請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/70612
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 周子賓 | |
dc.contributor.author | Yi-Mei Lee | en |
dc.contributor.author | 李奕枚 | zh_TW |
dc.date.accessioned | 2021-06-17T04:32:34Z | - |
dc.date.available | 2020-08-15 | |
dc.date.copyright | 2018-08-15 | |
dc.date.issued | 2018 | |
dc.date.submitted | 2018-08-10 | |
dc.identifier.citation | 1. Bastock, R. and D. St Johnston, Drosophila oogenesis. Curr Biol, 2008. 18(23): p. R1082-7.
2. Kugler, J.M. and P. Lasko, Localization, anchoring and translational control of oskar, gurken, bicoid and nanos mRNA during Drosophila oogenesis. Fly (Austin), 2009. 3(1): p. 15-28. 3. Huynh, J.R. and D. St Johnston, The origin of asymmetry: early polarisation of the Drosophila germline cyst and oocyte. Curr Biol, 2004. 14(11): p. R438-49. 4. Becalska, A.N. and E.R. Gavis, Lighting up mRNA localization in Drosophila oogenesis. Development, 2009. 136(15): p. 2493-503. 5. Muroyama, A. and T. Lechler, Microtubule organization, dynamics and functions in differentiated cells. Development, 2017. 144(17): p. 3012-3021. 6. Desai, A. and T.J. Mitchison, Microtubule polymerization dynamics. Annu Rev Cell Dev Biol, 1997. 13: p. 83-117. 7. Hausman, G.M.C.a.R.E., The Cytoskeleton and Cell Movement. The Cell: A Molecular Approach, 2013. 6th. Edition 8. Woehlke, G. and M. Schliwa, Walking on two heads: the many talents of kinesin. Nat Rev Mol Cell Biol, 2000. 1(1): p. 50-8. 9. Brendza, R.P., et al., A function for kinesin I in the posterior transport of oskar mRNA and Staufen protein. Science, 2000. 289(5487): p. 2120-2. 10. Steinhauer, J. and D. Kalderon, Microtubule polarity and axis formation in the Drosophila oocyte. Dev Dyn, 2006. 235(6): p. 1455-68. 11. Gonzalez-Reyes, A. and D. St Johnston, Role of oocyte position in establishment of anterior-posterior polarity in Drosophila. Science, 1994. 266(5185): p. 639-42. 12. Theurkauf, W.E., et al., Reorganization of the cytoskeleton during Drosophila oogenesis: implications for axis specification and intercellular transport. Development, 1992. 115(4): p. 923-36. 13. Clark, I., et al., Transient posterior localization of a kinesin fusion protein reflects anteroposterior polarity of the Drosophila oocyte. Curr Biol, 1994. 4(4): p. 289-300. 14. Lehmann, R., Germ Plasm Biogenesis--An Oskar-Centric Perspective. Curr Top Dev Biol, 2016. 116: p. 679-707. 15. Martin, K.C. and A. Ephrussi, mRNA localization: gene expression in the spatial dimension. Cell, 2009. 136(4): p. 719-30. 16. Ferrandon, D., et al., Staufen protein associates with the 3'UTR of bicoid mRNA to form particles that move in a microtubule-dependent manner. Cell, 1994. 79(7): p. 1221-32. 17. Hachet, O. and A. Ephrussi, Splicing of oskar RNA in the nucleus is coupled to its cytoplasmic localization. Nature, 2004. 428(6986): p. 959-63. 18. Simon, B., et al., The structure of the SOLE element of oskar mRNA. RNA, 2015. 21(8): p. 1444-53. 19. Ghosh, S., et al., Control of RNP motility and localization by a splicing-dependent structure in oskar mRNA. Nat Struct Mol Biol, 2012. 19(4): p. 441-9. 20. Hachet, O. and A. Ephrussi, Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport. Curr Biol, 2001. 11(21): p. 1666-74. 21. Kim-Ha, J., et al., Multiple RNA regulatory elements mediate distinct steps in localization of oskar mRNA. Development, 1993. 119(1): p. 169-78. 22. Castagnetti, S., et al., Control of oskar mRNA translation by Bruno in a novel cell-free system from Drosophila ovaries. Development, 2000. 127(5): p. 1063-8. 23. Micklem, D.R., et al., Distinct roles of two conserved Staufen domains in oskar mRNA localization and translation. EMBO J, 2000. 19(6): p. 1366-77. 24. Nakamura, A., et al., Me31B silences translation of oocyte-localizing RNAs through the formation of cytoplasmic RNP complex during Drosophila oogenesis. Development, 2001. 128(17): p. 3233-42. 25. Nakamura, A., K. Sato, and K. Hanyu-Nakamura, Drosophila cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis. Dev Cell, 2004. 6(1): p. 69-78. 26. Markussen, F.H., et al., Translational control of oskar generates short OSK, the isoform that induces pole plasma assembly. Development, 1995. 121(11): p. 3723-32. 