메뉴 건너뛰기




Volumn 365, Issue 2, 2012, Pages 445-457

Sm protein down-regulation leads to defects in nuclear pore complex disassembly and distribution in C. elegans embryos

Author keywords

Early embryonic divisions; Nuclear envelope breakdown; Nuclear pore complex; Sm proteins

Indexed keywords

PROTEIN SM;

EID: 84860007138     PISSN: 00121606     EISSN: 1095564X     Source Type: Journal    
DOI: 10.1016/j.ydbio.2012.02.036     Document Type: Article
Times cited : (13)

References (53)
  • 1
    • 47149089277 scopus 로고    scopus 로고
    • The life cycle of the metazoan nuclear envelope
    • Anderson D.J., Hetzer M.W. The life cycle of the metazoan nuclear envelope. Curr. Opin. Cell Biol. 2008, 20:386-392.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 386-392
    • Anderson, D.J.1    Hetzer, M.W.2
  • 2
    • 44449138334 scopus 로고    scopus 로고
    • Nuclear pore complex assembly through the cell cycle: regulation and membrane organization
    • Antonin W., Ellenberg J., Dultz E. Nuclear pore complex assembly through the cell cycle: regulation and membrane organization. FEBS Lett. 2008, 582:2004-2016.
    • (2008) FEBS Lett. , vol.582 , pp. 2004-2016
    • Antonin, W.1    Ellenberg, J.2    Dultz, E.3
  • 3
    • 33644745010 scopus 로고    scopus 로고
    • The Sm proteins regulate germ cell specification during early C. elegans embryogenesis
    • Barbee S.A., Evans T.C. The Sm proteins regulate germ cell specification during early C. elegans embryogenesis. Dev. Biol. 2006, 291:132-143.
    • (2006) Dev. Biol. , vol.291 , pp. 132-143
    • Barbee, S.A.1    Evans, T.C.2
  • 4
    • 0037015264 scopus 로고    scopus 로고
    • A novel function for the Sm proteins in germ granule localization during C. elegans embryogenesis
    • Barbee S.A., Lublin A.L., Evans T.C. A novel function for the Sm proteins in germ granule localization during C. elegans embryogenesis. Curr. Biol. 2002, 12:1502-1506.
    • (2002) Curr. Biol. , vol.12 , pp. 1502-1506
    • Barbee, S.A.1    Lublin, A.L.2    Evans, T.C.3
  • 7
    • 0037371466 scopus 로고    scopus 로고
    • Dynamics of the endoplasmic reticulum during early development of Drosophila melanogaster
    • Bobinnec Y., Marcaillou C., Morin X., Debec A. Dynamics of the endoplasmic reticulum during early development of Drosophila melanogaster. Cell Motil. Cytoskeleton 2003, 54:217-225.
    • (2003) Cell Motil. Cytoskeleton , vol.54 , pp. 217-225
    • Bobinnec, Y.1    Marcaillou, C.2    Morin, X.3    Debec, A.4
  • 11
    • 0141764733 scopus 로고    scopus 로고
    • Nuclear pore protein gp210 is essential for viability in HeLa cells and Caenorhabditis elegans
    • Cohen M., Feinstein N., Wilson K.L., Gruenbaum Y. Nuclear pore protein gp210 is essential for viability in HeLa cells and Caenorhabditis elegans. Mol. Biol. Cell 2003, 14:4230-4237.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4230-4237
    • Cohen, M.1    Feinstein, N.2    Wilson, K.L.3    Gruenbaum, Y.4
  • 12
    • 46249132388 scopus 로고    scopus 로고
    • Electron microscopy of lamin and the nuclear lamina in Caenorhabditis elegans
    • Cohen M., Santarella R., Wiesel N., Mattaj I., Gruenbaum Y. Electron microscopy of lamin and the nuclear lamina in Caenorhabditis elegans. Methods Cell Biol. 2008, 88:411-429.
    • (2008) Methods Cell Biol. , vol.88 , pp. 411-429
    • Cohen, M.1    Santarella, R.2    Wiesel, N.3    Mattaj, I.4    Gruenbaum, Y.5
  • 14
    • 52949107958 scopus 로고    scopus 로고
