinical Aspects. Boca Raton, FL: CRC Press; 1990: 3-27.
    • (1990) Controls of Sperm Motility: Biological and Clinical Aspects , pp. 3-27
    • Oko, R.1    Clermont, Y.2
  • 2
    • 0020623097 scopus 로고
    • Cyclic adenosine 3′,5′ monophosphate, calcium and protein phosphorylation in flagellar motility
    • Tash JS, Means AR. Cyclic adenosine 3′,5′ monophosphate, calcium and protein phosphorylation in flagellar motility. Biol Reprod 1983; 28:75-104.
    • (1983) Biol Reprod , vol.28 , pp. 75-104
    • Tash, J.S.1    Means, A.R.2
  • 3
    • 84907123783 scopus 로고
    • Regulation of mammalian sperm motility
    • Lindemann CB, Kanous KS. Regulation of mammalian sperm motility. Arch Androl 1989; 23:1-22.
    • (1989) Arch Androl , vol.23 , pp. 1-22
    • Lindemann, C.B.1    Kanous, K.S.2
  • 4
    • 0024329482 scopus 로고
    • Protein phosphorylation: The second messenger signal transducer of flagellar motility
    • Tash JS. Protein phosphorylation: the second messenger signal transducer of flagellar motility. Cell Motil Cytoskel 1989; 14:332-339.
    • (1989) Cell Motil Cytoskel , vol.14 , pp. 332-339
    • Tash, J.S.1
  • 5
    • 0028230419 scopus 로고
    • Role of cAMP in the reactivation of demembranated ram spermatozoa
    • San Agustin JT, Witman GB. Role of cAMP in the reactivation of demembranated ram spermatozoa. Cell Motil Cytoskel 1994; 27:206-218.
    • (1994) Cell Motil Cytoskel , vol.27 , pp. 206-218
    • San Agustin, J.T.1    Witman, G.B.2
  • 6
    • 0028605927 scopus 로고
    • Regulation of sperm motility: Emerging evidence for a major role for protein phosphatases
    • Tash JS, Bracho GE. Regulation of sperm motility: emerging evidence for a major role for protein phosphatases. J Androl 1994; 15:505-509.
    • (1994) J Androl , vol.15 , pp. 505-509
    • Tash, J.S.1    Bracho, G.E.2
  • 7
    • 0031573950 scopus 로고    scopus 로고
    • Regulation, localization, and anchoring of protein kinase A subunits during mouse sperm capacitation
    • Visconti PE, Johnson L, Oyaski M, Fornés M, Moss SB, Gerton GL, Kopf GS. Regulation, localization, and anchoring of protein kinase A subunits during mouse sperm capacitation. Dev Biol 1997; 192:351-363.
    • (1997) Dev Biol , vol.192 , pp. 351-363
    • Visconti, P.E.1    Johnson, L.2    Oyaski, M.3    Fornés, M.4    Moss, S.B.5    Gerton, G.L.6    Kopf, G.S.7
  • 8
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson T, Scott JD. Signaling through scaffold, anchoring, and adaptor proteins. Science 1997; 278:2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 9
    • 0027730774 scopus 로고
    • A-kinase anchoring proteins: A key to selective activation of cAMP-responsive elements
    • Coghlan VM, Bergeson SE, Langeberg L, Nilaver G, Scott JD. A-kinase anchoring proteins: a key to selective activation of cAMP-responsive elements. Mol Cell Biochem 1993; 128:309-319.
    • (1993) Mol Cell Biochem , vol.128 , pp. 309-319
    • Coghlan, V.M.1    Bergeson, S.E.2    Langeberg, L.3    Nilaver, G.4    Scott, J.D.5
  • 10
    • 0028588997 scopus 로고
    • A kinase anchor protein and the intracellular targeting of signals carried by cyclic-AMP
    • Rubin CS. A kinase anchor protein and the intracellular targeting of signals carried by cyclic-AMP Biochim Biophys Acta 1994; 1224: 467-479.
    • (1994) Biochim Biophys Acta , vol.1224 , pp. 467-479
    • Rubin, C.S.1
  • 11
    • 0028023326 scopus 로고
    • The major fibrous sheath polypeptide of mouse sperm: Structural and functional similarities to the A-kinase anchoring proteins
    • Carrera A, Gerton GL, Moss SB. The major fibrous sheath polypeptide of mouse sperm: structural and functional similarities to the A-kinase anchoring proteins. Dev Biol 1994; 165:272-284.
    • (1994) Dev Biol , vol.165 , pp. 272-284
    • Carrera, A.1    Gerton, G.L.2    Moss, S.B.3
  • 12
    • 0027199204 scopus 로고
    • The sliding of the fibrous sheath through the axoneme proximally together with microtubule extrusion
    • Si Y, Okuno M. The sliding of the fibrous sheath through the axoneme proximally together with microtubule extrusion. Exp Cell Res 1993; 208:170-174.