27. Riechmann, V., et al., Par-1 regulates stability of the posterior determinant Oskar by phosphorylation. Nat Cell Biol, 2002. 4(5): p. 337-42. 28. Vanzo, N.F. and A. Ephrussi, Oskar anchoring restricts pole plasm formation to the posterior of the Drosophila oocyte. Development, 2002. 129(15): p. 3705-14. 29. Glotzer, J.B., et al., Cytoplasmic flows localize injected oskar RNA in Drosophila oocytes. Curr Biol, 1997. 7(5): p. 326-37. 30. Cha, B.J., et al., Kinesin I-dependent cortical exclusion restricts pole plasm to the oocyte posterior. Nat Cell Biol, 2002. 4(8): p. 592-8. 31. Januschke, J., et al., The centrosome-nucleus complex and microtubule organization in the Drosophila oocyte. Development, 2006. 133(1): p. 129-39. 32. Zimyanin, V.L., et al., In vivo imaging of oskar mRNA transport reveals the mechanism of posterior localization. Cell, 2008. 134(5): p. 843-53. 33. Lie, Y.S. and P.M. Macdonald, Apontic binds the translational repressor Bruno and is implicated in regulation of oskar mRNA translation. Development, 1999. 126(6): p. 1129-38. 34. Wilhelm, J.E., et al., Cup is an eIF4E binding protein required for both the translational repression of oskar and the recruitment of Barentsz. J Cell Biol, 2003. 163(6): p. 1197-204. 35. Kinkelin, K., et al., Crystal structure of a minimal eIF4E-Cup complex reveals a general mechanism of eIF4E regulation in translational repression. RNA, 2012. 18(9): p. 1624-34. 36. Chekulaeva, M., M.W. Hentze, and A. Ephrussi, Bruno acts as a dual repressor of oskar translation, promoting mRNA oligomerization and formation of silencing particles. Cell, 2006. 124(3): p. 521-33. 37. Kim, G., et al., Region-specific activation of oskar mRNA translation by inhibition of Bruno-mediated repression. PLoS Genet, 2015. 11(2): p. e1004992. 38. Castagnetti, S. and A. Ephrussi, Orb and a long poly(A) tail are required for efficient oskar translation at the posterior pole of the Drosophila oocyte. Development, 2003. 130(5): p. 835-43. 39. Vazquez-Pianzola, P., H. Urlaub, and B. Suter, Pabp binds to the osk 3'UTR and specifically contributes to osk mRNA stability and oocyte accumulation. Dev Biol, 2011. 357(2): p. 404-18. 40. Garneau, N.L., J. Wilusz, and C.J. Wilusz, The highways and byways of mRNA decay. Nat Rev Mol Cell Biol, 2007. 8(2): p. 113-26. 41. Parker, R. and H. Song, The enzymes and control of eukaryotic mRNA turnover. Nat Struct Mol Biol, 2004. 11(2): p. 121-7. 42. Beelman, C.A., et al., An essential component of the decapping enzyme required for normal rates of mRNA turnover. Nature, 1996. 382(6592): p. 642-6. 43. Dunckley, T. and R. Parker, The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif. EMBO J, 1999. 18(19): p. 5411-22. 44. Sheth, U. and R. Parker, Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science, 2003. 300(5620): p. 805-8. 45. Tharun, S., et al., Yeast Sm-like proteins function in mRNA decapping and decay. Nature, 2000. 404(6777): p. 515-8. 46. Kedersha, N., et al., Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J Cell Biol, 2005. 169(6): p. 871-84. 47. Brengues, M., D. Teixeira, and R. Parker, Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science, 2005. 310(5747): p. 486-9. 48. Liu, J., et al., A role for the P-body component GW182 in microRNA function. Nat Cell Biol, 2005. 7(12): p. 1261-6. 49. Parker, R. and U. Sheth, P bodies and the control of mRNA translation and degradation. Mol Cell, 2007. 25(5): p. 635-46. 50. Lin, M.D., et al., Drosophila processing bodies in oogenesis. Dev Biol, 2008. 322(2): p. 276-88. 51. Yu, J.H., et al., Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body. RNA, 2005. 11(12): p. 1795-802. 52. Fenger-Gron, M., et al., Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol Cell, 2005. 20(6): p. 905-15. 53. Yang, Z., et al., GW182 is critical for the stability of GW bodies expressed during the cell cycle and cell proliferation. J Cell Sci, 2004. 117(Pt 23): p. 5567-78. 54. LaGrandeur, T.E. and R. Parker, Isolation and characterization of Dcp1p, the yeast mRNA decapping enzyme. EMBO J, 1998. 17(5): p. 1487-96. 55. Xu, J., et al., Arabidopsis DCP2, DCP1, and VARICOSE form a decapping complex required for postembryonic development. Plant Cell, 2006. 18(12): p. 3386-98. 56. Jinek, M., et al., The C-terminal region of Ge-1 presents conserved structural features required for P-body localization. RNA, 2008. 