    • Structure, dynamics and function of nuclear pore complexes
    • D'Angelo M.A., Hetzer M.W. Structure, dynamics and function of nuclear pore complexes. Trends Cell Biol. 2008, 18:456-466.
    • (2008) Trends Cell Biol. , vol.18 , pp. 456-466
    • D'Angelo, M.A.1    Hetzer, M.W.2
  • 15
    • 64749091534 scopus 로고    scopus 로고
    • ER membrane-bending proteins are necessary for de novo nuclear pore formation
    • Dawson T.R., Lazarus M.D., Hetzer M.W., Wente S.R. ER membrane-bending proteins are necessary for de novo nuclear pore formation. J. Cell Biol. 2009, 184:659-675.
    • (2009) J. Cell Biol. , vol.184 , pp. 659-675
    • Dawson, T.R.1    Lazarus, M.D.2    Hetzer, M.W.3    Wente, S.R.4
  • 16
    • 77957660297 scopus 로고    scopus 로고
    • Nuclear pore biogenesis into an intact nuclear envelope
    • Doucet C.M., Hetzer M.W. Nuclear pore biogenesis into an intact nuclear envelope. Chromosoma 2010, 119:469-477.
    • (2010) Chromosoma , vol.119 , pp. 469-477
    • Doucet, C.M.1    Hetzer, M.W.2
  • 17
    • 77953724768 scopus 로고    scopus 로고
    • Cell cycle-dependent differences in nuclear pore complex assembly in metazoa
    • Doucet C.M., Talamas J.A., Hetzer M.W. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell 2010, 141:1030-1041.
    • (2010) Cell , vol.141 , pp. 1030-1041
    • Doucet, C.M.1    Talamas, J.A.2    Hetzer, M.W.3
  • 18
    • 0031005268 scopus 로고    scopus 로고
    • From nucleoporins to nuclear pore complexes
    • Doye V., Hurt E. From nucleoporins to nuclear pore complexes. Curr. Opin. Cell Biol. 1997, 9:401-411.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 401-411
    • Doye, V.1    Hurt, E.2
  • 19
    • 77957743829 scopus 로고    scopus 로고
    • Live imaging of single nuclear pores reveals unique assembly kinetics and mechanism in interphase
    • Dultz E., Ellenberg J. Live imaging of single nuclear pores reveals unique assembly kinetics and mechanism in interphase. J. Cell Biol. 2010, 191:15-22.
    • (2010) J. Cell Biol. , vol.191 , pp. 15-22
    • Dultz, E.1    Ellenberg, J.2
  • 20
    • 40849097593 scopus 로고    scopus 로고
    • Systematic kinetic analysis of mitotic dis- and reassembly of the nuclear pore in living cells
    • Dultz E., Zanin E., Wurzenberger C., Braun M., Rabut G., Sironi L., Ellenberg J. Systematic kinetic analysis of mitotic dis- and reassembly of the nuclear pore in living cells. J. Cell Biol. 2008, 180:857-865.
    • (2008) J. Cell Biol. , vol.180 , pp. 857-865
    • Dultz, E.1    Zanin, E.2    Wurzenberger, C.3    Braun, M.4    Rabut, G.5    Sironi, L.6    Ellenberg, J.7
  • 21
    • 33749049426 scopus 로고    scopus 로고
    • The nuclear pore complex, nuclear transport, and apoptosis
    • Fahrenkrog B. The nuclear pore complex, nuclear transport, and apoptosis. Can. J. Physiol. Pharmacol. 2006, 84:279-286.
    • (2006) Can. J. Physiol. Pharmacol. , vol.84 , pp. 279-286
    • Fahrenkrog, B.1
  • 22
    • 34948818777 scopus 로고    scopus 로고
    • Two distinct human POM121 genes: requirement for the formation of nuclear pore complexes
    • Funakoshi T., Maeshima K., Yahata K., Sugano S., Imamoto F., Imamoto N. Two distinct human POM121 genes: requirement for the formation of nuclear pore complexes. FEBS Lett. 2007, 581:4910-4916.
    • (2007) FEBS Lett. , vol.581 , pp. 4910-4916
    • Funakoshi, T.1    Maeshima, K.2    Yahata, K.3    Sugano, S.4    Imamoto, F.5    Imamoto, N.6
