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Volumn 79, Issue 2, 2008, Pages 337-347

Phosphorylation-dependent interaction of tyrosine 3-monooxygenase/ tryptophan 5-monooxygenase activation protein (YWHA) with PADI6 following oocyte maturation in mice

Author keywords

14 3 3; Egg; Gamete biology; Gametogenesis; Mouse; Oocyte; Oocyte development; Oocyte maturation; Ovum; PAD6; PADI6; Peptidylarginine deiminase; Phosphorylation; YWHA

Indexed keywords

CITRULLINE; GLUTATHIONE TRANSFERASE; OXYGENASE; PEPTIDYLARGININE DEIMINASE TYPE VI; PROTEIN; TYROSINE 3 MONOOXYGENASE TRYPTOPHAN 5 MONOOXYGENASE ACTIVATION PROTEIN;

EID: 48749116843     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod.108.069328     Document Type: Article
Times cited : (16)

References (44)
  • 1
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 proteins: A historic overview
    • Aitken A. 14-3-3 proteins: a historic overview. Semin Cancer Biol 2006; 16:162-172.
    • (2006) Semin Cancer Biol , vol.16 , pp. 162-172
    • Aitken, A.1
  • 3
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe MB. How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett 2002; 513:53-57.
    • (2002) FEBS Lett , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 4
    • 0034788964 scopus 로고    scopus 로고
    • 14-3-3 proteins: Key regulators of cell division, signaling, and apoptosis
    • van Hemert MJ, Steensma HY, van Heusden GP. 14-3-3 proteins: key regulators of cell division, signaling, and apoptosis. Bioessays 2001; 23:936-946.
    • (2001) Bioessays , vol.23 , pp. 936-946
    • van Hemert, M.J.1    Steensma, H.Y.2    van Heusden, G.P.3
  • 5
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • Dougherty MK, Morrison DK. Unlocking the code of 14-3-3. J Cell Sci 2004; 117:1875-1884.
    • (2004) J Cell Sci , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 6
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • Mackintosh C. Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem J 2004; 381:329-342.
    • (2004) Biochem J , vol.381 , pp. 329-342
    • Mackintosh, C.1
  • 7
    • 3543035767 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins
    • Meek SEM, Lane WS, Piwnica-Worms H. Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins. J Biol Chem 2004; 279:32046-32054.
    • (2004) J Biol Chem , vol.279 , pp. 32046-32054
    • Meek, S.E.M.1    Lane, W.S.2    Piwnica-Worms, H.3
  • 8
    • 0041312686 scopus 로고    scopus 로고
    • 14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase
    • Rubio MP, Peggie M, Wong BHC, Morrice N, MacKintosh C. 14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase. EMBO J 2003; 22:3514-3523.
    • (2003) EMBO J , vol.22 , pp. 3514-3523
    • Rubio, M.P.1    Peggie, M.2    Wong, B.H.C.3    Morrice, N.4    MacKintosh, C.5
  • 9
    • 19344376145 scopus 로고    scopus 로고
    • 14-3-3 proteins: A number of functions for a numbered protein
    • Bridges D, Moorhead GB. 14-3-3 proteins: a number of functions for a numbered protein. Sci STKE 2005; re10.
    • (2005) Sci STKE
    • Bridges, D.1    Moorhead, G.B.2
  • 10
    • 33745153790 scopus 로고    scopus 로고
    • Differential role of 14-3-3 family members in Xenopus development
    • Lau JMC, Wu CL, Muslin AJ. Differential role of 14-3-3 family members in Xenopus development. Dev Dyn 2006; 235:1761-1776.
    • (2006) Dev Dyn , vol.235 , pp. 1761-1776
    • Lau, J.M.C.1    Wu, C.L.2    Muslin, A.J.3
  • 11
    • 25144441037 scopus 로고    scopus 로고
    • Role of 14-3-3 proteins in eukaryotic signaling and development
    • Darling DL, Yingling J, Wynshaw-Boris A. Role of 14-3-3 proteins in eukaryotic signaling and development. Curr Top Dev Biol 2005; 68:281-315.
    • (2005) Curr Top Dev Biol , vol.68 , pp. 281-315
    • Darling, D.L.1    Yingling, J.2    Wynshaw-Boris, A.3
  • 12
    • 33745654966 scopus 로고    scopus 로고
    • Amino acids C-terminal to the 14-3-3 binding motif in CDC25B affect the efficiency of 14-3-3 binding