14(10): p. 1991-8. 57. Lin, M.D., et al., Drosophila decapping protein 1, dDcp1, is a component of the oskar mRNP complex and directs its posterior localization in the oocyte. Dev Cell, 2006. 10(5): p. 601-13. 58. Fan, S.J., V. Marchand, and A. Ephrussi, Drosophila Ge-1 promotes P body formation and oskar mRNA localization. PLoS One, 2011. 6(5): p. e20612. 59. She, M., et al., Structural basis of dcp2 recognition and activation by dcp1. Mol Cell, 2008. 29(3): p. 337-49. 60. van Dijk, E., et al., Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J, 2002. 21(24): p. 6915-24. 61. Wang, Z., et al., The hDcp2 protein is a mammalian mRNA decapping enzyme. Proc Natl Acad Sci U S A, 2002. 99(20): p. 12663-8. 62. Lykke-Andersen, J., Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay. Mol Cell Biol, 2002. 22(23): p. 8114-21. 63. Chang, C.T., et al., The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1. Nucleic Acids Res, 2014. 42(8): p. 5217-33. 64. She, M., et al., Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe. Nat Struct Mol Biol, 2006. 13(1): p. 63-70. 65. Schwartz, D.C. and R. Parker, Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae. Mol Cell Biol, 1999. 19(8): p. 5247-56. 66. Schwartz, D.C. and R. Parker, mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E. Mol Cell Biol, 2000. 20(21): p. 7933-42. 67. Kim-Ha, J., K. Kerr, and P.M. Macdonald, Translational regulation of oskar mRNA by bruno, an ovarian RNA-binding protein, is essential. Cell, 1995. 81(3): p. 403-12. 68. Rongo, C., E.R. Gavis, and R. Lehmann, Localization of oskar RNA regulates oskar translation and requires Oskar protein. Development, 1995. 121(9): p. 2737-46. 69. Chen, C.-H., Analysis of drosophila decapping protein 2, ddcp2, in axis determination during drosophila oogenesis, in National Taiwan University. 2006, Master thesis, National Taiwan University. 70. Wu, M.-L., The genomic analysis of drosophila decapping protein 2, dDcp2, in National Taiwan University. 2006, Master thesis, National Taiwan University. 71. Ling, S.H., R. Qamra, and H. Song, Structural and functional insights into eukaryotic mRNA decapping. Wiley Interdiscip Rev RNA, 2011. 2(2): p. 193-208. 72. Tharun, S. and R. Parker, Analysis of mutations in the yeast mRNA decapping enzyme. Genetics, 1999. 151(4): p. 1273-85. 73. Coller, J. and R. Parker, Eukaryotic mRNA decapping. Annu Rev Biochem, 2004. 73: p. 861-90. 74. Sakuno, T., et al., Decapping reaction of mRNA requires Dcp1 in fission yeast: its characterization in different species from yeast to human. J Biochem, 2004. 136(6): p. 805-12. 75. Steiger, M., et al., Analysis of recombinant yeast decapping enzyme. RNA, 2003. 9(2): p. 231-8. 76. Tritschler, F., et al., DCP1 forms asymmetric trimers to assemble into active mRNA decapping complexes in metazoa. Proc Natl Acad Sci U S A, 2009. 106(51): p. 21591-6. 77. Tian, Y.-L., Drosophila decapping protein 2, dDcp2, regulates the cytoplasmic streaming of the oocyte, in National Taiwan University. 2008, Master thesis, National Taiwan University. 78. Meignin, C. and I. Davis, Transmitting the message: intracellular mRNA localization. Curr Opin Cell Biol, 2010. 22(1): p. 112-9. 79. Shen, W.-H., Drosophila decapping protein 2, dDcp2, participates in the regulation of microtubule dynamics, in National Taiwan University. 2010, Master thesis, National Taiwan University. 80. Lu, C.-C., The analysis of interactions between Drosophila processing-body components and Dmoesin, in National Taiwan University. 2014, Master thesis, National Taiwan University. 81. Cheng, J.-H., Dynamic processing body component drosophila decapping protein 1, dDcp1, in follicle cells and the oocyte, in National Taiwan University. 2009, Master thesis, National Taiwan University. 82. Bertrand, E., et al., Localization of ASH1 mRNA particles in living yeast. Mol Cell, 1998. 2(4): p. 437-45. 83. Chiang, P.-H., dDcp1-dDcp2A-dGe-1 form a complex and the analysis of dDcp2A function in F-actin behavior in the Drosophila oocyte, in National Taiwan University. 2014, Master thesis, National Taiwan University. 84. Caponigro, G. and R. Parker, Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast. Genes Dev, 1995. 9(19): p. 2421-32. 