메뉴 건너뛰기




Volumn 2, Issue 2, 2013, Pages 170-182

Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition

Author keywords

Maternal to zygotic transition; Ubiquitin proteasome system; ZPAC

Indexed keywords


EID: 84965021883     PISSN: None     EISSN: 20466390     Source Type: Journal    
DOI: 10.1242/bio.20123020     Document Type: Article
Times cited : (26)

References (53)
  • 2
    • 62149097545 scopus 로고    scopus 로고
    • Expression and functional analyses of circadian genes in mouse oocytes and preimplantation embryos: Cry1 is involved in the meiotic process independently of circadian clock regulation
    • Amano, T., Matsushita, A., Hatanaka, Y., Watanabe, T., Oishi, K., Ishida, N., Anzai, M., Mitani, T., Kato, H., Kishigami, S. et al. (2009). Expression and functional analyses of circadian genes in mouse oocytes and preimplantation embryos: Cry1 is involved in the meiotic process independently of circadian clock regulation. Biol. Reprod. 80, 473-483.
    • (2009) Biol. Reprod. , vol.80 , pp. 473-483
    • Amano, T.1    Matsushita, A.2    Hatanaka, Y.3    Watanabe, T.4    Oishi, K.5    Ishida, N.6    Anzai, M.7    Mitani, T.8    Kato, H.9    Kishigami, S.10
  • 3
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister, W., Walz, J., Zühl, F. and Seemüller, E. (1998). The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 4
    • 33644859083 scopus 로고    scopus 로고
    • The ubiquitin proteolytic system: From a vague idea, through basic mechanisms, and onto human diseases and drug targeting
    • Ciechanover, A. (2006). The ubiquitin proteolytic system: from a vague idea, through basic mechanisms, and onto human diseases and drug targeting. Neurology 66 Suppl 1, S7-S19.
    • (2006) Neurology , vol.66 , pp. S7-S19
    • Ciechanover, A.1
  • 5
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K. and Goldberg, A. L. (1996). Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 6
    • 4143072546 scopus 로고    scopus 로고
    • A clean start: Degradation of maternal proteins at the oocyte-to-embryo transition
    • DeRenzo, C. and Seydoux, G. (2004). A clean start: degradation of maternal proteins at the oocyte-to-embryo transition. Trends Cell Biol. 14, 420-426.
    • (2004) Trends Cell Biol. , vol.14 , pp. 420-426
    • DeRenzo, C.1    Seydoux, G.2
  • 7
    • 33745829795 scopus 로고    scopus 로고
    • Molecular chaperones: Assisting assembly in addition to folding
    • Ellis, R. J. (2006). Molecular chaperones: assisting assembly in addition to folding. Trends Biochem. Sci. 31, 395-401.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 395-401
    • Ellis, R.J.1
  • 8
    • 67650832144 scopus 로고    scopus 로고
    • Gene expression during the oocyteto-embryo transition in mammals
    • Evsikov, A. V. and Marín de Evsikova, C. (2009). Gene expression during the oocyteto-embryo transition in mammals. Mol. Reprod. Dev. 76, 805-818.
    • (2009) Mol. Reprod. Dev. , vol.76 , pp. 805-818
    • Evsikov, A.V.1    Marín De-Evsikova, C.2
  • 10
  • 11
    • 36749025650 scopus 로고    scopus 로고
    • The proteasome maturation protein POMP facilitates major steps of 20S proteasome formation at the endoplasmic reticulum
    • Fricke, B., Heink, S., Steffen, J., Kloetzel, P. M. and Krüger, E. (2007). The proteasome maturation protein POMP facilitates major steps of 20S proteasome formation at the endoplasmic reticulum. EMBO Rep. 8, 1170-1175.
    • (2007) EMBO Rep. , vol.8 , pp. 1170-1175
    • Fricke, B.1    Heink, S.2    Steffen, J.3    Kloetzel, P.M.4    Krüger, E.5
  • 12
    • 21544475903 scopus 로고    scopus 로고
    • IFN-γ-induced immune adaptation of the proteasome system is an accelerated and transient response
    • Heink, S., Ludwig, D., Kloetzel, P. M. and Krüger, E. (2005). IFN-γ-induced immune adaptation of the proteasome system is an accelerated and transient response. Proc. Natl. Acad. Sci. USA 102, 9241-9246.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9241-9246
    • Heink, S.1    Ludwig, D.2    Kloetzel, P.M.3    Krüger, E.4