    • (1993) Exp Cell Res , vol.208 , pp. 170-174
    • Si, Y.1    Okuno, M.2
  • 13
    • 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. 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 1996; 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
  • 15
    • 0033610895 scopus 로고    scopus 로고
    • An X-linked gene encodes a major human sperm fibrous sheath protein, hAKAP82. Genomic organization, protein kinase A-RII binding, and distribution of the precursor in the sperm tail
    • Turner RMO, Johnson LR, Haig-Ladewig L, Gerton GL, Moss SB. An X-linked gene encodes a major human sperm fibrous sheath protein, hAKAP82. Genomic organization, protein kinase A-RII binding, and distribution of the precursor in the sperm tail. J Biol Chem 1998; 273:32135-32141.
    • (1998) J Biol Chem , vol.273 , pp. 32135-32141
    • Turner, R.M.O.1    Johnson, L.R.2    Haig-Ladewig, L.3    Gerton, G.L.4    Moss, S.B.5
  • 16
    • 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. Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′,5′-monophosphate-dependent pathway. Biol Reprod 1997; 56:707-719.
    • (1997) Biol Reprod , vol.56 , pp. 707-719
    • Galantino-Homer, H.L.1    Visconti, P.E.2    Kopf, G.S.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner W, Weissman C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal Biochem 1973; 56:502-504.
    • (1973) Anal Biochem , vol.56 , pp. 502-504
    • Schaffner, W.1    Weissman, C.2
  • 19
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 20
    • 0018800918 scopus 로고
    • Characterization and comparison of membrane-associated and cytosolic cAMP-dependent protein kinases: Physiochemical and immunological studies on bovine cerebral cortex protein kinases
    • Rubin CS, Rangel Aldao R, Sankar D, Erlichman J, Fleischer N. Characterization and comparison of membrane-associated and cytosolic cAMP-dependent protein kinases: physiochemical and immunological studies on bovine cerebral cortex protein kinases. J Biol Chem 1979; 254:3797-3805.
    • (1979) J Biol Chem , vol.254 , pp. 3797-3805
    • Rubin, C.S.1    Rangel Aldao, R.2    Sankar, D.3    Erlichman, J.4    Fleischer, N.5
  • 21
    • 0023018797 scopus 로고
    • Differential binding of the regulatory subunits (RII) of cAMP-dependent protein kinase II from bovine brain and muscle to RII-binding proteins
    • Leiser M, Rubin CS, Erlichman J. Differential binding of the regulatory subunits (RII) of cAMP-dependent protein kinase II from bovine brain and muscle to RII-binding proteins. J Biol Chem 1986; 261:1904-1908.
    • (1986) J Biol Chem , vol.261 , pp. 1904-1908
    • Leiser, M.1    Rubin, C.S.2    Erlichman, J.3
  • 22
    • 0021352272 scopus 로고
    • Characterization and localization of cAMP-dependent protein kinases in rat caudal epididymal sperm
    • Horowitz JA, Toeg H, Orr GA. Characterization and localization of cAMP-dependent protein kinases in rat caudal epididymal sperm. J Biol Chem 1984; 259:832-838.
    • (1984) J Biol Chem , vol.259 , pp. 832-838
    • Horowitz, J.A.1    Toeg, H.2    Orr, G.A.3
  • 23
    • 0023841019 scopus 로고
    • Interaction of the regulatory subunit of a type II cAMP-dependent protein kinase with the mammalian sperm flagellum
    • Horowitz JA, Wasco W, Leiser M, Orr GA. Interaction of the regulatory subunit of a type II cAMP-dependent protein kinase with the mammalian sperm flagellum. J Biol Chem 1988; 263:2098-2104.
    • (1988) J Biol Chem , vol.263 , pp. 2098-2104
    • Horowitz, J.A.1    Wasco, W.2    Leiser, M.3    Orr, G.A.4
  • 24
    • 0031040893 scopus 로고    scopus 로고
    • Protein kinase A anchoring inhibitor peptides arrest mammalian sperm motility
    • Vijayaraghavan S, Goueli S, Davey MP, Carr DW. Protein kinase A anchoring inhibitor peptides arrest mammalian sperm motility. J Biol Chem 1997; 272:4747-4752.
    • (1997) J Biol Chem , vol.272 , pp. 4747-4752
    • Vijayaraghavan, S.1    Goueli, S.2    Davey, M.P.3    Carr, D.W.4
  • 25
    • 0028810676 scopus 로고
    • Characterization of S-AKAP84, a novel developmentally regulated A kinase anchor protein of male germ cells
    • Lin RY, Moss SB, Rubin CS. Characterization of S-AKAP84, a novel developmentally regulated A kinase anchor protein of male germ cells. J Biol Chem 1995; 270:27804-27811.
    • (1995) J Biol Chem , vol.270 , pp. 27804-27811
    • Lin, R.Y.1    Moss, S.B.2    Rubin, C.S.3
  • 26
    • 0030974317 scopus 로고    scopus 로고
    • Cloning and characterization of a testis-specific, developing regulated A-kinase-anchoring protein (TAKAP-80) present in the fibrous sheath of rat sperm
    • Mei X, Singh IS, Erlichman J, Orr GA. Cloning and characterization of a testis-specific, developing regulated A-kinase-anchoring protein (TAKAP-80) present in the fibrous sheath of rat sperm. Eur J Biochem 1997; 246:425-432.