85. Chuang, T.W., et al., The RNA-binding protein Y14 inhibits mRNA decapping and modulates processing body formation. Mol Biol Cell, 2013. 24(1): p. 1-13. 86. Akhmanova, A. and M.O. Steinmetz, Microtubule +TIPs at a glance. J Cell Sci, 2010. 123(Pt 20): p. 3415-9. 87. Do, K.K., K.L. Hoang, and S.A. Endow, The kinesin-13 KLP10A motor regulates oocyte spindle length and affects EB1 binding without altering microtubule growth rates. Biol Open, 2014. 3(7): p. 561-70. 88. Gu, C., et al., The microtubule plus-end tracking protein EB1 is required for Kv1 voltage-gated K+ channel axonal targeting. Neuron, 2006. 52(5): p. 803-16. 89. Alves-Silva, J., et al., Spectraplakins promote microtubule-mediated axonal growth by functioning as structural microtubule-associated proteins and EB1-dependent +TIPs (tip interacting proteins). J Neurosci, 2012. 32(27): p. 9143-58. 90. Tian, A.G. and W.M. Deng, Par-1 and Tau regulate the anterior-posterior gradient of microtubules in Drosophila oocytes. Dev Biol, 2009. 327(2): p. 458-64. 91. Lai, Y.-C., Drosophila decapping protein 2, dDcP2,regulates microtubule organization in the oocyte, in National Taiwan University. 2009, Master thesis, National Taiwan University. 92. Alberts B., J.A., Lewis J., Raff M., Roberts K., Walter P., Molecular biology of the cell. 5th ed.. ed, ed. B. Alberts. 2008, New York: New York : Garland Science. 93. Bonne, D., et al., 4',6-Diamidino-2-phenylindole, a fluorescent probe for tubulin and microtubules. J Biol Chem, 1985. 260(5): p. 2819-25. 94. Aizer, A., et al., The dynamics of mammalian P body transport, assembly, and disassembly in vivo. Mol Biol Cell, 2008. 19(10): p. 4154-66. 95. Lantz, V.A., S.E. Clemens, and K.G. Miller, The actin cytoskeleton is required for maintenance of posterior pole plasm components in the Drosophila embryo. Mech Dev, 1999. 85(1-2): p. 111-22. 96. Shulman, J.M., R. Benton, and D. St Johnston, The Drosophila homolog of C. elegans PAR-1 organizes the oocyte cytoskeleton and directs oskar mRNA localization to the posterior pole. Cell, 2000. 101(4): p. 377-88. 97. Doerflinger, H., et al., Drosophila anterior-posterior polarity requires actin-dependent PAR-1 recruitment to the oocyte posterior. Curr Biol, 2006. 16(11): p. 1090-5. 98. Vanzo, N., et al., Stimulation of endocytosis and actin dynamics by Oskar polarizes the Drosophila oocyte. Dev Cell, 2007. 12(4): p. 543-55. 99. Tanaka, T. and A. Nakamura, The endocytic pathway acts downstream of Oskar in Drosophila germ plasm assembly. Development, 2008. 135(6): p. 1107-17. 100. Tanaka, T., et al., Drosophila Mon2 couples Oskar-induced endocytosis with actin remodeling for cortical anchorage of the germ plasm. Development, 2011. 138(12): p. 2523-32. 101. Chang, C.W., et al., Anterior-posterior axis specification in Drosophila oocytes: identification of novel bicoid and oskar mRNA localization factors. Genetics, 2011. 188(4): p. 883-96. 102. Manseau, L., J. Calley, and H. Phan, Profilin is required for posterior patterning of the Drosophila oocyte. Development, 1996. 122(7): p. 2109-16. 103. Tetzlaff, M.T., H. Jackle, and M.J. Pankratz, Lack of Drosophila cytoskeletal tropomyosin affects head morphogenesis and the accumulation of oskar mRNA required for germ cell formation. EMBO J, 1996. 15(6): p. 1247-54. 104. Veeranan-Karmegam, R., et al., A new isoform of Drosophila non-muscle Tropomyosin 1 interacts with Kinesin-1 and functions in oskar mRNA localization. J Cell Sci, 2016. 129(22): p. 4252-4264. 105. Suyama, R., et al., The actin-binding protein Lasp promotes Oskar accumulation at the posterior pole of the Drosophila embryo. Development, 2009. 136(1): p. 95-105. 106. Jankovics, F., et al., MOESIN crosslinks actin and cell membrane in Drosophila oocytes and is required for OSKAR anchoring. Curr Biol, 2002. 12(23): p. 2060-5. 107. Polesello, C., et al., Dmoesin controls actin-based cell shape and polarity during Drosophila melanogaster oogenesis. Nat Cell Biol, 2002. 4(10): p. 782-9. 108. Srivastava, J. and D. Barber, Actin co-sedimentation assay; for the analysis of protein binding to F-actin. J Vis Exp, 2008(13). 109. Tanaka, T. and A. Nakamura, Oskar-induced endocytic activation and actin remodeling for anchorage of the Drosophila germ plasm. Bioarchitecture, 2011. 1(3): p. 122-126. 110. Tsai, Y.