  • 16
    • 0028997958 scopus 로고
    • Preimplantation development of mouse embryos in KSOM: Augmentation by amino acids and analysis of gene expression
    • Ho, Y., Wigglesworth, K., Eppig, J. J. and Schultz, R. M. (1995). Preimplantation development of mouse embryos in KSOM: augmentation by amino acids and analysis of gene expression. Mol. Reprod. Dev. 41, 232-238.
    • (1995) Mol. Reprod. Dev. , vol.41 , pp. 232-238
    • Ho, Y.1    Wigglesworth, K.2    Eppig, J.J.3    Schultz, R.M.4
  • 17
    • 33646686594 scopus 로고    scopus 로고
    • Possible tetramerisation of the proteasome maturation factor POMP/proteassemblin/hUmp1 and its subcellular localisation
    • Hoefer, M. M., Boneberg, E. M., Grotegut, S., Kusch, J. and Illges, H. (2006). Possible tetramerisation of the proteasome maturation factor POMP/proteassemblin/hUmp1 and its subcellular localisation. Int. J. Biol. Macromol. 38, 259-267.
    • (2006) Int. J. Biol. Macromol. , vol.38 , pp. 259-267
    • Hoefer, M.M.1    Boneberg, E.M.2    Grotegut, S.3    Kusch, J.4    Illges, H.5
  • 18
    • 4344714017 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway modulates mouse oocyte meiotic maturation and fertilization via regulation of MAPK cascade and cyclin B1 degradation
    • Huo, L. J., Fan, H. Y., Zhong, Z. S., Chen, D. Y., Schatten, H. and Sun, Q. Y. (2004). Ubiquitin-proteasome pathway modulates mouse oocyte meiotic maturation and fertilization via regulation of MAPK cascade and cyclin B1 degradation. Mech. Dev. 121, 1275-1287.
    • (2004) Mech. Dev. , vol.121 , pp. 1275-1287
    • Huo, L.J.1    Fan, H.Y.2    Zhong, Z.S.3    Chen, D.Y.4    Schatten, H.5    Sun, Q.Y.6
  • 21
    • 54049107641 scopus 로고    scopus 로고
    • Some assembly required: Dedicated chaperones in eukaryotic proteasome biogenesis
    • Kusmierczyk, A. R. and Hochstrasser, M. (2008). Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis. Biol. Chem. 389, 1143-1151.
    • (2008) Biol. Chem. , vol.389 , pp. 1143-1151
    • Kusmierczyk, A.R.1    Hochstrasser, M.2
  • 23
    • 34247617365 scopus 로고    scopus 로고
    • β-Subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint
    • Li, X., Kusmierczyk, A. R., Wong, P., Emili, A. and Hochstrasser, M. (2007). β-Subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint. EMBO J. 26, 2339-2349.
    • (2007) EMBO J. , vol.26 , pp. 2339-2349
    • Li, X.1    Kusmierczyk, A.R.2    Wong, P.3    Emili, A.4    Hochstrasser, M.5
  • 24
    • 77950347539 scopus 로고    scopus 로고
    • Maternal control of early mouse development
    • Li, L., Zheng, P. and Dean, J. (2010). Maternal control of early mouse development. Development 137, 859-870.
    • (2010) Development , vol.137 , pp. 859-870
    • Li, L.1    Zheng, P.2    Dean, J.3
  • 25
    • 0032827329 scopus 로고    scopus 로고
    • Neuronal apoptosis inhibitory protein (NAIP) may enhance the survival of granulosa cells thus indirectly affecting oocyte survival
    • Matsumoto, K., Nakayama, T., Sakai, H., Tanemura, K., Osuga, H., Sato, E. and Ikeda, J. E. (1999). Neuronal apoptosis inhibitory protein (NAIP) may enhance the survival of granulosa cells thus indirectly affecting oocyte survival. Mol. Reprod. Dev. 54, 103-111.
    • (1999) Mol. Reprod. Dev. , vol.54 , pp. 103-111
    • Matsumoto, K.1    Nakayama, T.2    Sakai, H.3    Tanemura, K.4    Osuga, H.5    Sato, E.6    Ikeda, J.E.7
  • 26
    • 46349103626 scopus 로고    scopus 로고
    • Identification of ZAG1, a novel protein expressed in mouse preimplantation, and its putative roles in zygotic genome activation
    • Matsuoka, T., Sato, M., Tokoro, M., Shin, S. W., Uenoyama, A., Ito, K., Hitomi, S., Amano, T., Anzai, M., Kato, H. et al. (2008). Identification of ZAG1, a novel protein expressed in mouse preimplantation, and its putative roles in zygotic genome activation. J. Reprod. Dev. 54, 192-197.
    • (2008) J. Reprod. Dev. , vol.54 , pp. 192-197
    • Matsuoka, T.1    Sato, M.2    Tokoro, M.3    Shin, S.W.4    Uenoyama, A.5    Ito, K.6    Hitomi, S.7    Amano, T.8    Anzai, M.9    Kato, H.10