    • (1997) Eur J Biochem , vol.246 , pp. 425-432
    • Mei, X.1    Singh, I.S.2    Erlichman, J.3    Orr, G.A.4
  • 27
    • 0018830277 scopus 로고
    • A c-AMP-dependent phosphorylated motility protein in bovine epididymal sperm
    • Brandt H, Hoskins DD. A c-AMP-dependent phosphorylated motility protein in bovine epididymal sperm. J Biol Chem 1980; 255:982-987.
    • (1980) J Biol Chem , vol.255 , pp. 982-987
    • Brandt, H.1    Hoskins, D.D.2
  • 28
    • 0021184785 scopus 로고
    • Flagellar motility requires the cAMP-dependent phosphorylation of a heat-stable NP-40-soluble 56-kDa protein, axokinin
    • Tash JS, Kakar SS, Means AR. Flagellar motility requires the cAMP-dependent phosphorylation of a heat-stable NP-40-soluble 56-kDa protein, axokinin. Cell 1984; 38:551-559.
    • (1984) Cell , vol.38 , pp. 551-559
    • Tash, J.S.1    Kakar, S.S.2    Means, A.R.3
  • 29
    • 0023646056 scopus 로고
    • Involvement of tyrosine protein kinase in the initiation of flagellar movement in rainbow trout spermatozoa
    • Hayashi H, Yamamoto K, Yonekawa H, Morisawa M. Involvement of tyrosine protein kinase in the initiation of flagellar movement in rainbow trout spermatozoa. J Biol Chem 1987; 262:16692-16698.
    • (1987) J Biol Chem , vol.262 , pp. 16692-16698
    • Hayashi, H.1    Yamamoto, K.2    Yonekawa, H.3    Morisawa, M.4
  • 30
    • 0030923852 scopus 로고    scopus 로고
    • A tyrosine-phosphorylated 55-kilodalton motility-associated bovine sperm protein is regulated by cyclic adenosine 3′,5′-monophosphates and calcium
    • Vijayaraghavan S, Trautman KD, Goueli SA, Carr DW. A tyrosine-phosphorylated 55-kilodalton motility-associated bovine sperm protein is regulated by cyclic adenosine 3′,5′-monophosphates and calcium. Biol Reprod 1997; 56:1450-1457.
    • (1997) Biol Reprod , vol.56 , pp. 1450-1457
    • Vijayaraghavan, S.1    Trautman, K.D.2    Goueli, S.A.3    Carr, D.W.4
  • 31
    • 0030047194 scopus 로고    scopus 로고
    • Sperm motility development in the epididymis is associated with decreased glycogen synthase kinase-3 and protein phosphatase 1 activity
    • Vijayaraghavan S, Stephens DT, Trautman K. Sperm motility development in the epididymis is associated with decreased glycogen synthase kinase-3 and protein phosphatase 1 activity. Biol Reprod 1996; 54:709-718.
    • (1996) Biol Reprod , vol.54 , pp. 709-718
    • Vijayaraghavan, S.1    Stephens, D.T.2    Trautman, K.3
  • 32
    • 0024409495 scopus 로고
    • The major component of the rat sperm fibrous sheath is a phosphoprotein
    • Brito M, Figuero J, Maldonado EU, Vera JC, Burzio LO. The major component of the rat sperm fibrous sheath is a phosphoprotein. Gamete Res 1989; 22:205-217.
    • (1989) Gamete Res , vol.22 , pp. 205-217
    • Brito, M.1    Figuero, J.2    Maldonado, E.U.3    Vera, J.C.4    Burzio, L.O.5
  • 34
    • 0027948083 scopus 로고
    • Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and affect fertilization
    • Baba T, Azuma S, Kashiwabara S, Toyoda Y. Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and affect fertilization. J Biol Chem 1994; 269:31845-31849.
    • (1994) J Biol Chem , vol.269 , pp. 31845-31849
    • Baba, T.1    Azuma, S.2    Kashiwabara, S.3    Toyoda, Y.4
  • 35
    • 0031035977 scopus 로고    scopus 로고
    • Spermatozoa lacking acrosin protein show delayed fertilization
    • Adham IM, Nayernia K, Engel W. Spermatozoa lacking acrosin protein show delayed fertilization. Mol Reprod Dev 1997; 46:370-376.
    • (1997) Mol Reprod Dev , vol.46 , pp. 370-376
    • Adham, I.M.1    Nayernia, K.2    Engel, W.3
  • 36
    • 0030903895 scopus 로고    scopus 로고
    • Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits
    • Huang LJ-s, Durick K, Weiner JA, Chun J, Taylor SS. Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits. J Biol Chem 1997; 272:8057-8064.
    • (1997) J Biol Chem , vol.272 , pp. 8057-8064
    • Huang, L.J.-S.1    Durick, K.2    Weiner, J.A.3    Chun, J.4    Taylor, S.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.