-H., Investigate the upstream regulators for dmoesin phosphorylation in the oocyte and the relationship between drosophila decapping protein 2 and cappuccino, in National Taiwan University. 2017, Master thesis, National Taiwan University. 111. Guo, S. and K.J. Kemphues, par-1, a gene required for establishing polarity in C. elegans embryos, encodes a putative Ser/Thr kinase that is asymmetrically distributed. Cell, 1995. 81(4): p. 611-20. 112. Parton, R.M., et al., A PAR-1-dependent orientation gradient of dynamic microtubules directs posterior cargo transport in the Drosophila oocyte. J Cell Biol, 2011. 194(1): p. 121-35. 113. Doerflinger, H., et al., Bazooka is required for polarisation of the Drosophila anterior-posterior axis. Development, 2010. 137(10): p. 1765-73. 114. Bretscher, A., K. Edwards, and R.G. Fehon, ERM proteins and merlin: integrators at the cell cortex. Nat Rev Mol Cell Biol, 2002. 3(8): p. 586-99. 115. Fehon, R.G., A.I. McClatchey, and A. Bretscher, Organizing the cell cortex: the role of ERM proteins. Nat Rev Mol Cell Biol, 2010. 11(4): p. 276-87. 116. Solinet, S., et al., The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex. J Cell Biol, 2013. 202(2): p. 251-60. 117. Vilmos, P., et al., The actin-binding ERM protein Moesin directly regulates spindle assembly and function during mitosis. Cell Biol Int, 2016. 40(6): p. 696-707. 118. Verdier, V., et al., Drosophila Rho-kinase (DRok) is required for tissue morphogenesis in diverse compartments of the egg chamber during oogenesis. Dev Biol, 2006. 297(2): p. 417-32. 119. Hughes, S.C., E. Formstecher, and R.G. Fehon, Sip1, the Drosophila orthologue of EBP50/NHERF1, functions with the sterile 20 family kinase Slik to regulate Moesin activity. J Cell Sci, 2010. 123(Pt 7): p. 1099-107. 120. Huang, L., et al., Replacement of threonine 558, a critical site of phosphorylation of moesin in vivo, with aspartate activates F-actin binding of moesin. Regulation by conformational change. J Biol Chem, 1999. 274(18): p. 12803-10. 121. Manseau, L.J. and T. Schupbach, cappuccino and spire: two unique maternal-effect loci required for both the anteroposterior and dorsoventral patterns of the Drosophila embryo. Genes Dev, 1989. 3(9): p. 1437-52. 122. Coutelis, J.B. and A. Ephrussi, Rab6 mediates membrane organization and determinant localization during Drosophila oogenesis. Development, 2007. 134(7): p. 1419-30. 123. Cheng, C.-Y., Processing body components cooperate to assist the posterior localization of oskar mRNP complex in the oocyte, in Processing body components cooperate to assist the posterior localization of oskar mRNP complex in the oocyte. 2012, Master thesis, National Taiwan University. 124. Weil, T.T., et al., Drosophila patterning is established by differential association of mRNAs with P bodies. Nat Cell Biol, 2012. 14(12): p. 1305-13. 125. Zimyanin, V., N. Lowe, and D. St Johnston, An oskar-dependent positive feedback loop maintains the polarity of the Drosophila oocyte. Curr Biol, 2007. 17(4): p. 353-9. 126. Deng, J.-Y., Dmoesin regulates the anchorage of oskar mRNP complex in drosophila oocyte, in National Taiwan University. 2017, Master thesis, National Taiwan University. 127. Liu, Y.-C., Developmental genetic study of dHedls, Drosophila homologue of human enhancer of decapping large subunit. National Taiwan University, 2008. 128. Clark, I.E., L.Y. Jan, and Y.N. Jan, Reciprocal localization of Nod and kinesin fusion proteins indicates microtubule polarity in the Drosophila oocyte, epithelium, neuron and muscle. Development, 1997. 124(2): p. 461-70. 129. Liu, S.W., et al., Analysis of mRNA decapping. Methods Enzymol, 2008. 448: p. 3-21. 130. Karpova, N., et al., Jupiter, a new Drosophila protein associated with microtubules. Cell Motil Cytoskeleton, 2006. 63(5): p. 301-12. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/70612 | - |
dc.description.abstract | 在果蠅(Drosophila. melanogaster)卵發育(oogenesis)過程中,oskar 訊息核醣核酸(oskar mRNA)被運送、坐落於卵母細胞後端,決定了胚胎後端體節的發育與生殖細胞的前驅細胞(極細胞pole cell)的產生。核糖核酸代謝裂解體(mRNA processing bodies, P-bodies)主要功能負責5’到3’核糖核酸裂解,也參與核糖核酸運送、剪接、儲存或轉譯抑制等相關機制。之前的研究顯示去蓋頭蛋白質1 (dDcp1)為oskar mRNA蛋白質複合體的成員;但對於dDcp1為何參與在oskar mRNA座落於卵後端調控機制中扮演的角色尚不清楚。本論文研究動機為找到P-bodies在oskar mRNA後端坐落調控機制扮演的功能探討。在此論文中,我提出P-bodies成員dDcp1, 去蓋頭蛋白質2 (dDcp2),促進去蓋頭大蛋白(dGe-1)與果蠅膜突蛋白(Drosophila moesin, Dmoesin)共同作用於oskar mRNA在卵母細胞的運送與正確定錨。