    • Uchida S, Kubo A, Kizu R, Nakagama H, Matsunaga T, Ishizaka Y, Yamashita K. Amino acids C-terminal to the 14-3-3 binding motif in CDC25B affect the efficiency of 14-3-3 binding. J Biochem 2006; 139:761-769.
    • (2006) J Biochem , vol.139 , pp. 761-769
    • Uchida, S.1    Kubo, A.2    Kizu, R.3    Nakagama, H.4    Matsunaga, T.5    Ishizaka, Y.6    Yamashita, K.7
  • 13
    • 0242389822 scopus 로고    scopus 로고
    • PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation
    • Margolis SS, Walsh S, Weiser DC, Yoshida M, Shenolikar S, Kornbluth S. PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation. EMBO J 2003; 22:5734-5745.
    • (2003) EMBO J , vol.22 , pp. 5734-5745
    • Margolis, S.S.1    Walsh, S.2    Weiser, D.C.3    Yoshida, M.4    Shenolikar, S.5    Kornbluth, S.6
  • 14
    • 0033561439 scopus 로고    scopus 로고
    • Maintenance of G(2) arrest in the Xenopus oocyte: A role for 14-3-3-mediated inhibition of Cdc25 nuclear import
    • Yang J, Winkler K, Yoshida M, Kornbluth S. Maintenance of G(2) arrest in the Xenopus oocyte: a role for 14-3-3-mediated inhibition of Cdc25 nuclear import. EMBO J 1999; 18:2174-2183.
    • (1999) EMBO J , vol.18 , pp. 2174-2183
    • Yang, J.1    Winkler, K.2    Yoshida, M.3    Kornbluth, S.4
  • 15
    • 33744544172 scopus 로고    scopus 로고
    • 14-3-3 proteins in cell cycle regulation
    • Hermeking H, Benzinger A. 14-3-3 proteins in cell cycle regulation. Semin Cancer Biol 2006; 16:183-192.
    • (2006) Semin Cancer Biol , vol.16 , pp. 183-192
    • Hermeking, H.1    Benzinger, A.2
  • 17
    • 0242720407 scopus 로고    scopus 로고
    • Vossenaar ER, Zendman AJW, van Venrooij WJ, Pruijn GJM. PAD, a growing family of citrullinating enzymes: genes, features, and involvement in disease. Bioessays 2003; 25:1106-1118.
    • Vossenaar ER, Zendman AJW, van Venrooij WJ, Pruijn GJM. PAD, a growing family of citrullinating enzymes: genes, features, and involvement in disease. Bioessays 2003; 25:1106-1118.
  • 21
    • 1842829046 scopus 로고    scopus 로고
    • Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved noncoding segments and a new human gene, PADI6
    • Chavanas S, Mechin MC, Takahara H, Kawada A, Nachat R, Serre G, Simon M. Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved noncoding segments and a new human gene, PADI6. Gene 2004; 330:19-27.
    • (2004) Gene , vol.330 , pp. 19-27
    • Chavanas, S.1    Mechin, M.C.2    Takahara, H.3    Kawada, A.4    Nachat, R.5    Serre, G.6    Simon, M.7
  • 24
    • 0026551829 scopus 로고
    • Repetitive calcium transients and the role of calcium in exocytosis and cell-cycle activation in the mouse egg
    • Kline D, Kline JT. Repetitive calcium transients and the role of calcium in exocytosis and cell-cycle activation in the mouse egg. Dev Biol 1992; 149:80-89.
    • (1992) Dev Biol , vol.149 , pp. 80-89
    • Kline, D.1    Kline, J.T.2
  • 25
    • 0028090001 scopus 로고
    • Regulation of intracellular calcium in the mouse egg - calcium release in response to sperm or inositol trisphosphate is enhanced after meiotic maturation
    • Mehlmann LM, Kline D. Regulation of intracellular calcium in the mouse egg - calcium release in response to sperm or inositol trisphosphate is enhanced after meiotic maturation. Biol Reprod 1994; 51:1088-1098.
    • (1994) Biol Reprod , vol.51 , pp. 1088-1098
    • Mehlmann, L.M.1    Kline, D.2
  • 26
    • 0037112527 scopus 로고    scopus 로고
    • 14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation site(s)
    • Liu MY, Cai SL, Espejo A, Bedford MT, Walker CL. 14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation site(s). Cancer Res 2002; 62:6475-6480.
    • (2002) Cancer Res , vol.62 , pp. 6475-6480
    • Liu, M.Y.1    Cai, S.L.2    Espejo, A.3    Bedford, M.T.4    Walker, C.L.5
  • 28
    • 0035816718 scopus 로고    scopus 로고
    • Microtubule integrity regulates Pak leading to ras-independent activation of Raf-1-insights into mechanisms of Raf-1 activation