  • 28
    • 0037821846 scopus 로고    scopus 로고
    • Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of Mammalian proteasomes
    • Meiners, S., Heyken, D., Weller, A., Ludwig, A., Stangl, K., Kloetzel, P. M. and Krüger, E. (2003). Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of Mammalian proteasomes. J. Biol. Chem. 278, 21517-21525.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21517-21525
    • Meiners, S.1    Heyken, D.2    Weller, A.3    Ludwig, A.4    Stangl, K.5    Kloetzel, P.M.6    Krüger, E.7
  • 29
    • 0037007233 scopus 로고    scopus 로고
    • Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction
    • Mendez, R., Barnard, D. and Richter, J. D. (2002). Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction. EMBO J. 21, 1833-1844.
    • (2002) EMBO J. , vol.21 , pp. 1833-1844
    • Mendez, R.1    Barnard, D.2    Richter, J.D.3
  • 33
    • 35348886029 scopus 로고    scopus 로고
    • Concise review: Role and function of the ubiquitinproteasome system in mammalian stem and progenitor cells
    • Naujokat, C. and Sarić, T. (2007). Concise review: role and function of the ubiquitinproteasome system in mammalian stem and progenitor cells. Stem Cells 25, 2408-2418.
    • (2007) Stem Cells , vol.25 , pp. 2408-2418
    • Naujokat, C.1    Sarić, T.2
  • 36
    • 0043198364 scopus 로고    scopus 로고
    • Coordinate activation of maternal protein degradation during the egg-to-embryo transition in C. Elegans
    • Pellettieri, J., Reinke, V., Kim, S. K. and Seydoux, G. (2003). Coordinate activation of maternal protein degradation during the egg-to-embryo transition in C. elegans. Dev. Cell 5, 451-462.
    • (2003) Dev. Cell , vol.5 , pp. 451-462
    • Pellettieri, J.1    Reinke, V.2    Kim, S.K.3    Seydoux, G.4
  • 37
    • 0023184527 scopus 로고
    • Differential effects of activators of cAMP-dependent protein kinase and protein kinase C on cleavage of one-cell mouse embryos and protein synthesis and phosphorylation in one- and two-cell embryos
    • Poueymirou, W. T. and Schultz, R. M. (1987). Differential effects of activators of cAMP-dependent protein kinase and protein kinase C on cleavage of one-cell mouse embryos and protein synthesis and phosphorylation in one- and two-cell embryos. Dev. Biol. 121, 489-498.
    • (1987) Dev. Biol. , vol.121 , pp. 489-498
    • Poueymirou, W.T.1    Schultz, R.M.2
  • 38
    • 50849123778 scopus 로고    scopus 로고
    • PACemakers of proteasome core particle assembly
    • Ramos, P. C. and Dohmen, R. J. (2008). PACemakers of proteasome core particle assembly. Structure 16, 1296-1304.
    • (2008) Structure , vol.16 , pp. 1296-1304
    • Ramos, P.C.1    Dohmen, R.J.2
  • 39
    • 0032548998 scopus 로고    scopus 로고
    • Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly
    • Ramos, P. C., Höckendorff, J., Johnson, E. S., Varshavsky, A. and Dohmen, R. J. (1998). Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell 92, 489-499.
    • (1998) Cell , vol.92 , pp. 489-499
    • Ramos, P.C.1    Höckendorff, J.2    Johnson, E.S.3    Varshavsky, A.4    Dohmen, R.J.5
  • 40
  • 41
    • 34247468830 scopus 로고    scopus 로고
    • The maternal-zygotic transition: Death and birth of RNAs
    • Schier, A. F. (2007). The maternal-zygotic transition: death and birth of RNAs. Science 316, 406-407.
    • (2007) Science , vol.316 , pp. 406-407
    • Schier, A.F.1
  • 42
    • 26844433577 scopus 로고    scopus 로고
    • Proteasome-associated proteins: Regulation of a proteolytic machine
    • Schmidt, M., Hanna, J., Elsasser, S. and Finley, D. (2005). Proteasome-associated proteins: regulation of a proteolytic machine. Biol. Chem. 386, 725-737.
    • (2005) Biol. Chem. , vol.386 , pp. 725-737
    • Schmidt, M.1    Hanna, J.2    Elsasser, S.3    Finley, D.4
  • 43
    • 0036629076 scopus 로고    scopus 로고
    • The molecular foundations of the maternal to zygotic transition in the preimplantation embryo