首先、我發現dDcp1、dDcp2和dGe-1在卵母細胞中以去蓋頭複合體(decapping complex)的方式坐落於細胞皮層(Cortex),而且dDcp2決定dDcp1和dGe-1正確坐落在細胞皮層,比較之前單個基因對於oskar mRNA在卵母細胞中扮演角色分析,我推測整個複合體必須先形成才進而調控oskar mRNA在卵母細胞後端的定位。再者、文獻指出微管骨架 (microtubule cytoskeleton)和纖維絲肌動蛋白(Filamentous-actin, F-actin)分別參與oskar mRNA的運送和定錨。我也發現dDcp2對微管生長和纖維性肌動蛋白的建構皆有正面調控的功能,綜合以上推測decapping complex可能藉由對微管骨架和纖維絲肌動蛋白的正面調控來幫助oskar mRNA的運送和定錨。 其三、Dmoesin負責連結細胞膜和纖維絲肌動蛋白,以維持細胞形狀,在卵母細胞的皮層上,可以明顯地測到果蠅膜突蛋白。我發現dDcp2與Dmoesin互相依附地(mutually-dependent)座落於皮層上;當一方突變缺失時,另一方伴隨纖維絲肌動蛋白同時脫落於卵母細胞質中。先前研究指出,在卵發育的滋養細胞(nurse cells)與卵母細胞質中,oskar mRNA蛋白質複合體與P-bodies處於動態地進行成員互換;意即oskar mRNA處在隨時可被裂解的P-bodie中,然而Dmoesin抑制dDcp2的mRNA去蓋頭酵素活性,可避免oskar mRNA在卵發育過程被降解掉。此外,Dmoesin的磷酸化狀態可決定dDcp2在卵母細胞中的分布位置,過量表現磷酸化的Dmoesin可累積較多的dDcp2坐落在細胞皮層,反之表現非磷酸化Dmoesin使dDcp2散布在細胞質。 我綜合上述結果與實驗室前人研究成果,提出:一、果蠅膜突蛋白和去蓋頭蛋白質2在卵母細胞皮層形成oskar訊息核醣核酸的定錨者(anchor);二、去蓋頭蛋白2和果蠅膜突蛋白組成oskar訊息核醣核酸的輸送複合體(the transporting complex)和定錨複合體(the anchoring complex),藉由調控果蠅膜突蛋白的磷酸化狀態,兩複合體在卵母細胞後端進行動態轉換,最終完成oskar訊息核醣核酸在卵母細胞後端的定錨。 | zh_TW |
dc.description.abstract | During oogenesis in the fruit fly (Drosophila melanogaster), oskar mRNA is delivered and localized to the posterior, and thereby also promotes the assembly of germ plasm, which is a specialized cytoplasm for germ-cell formation. Processing bodies (P-bodies) of mRNA are sites that 5’ to 3’ mRNA degradation happens, including the removal of 5’ cap on mRNA and mRNA exonuclease activity. In a previous study, the Drosophila decapping protein 1 (dDcp1) has been found as a component of the oskar messenger ribonucleoprotein (mRNP), directing its posterior localization. In this study, I aimed to the three components of a decapping complex (dDcp1, Drosophila decapping protein 2 (dDcp2) and dGe-1) cooperating with Drosophila moesin (Dmoesin) participates in the transport and anchoring of oskar mRNP in the oocyte.
First, I found that the trimeric complex forming by dDcp1, dDcp2, and dGe-1 stands along the oocyte cortex and is required for the posterior localization of oskar mRNA. Moreover, the presence of dDcp2 plays a critical role in sustaining the cortical localizations of dDcp1 and dGe-1 in oocytes. Second, previous studies point out that microtubule cytoskeleton is responsible for the oskar mRNA transport and F-actin microfilaments facilitate the oskar mRNA anchorage. I found that dDcp2, except the mRNA decapping activity, shows a positive regulation both on the microtubule growth and F-actin proper formation in oocytes. Third, Dmoesin is a crosslinker connecting the membrane and F-actin along the cortex. dDcp2 and Dmoesin show a mutually-dependent adherecne along the oocyte cortex. Lastly, the phosphorylation status of Dmoeisn determines the allocation of dDcp2 in the oocyte. Overexpression of phospho-Dmoesin accumulates the cortical dDcp2, whereas overexpression of nonphospho-Dmoeisn draws dDcp2 into the ooplasm. Hence, we propose that from stage 6 dDcp2 and phospho-Dmoesin form a pre-localized anchor for locate oskar mRNA along the cortex. And Dmoesin-dDcp2 recruit oskar mRNA-dDcp1-dGe-1 to be the anchoring complex. nonphospho-Dmoe and dDcp2 organize a transporting complex to move oskar mRNA-dDcp1 from the cortex. At the posterior, phosphorylation status exchange the components of the two complex and oskar mRNA can be anchored properly. | en |
dc.description.provenance | Made available in DSpace on 2021-06-17T04:32:34Z (GMT). No. of bitstreams: 1 ntu-107-D98b43002-1.pdf: 7740937 bytes, checksum: 6855eaab0c117ec6ab32804e6b3f91fe (MD5) Previous issue date: 2018 | en |
dc.description.tableofcontents | 口試委員會審定書