    • Zang MW, Waelde CA, Xiang XQ, Rana A, Wen R, Luo ZJ. Microtubule integrity regulates Pak leading to ras-independent activation of Raf-1-insights into mechanisms of Raf-1 activation. J Biol Chem 2001; 276:25157-25165.
    • (2001) J Biol Chem , vol.276 , pp. 25157-25165
    • Zang, M.W.1    Waelde, C.A.2    Xiang, X.Q.3    Rana, A.4    Wen, R.5    Luo, Z.J.6
  • 30
    • 0035854682 scopus 로고    scopus 로고
    • Endothelin-1 induces serine phosphorylation of the adaptor protein p66(Shc) and its association with 14-3-3 protein in glomerular mesangial cells
    • Foschi M, Franchi F, Han JH, La Villa G, Sorokin A. Endothelin-1 induces serine phosphorylation of the adaptor protein p66(Shc) and its association with 14-3-3 protein in glomerular mesangial cells. J Biol Chem 2001; 276:26640-26647.
    • (2001) J Biol Chem , vol.276 , pp. 26640-26647
    • Foschi, M.1    Franchi, F.2    Han, J.H.3    La Villa, G.4    Sorokin, A.5
  • 32
    • 34548418142 scopus 로고    scopus 로고
    • Methods for the detection and analysis of protein-protein interactions
    • Berggard T, Linse S, James P. Methods for the detection and analysis of protein-protein interactions. Proteomics 2007; 7:2833-2842.
    • (2007) Proteomics , vol.7 , pp. 2833-2842
    • Berggard, T.1    Linse, S.2    James, P.3
  • 34
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer JC, Cantley LC, Yaffe MB. Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res 2003; 31:3635-3641.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 35
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N, Gammeltoft S, Brunak S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 1999; 294:1351-1362.
    • (1999) J Mol Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 36
    • 0031685562 scopus 로고    scopus 로고
    • MAP kinase cascade, but not ERKs, activated during early cleavage of mouse embryos
    • Haraguchi S, Naito K, Sato E. MAP kinase cascade, but not ERKs, activated during early cleavage of mouse embryos. Mol Reprod Dev 1998; 51:148-155.
    • (1998) Mol Reprod Dev , vol.51 , pp. 148-155
    • Haraguchi, S.1    Naito, K.2    Sato, E.3
  • 37
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, Seraphin B. A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 1999; 17:1030-1032.
    • (1999) Nat Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 38
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 proteins: Active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion G, Avruch J. 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J Biol Chem 2002; 277:3061-3064.
    • (2002) J Biol Chem , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 39
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin AJ, Tanner JW, Allen PM, Shaw AS. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 1996; 84:889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 40
    • 0030827138 scopus 로고    scopus 로고
    • Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3 beta protein
    • Zhang SH, Kobayashi R, Graves PR, Piwnica Worms H, Tonks NK. Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3 beta protein. J Biol Chem 1997; 272:27281-27287.
    • (1997) J Biol Chem , vol.272 , pp. 27281-27287
    • Zhang, S.H.1    Kobayashi, R.2    Graves, P.R.3    Piwnica Worms, H.4    Tonks, N.K.5
  • 44
    • 0031027753 scopus 로고    scopus 로고
    • Ribosomal S6 kinase p90(rsk) and mRNA cap-binding protein eIF4E phosphorylations correlate with MAP kinase activation during meiotic reinitiation of mouse oocytes
    • Gavin AC, Schorderet-Slatkine S. Ribosomal S6 kinase p90(rsk) and mRNA cap-binding protein eIF4E phosphorylations correlate with MAP kinase activation during meiotic reinitiation of mouse oocytes. Mol Reprod Dev 1997; 46:383-391.
    • (1997) Mol Reprod Dev , vol.46 , pp. 383-391
    • Gavin, A.C.1    Schorderet-Slatkine, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.