    • Schultz, R. M. (2002). The molecular foundations of the maternal to zygotic transition in the preimplantation embryo. Hum. Reprod. Update 8, 323-331.
    • (2002) Hum. Reprod. Update , vol.8 , pp. 323-331
    • Schultz, R.M.1
  • 46
    • 34247523194 scopus 로고    scopus 로고
    • Regulation of the oocyte-to-zygote transition
    • Stitzel, M. L. and Seydoux, G. (2007). Regulation of the oocyte-to-zygote transition. Science 316, 407-408.
    • (2007) Science , vol.316 , pp. 407-408
    • Stitzel, M.L.1    Seydoux, G.2
  • 47
    • 54249158324 scopus 로고    scopus 로고
    • Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
    • Tai, H. C. and Schuman, E. M. (2008). Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nat. Rev. Neurosci. 9, 826-838.
    • (2008) Nat. Rev. Neurosci. , vol.9 , pp. 826-838
    • Tai, H.C.1    Schuman, E.M.2
  • 48
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid proteasomes. Induction by interferon-γ and contribution to ATPdependent proteolysis
    • Tanahashi, N., Murakami, Y., Minami, Y., Shimbara, N., Hendil, K. B. and Tanaka, K. (2000). Hybrid proteasomes. Induction by interferon-γ and contribution to ATPdependent proteolysis. J. Biol. Chem. 275, 14336-14345.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14336-14345
    • Tanahashi, N.1    Murakami, Y.2    Minami, Y.3    Shimbara, N.4    Hendil, K.B.5    Tanaka, K.6
  • 49
    • 78951479670 scopus 로고    scopus 로고
    • Deposition of acetylated histones by RNAP II promoter clearance may occur at onset of zygotic gene activation in preimplantation mouse embryos
    • Tokoro, M., Shin, S. W., Nishikawa, S., Lee, H. H., Hatanaka, Y., Amano, T., Mitani, T., Kato, H., Anzai, M., Kishigami, S. et al. (2010). Deposition of acetylated histones by RNAP II promoter clearance may occur at onset of zygotic gene activation in preimplantation mouse embryos. J. Reprod. Dev. 56, 607-615.
    • (2010) J. Reprod. Dev. , vol.56 , pp. 607-615
    • Tokoro, M.1    Shin, S.W.2    Nishikawa, S.3    Lee, H.H.4    Hatanaka, Y.5    Amano, T.6    Mitani, T.7    Kato, H.8    Anzai, M.9    Kishigami, S.10
  • 50
    • 46849115787 scopus 로고    scopus 로고
    • Autophagy is essential for preimplantation development of mouse embryos
    • Tsukamoto, S., Kuma, A., Murakami, M., Kishi, C., Yamamoto, A. and Mizushima, N. (2008). Autophagy is essential for preimplantation development of mouse embryos. Science 321, 117-120.
    • (2008) Science , vol.321 , pp. 117-120
    • Tsukamoto, S.1    Kuma, A.2    Murakami, M.3    Kishi, C.4    Yamamoto, A.5    Mizushima, N.6
  • 51
    • 44849099551 scopus 로고    scopus 로고
    • Cis-acting elements (E-box and NBE) in the promoter region of three maternal genes (Histone H1oo, Nucleoplasmin 2, and Zygote Arrest 1) are required for oocyte-specific gene expression in the mouse
    • Tsunemoto, K., Anzai, M., Matsuoka, T., Tokoro, M., Shin, S. W., Amano, T., Mitani, T., Kato, H., Hosoi, Y., Saeki, K. et al. (2008). Cis-acting elements (E-box and NBE) in the promoter region of three maternal genes (Histone H1oo, Nucleoplasmin 2, and Zygote Arrest 1) are required for oocyte-specific gene expression in the mouse. Mol. Reprod. Dev. 75, 1104-1108.
    • (2008) Mol. Reprod. Dev. , vol.75 , pp. 1104-1108
    • Tsunemoto, K.1    Anzai, M.2    Matsuoka, T.3    Tokoro, M.4    Shin, S.W.5    Amano, T.6    Mitani, T.7    Kato, H.8    Hosoi, Y.9    Saeki, K.10
  • 52
    • 20444404618 scopus 로고    scopus 로고
    • Regulated protein degradation
    • Varshavsky, A. (2005). Regulated protein degradation. Trends Biochem. Sci. 30, 283-286.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 283-286
    • Varshavsky, A.1
  • 53
    • 0037155196 scopus 로고    scopus 로고
    • Analysis of Drosophila 26 S proteasome using RNA interference
    • Wójcik, C. and DeMartino, G. N. (2002). Analysis of Drosophila 26 S proteasome using RNA interference. J. Biol. Chem. 277, 6188-6197.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6188-6197
    • Wójcik, C.1    DeMartino, G.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.