致謝 ii 中文摘要 iii Abstract v Table of contents vii List of tables xvii List of figures xviii Abbreviations xxii Chapter 1: Main introduction 1 Main Introduction 2 I. The Drosophila oogenesis 2 II. Microtubule and motor proteins 3 III. The rearrangements of a microtubule polarity determine the localizations of maternal messenger RNAs during oogenesis 4 IV. Four essential elements are required for the posterior localization of oskar mRNP 5 1. Cis-acting sequence and oskar mRNP 6 2. Two Osk isoforms are produced and show a different function 6 3. Trans-factors of oskar mRNP 7 4. Kinesin-heavy chain mediates the posterior localization of oskar mRNP in the oocyte 7 5. The translation of oskar mRNA is repressed during the process of its transport 8 6. A anchor for oskar mRNA localization in an oocyte 10 V. Processing body components are involved in the oskar mRNP localization 12 1. mRNA degradation involves multiple activities 12 2. The discovery of the processing body 12 3. The main markers of P-bodies: the decapping complex 13 4. Decapping protein 1 14 5. Decapping protein 2 (Dcp2) 15 6. Ge-1/Human enhancer of decapping large subunit/Enhancer of Decapping Coactivactor 4 is essential for the decapping complex 16 7. osk mRNP is a modified processing body 17 VI. A Brief of this thesis 18 Chapter 2: dDcp2 forms a trimeric complex with dDcp1 and dGe-1 in the oocyte posterior 20 Summary 21 Introduction 22 I. The interaction of Dcp1p and Dcp2p in yeast 22 II. The interaction of Dcp1, Dcp2 and VARICOSE in plant 24 III. The interaction of Dcp1a, Dcp2 and Hedls/Ge-1 in human 24 IV. Dcp2 in fly is required for development 25 V. dDcp2 is required for the localization of oskar mRNP at the posterior in the oocyte 26 VI. The brief of the chapter 26 Results 28 I. dDcp2 shows a cortical localization in the oocytes. 28 II. dDcp1, dDcp2, and dGe-1 form a complex in vivo 29 III. dDcp2 has an intimate localization with oskar mRNA at the posterior cortex in the oocyte 30 IV. The posterior crescent of dDcp1 and cortical localization of dGe-1 depend on the presence of dDcp2 in the oocytes 31 Discussion 32 I. The interactions of dDcp1-dDcp2-dGe-1 in Drosophila and human 32 II. The repression of the decapping complex in oogenesis 33 Chapter 3: dDcp2 displays a positive function for microtubule organization 34 Summary 35 Introduction 36 I. The cycle of Microtubule growth and shrinkage is dynamic in cells 36 II. Microtubule reorganization establishes the polarity and facilitates the localizations of maternal mRNAs in the oocytes 37 III. A brief of this chapter 38 Results 39 I. dDcp2 partially colocalizes with microtubules in the oocytes 39 II. dDcp2 is a microtubule-associated protein 40 III. dDcp2 and dDcp2–NA can stabilize the microtubule polymerization in vitro 41 IV. EGFP- dDcp2 moves with an anterior to posterior direction in the oocytes 44 Discussion 45 I. dDcp2 presents a positive regulation on MT growth and stabilization 45 II. P-body components participate in the MT dynamics 46 Chapter 4: dDcp2 is required for F-actin formation in oogenesis 47 Summary 48 Introduction 49 I. F-actin is essential for osk mRNP and pole plasm localization in the posterior cortex of the oocyte 49 II. A Long Osk-dependent F-actin remodeling machinery promotes the anchorage of oskar mRNA at the posterior cortex 49 III. F-actin associated proteins promote oskar mRNP posterior localization 51 IV. A brief of this chapter 53 Results 54 I. dDcp2 interacts with F-actin in vivo and in vitro 54 II. dDcp2 is essential for the posterior F-actin projection and cortical F-actin distribution 55 III. Ectopic expression of dDcp2 can promote the F-actin in remodeling at the anterior pole of the oocytes 57 Discussion 58 I. dDcp2 may act as the downstream of Osk signaling in the oocyte 58 II. dDcp2 participates in the posterior F-actin remodeling 59 III. dDcp2 probably participates in the posterior Par-1 localization 60 Chapter 5: dDcp2 interacts intimately with Dmoesin in the oocyte 62 Summary 63 Introduction 65 I. Dmoesin is the only homolog of ERM family in Drosophila 65 II. Dmoesin activation depends on its phosphorylation status 65 III. Dmoesin is required for the posterior Osk anchorage 66 IV. Dmoeisn showed a positive IP interaction with dDcp2 in S2 cells 66 V. Dmoesin FERM fragment interacts with dDcp2-M physically 67 VI. A brief of this chapter 67 Results 68 I. F-actin severe clumps present in dDcp2del21 GLC oocytes 68 II. The cortical localization of dDcp2 is independent on F-actin 68 III. The cortical localization of dDcp2 and Dmoesin is mutually-dependent 69 1. p-Dmoe and dDcp2 show a mutually-dependent relationship for their adherence along the cortex 69 2. p-Dmoesin becomes detached in the oocytes of W1E360A/E361A; dDcp2del21 GLC egg chambers 70 IV. The decapping complex can enhance the dDcp2 decapping enzyme activity 71 V. Dmoesin represses the dDcp2 decapping activity 73 VI. Both ovarian phospho-Dmoesin and nonphospho-Dmoesin show a repression ability of dDcp2 decapping activity 77 Discussion 80 I. dDcp2 and Dmoesin have a tight interaction in an oocyte 80 II. The osk mRNA stability is properly controlled during the transport and anchoring at the posterior pole 81 Chapter 6: Phospho-Dmoesin and dDcp2 form an anchor for osk mRNP cortical allocation 83 Summary 84 Introduction 86 I. A putative anchor for oskar mRNA localization in an oocyte 86 II. A brief of this chapter 87 Results 88 I. Phosphorylation status of Dmoesin determines the allocation of dDcp2 in the oocyte 88 II. Phosphorylation status of Dmoe cooperates with dDcp2 to affect the Osk localization in the oocytes 88 III. Nonp-Dmoe and dDcp2 overexpression caused the appearance of ectopic Osk protein dot near the posterior end of the oocyte 90 IV. p-Dmoe and dDcp2 double overexpression resulted in the decrease of posterior Osk 91 V. Different phosphorylation status of Dmoe cooperates with dDcp2 to mediate oskar mRNA allocations in the oocytes 93 VI. osk mRNA becomes diffused in the nonp-Dmoe and dDcp2 overexpressing oocytes 94 VII. oskar mRNA allocates along the lateral-posterior cortex in p-Dmoe and dDcp2 overexpressing oocytes 95 Discussion 97 I. p-Dmoe and dDcp2 organize a pre-localized anchor for osk mRNA 97 II. There are a transporting and an anchoring complexes for osk mRNP in the oocyte. 98 1. The prelocalized anchor, phospho-Dmoe and dDcp2, constitute the anchoring complex with dDcp1-dGe-1 and osk mRNA along the cortex 98 2. Nonphospho-Dmoe and dDcp2 constitute the transporting complex 98 Chapter 7: Dmoesin and dDcp2 constitute the transporting and anchoring complexes for oskar mRNP 100 Summary 101 Introduction 103 I. The posterior preference for osk mRNP localization 103 II. A brief of this chapter 103 Results 105 I. Ectopic Osk dot in UASp-osk oocytes supports the presence of the transporting complex caused in nonp-Dmoe and dDcp2 overexpressing oocyte 105 II. Overexpression of dDcp2 can compensate the shortage of the transporting capacity in UASp-osk overexpression 105 III. The alternation of Dmoe phosphorylation states can respond to the increase of osk mRNA 106 IV. The components of the transporting complex 107 V. Phospho-Dmoesin restricts dDcp2 positive function for microtubule growth. 107 VI. A-P gradient and MT bundles in WT-Dmoe and dDcp2 overexpression were comparable to the wild-type. 108 VII. An evenly distribution of MT at stage 9 was observed in phospho-Dmoe and dDcp2 expressing oocytes. 108 VIII. A cortical anchoring MT staining at stage 10B were shown in phospho-Dmoe and dDcp2 expressing oocytes. 109 I. The osk mRNP anchoring complex 110 II. The osk mRNP transporting complex 110 Chapter 8 Materials and methods 112 Fly stocks 113 I. Genetic abbreviations 113 Constructions 115 Transgenic flies 117 Antibody Generation 118 Antibodies and reagents 119 Ovary immunofluorescence staining 119 Whole-mount ovary in situ hybridization 121 Western blotting and Immunoprecipitation (IP) 122 Recombinant protein expression and purification 123 F-actin binding assay 124 In vitro decapping assay 124 Quantitative Real-Time Polymorphism Chain Reaction (qPCR) 126 Microtubule sedimentation assay 126 Preparation of Assembly-Competent Axonemal Tubulin 127 Turbidity Assay of Tubulin Polymerization 128 Chapter 9 References 129 Tables and Figures 139 | |
dc.language.iso | en | |
dc.title | 核糖核酸降解複合體成員及膜突蛋白在果蠅卵細胞中調控oskar核糖核酸的運送與定錨 | zh_TW |
dc.title | Components of mRNA Processing Body and Dmoesin Control the Transport and Anchorage of oskar mRNA in the Drosophila oocyte | en |
dc.type | Thesis | |
dc.date.schoolyear | 106-2 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 莊志立,張俊哲,董桂書,林明德 | |
dc.subject.keyword | 核糖核酸降解複合體,膜突蛋白,oskar核糖核酸,果蠅卵細胞, | zh_TW |
dc.subject.keyword | oskar mRNP,Transport,Anchorage,dDcp1,dDcp2,dGe-1,Drosophila moesin,Processing bodies, | en |
dc.relation.page | 202 | |
dc.identifier.doi | 10.6342/NTU201802955 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2018-08-10 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 分子與細胞生物學研究所 | zh_TW |
顯示於系所單位: | 分子與細胞生物學研究所 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-107-1.pdf 目前未授權公開取用 | 7.56 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。