  • 23
    • 79953296849 scopus 로고    scopus 로고
    • Localization of Pom121 to the inner nuclear membrane is required for an early step of interphase nuclear pore complex assembly
    • Funakoshi T., Clever M., Watanabe A., Imamoto N. Localization of Pom121 to the inner nuclear membrane is required for an early step of interphase nuclear pore complex assembly. Mol. Biol. Cell 2011, 22:1058-1069.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1058-1069
    • Funakoshi, T.1    Clever, M.2    Watanabe, A.3    Imamoto, N.4
  • 24
    • 0344875469 scopus 로고    scopus 로고
    • Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the limit of nuclear pore complex size exclusion in vivo
    • Galy V., Mattaj I.W., Askjaer P. Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the limit of nuclear pore complex size exclusion in vivo. Mol. Biol. Cell 2003, 14:5104-5115.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 5104-5115
    • Galy, V.1    Mattaj, I.W.2    Askjaer, P.3
  • 26
    • 68949194442 scopus 로고    scopus 로고
    • Inactivation of the C. elegans lipin homolog leads to ER disorganization and to defects in the breakdown and reassembly of the nuclear envelope
    • Golden A., Liu J., Cohen-Fix O. Inactivation of the C. elegans lipin homolog leads to ER disorganization and to defects in the breakdown and reassembly of the nuclear envelope. J. Cell Sci. 2009, 122:1970-1978.
    • (2009) J. Cell Sci. , vol.122 , pp. 1970-1978
    • Golden, A.1    Liu, J.2    Cohen-Fix, O.3
  • 29
    • 78549233307 scopus 로고    scopus 로고
    • The function of spliceosome components in open mitosis
    • Hofmann J.C., Husedzinovic A., Gruss O.J. The function of spliceosome components in open mitosis. Nucleus 2010, 1:447-459.
    • (2010) Nucleus , vol.1 , pp. 447-459
    • Hofmann, J.C.1    Husedzinovic, A.2    Gruss, O.J.3
  • 33
    • 0034492454 scopus 로고    scopus 로고
    • C. elegans nuclear envelope proteins emerin, MAN1, lamin, and nucleoporins reveal unique timing of nuclear envelope breakdown during mitosis
    • Lee K.K., Gruenbaum Y., Spann P., Liu J., Wilson K.L. C. elegans nuclear envelope proteins emerin, MAN1, lamin, and nucleoporins reveal unique timing of nuclear envelope breakdown during mitosis. Mol. Biol. Cell 2000, 11:3089-3099.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3089-3099
    • Lee, K.K.1    Gruenbaum, Y.2    Spann, P.3    Liu, J.4    Wilson, K.L.5
  • 34
    • 0344835675 scopus 로고    scopus 로고
    • Nuclear envelope breakdown in starfish oocytes proceeds by partial NPC disassembly followed by a rapidly spreading fenestration of nuclear membranes
    • Lenart P., Rabut G., Daigle N., Hand A.R., Terasaki M., Ellenberg J. Nuclear envelope breakdown in starfish oocytes proceeds by partial NPC disassembly followed by a rapidly spreading fenestration of nuclear membranes. J. Cell Biol. 2003, 160:1055-1068.
    • (2003) J. Cell Biol. , vol.160 , pp. 1055-1068
    • Lenart, P.1    Rabut, G.2    Daigle, N.3    Hand, A.R.4    Terasaki, M.5    Ellenberg, J.6
  • 35
    • 17044457744 scopus 로고    scopus 로고
    • The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis
    • Loiodice I., Alves A., Rabut G., Van Overbeek M., Ellenberg J., Sibarita J.B., Doye V. The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis. Mol. Biol. Cell 2004, 15:3333-3344.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3333-3344
    • Loiodice, I.1    Alves, A.2    Rabut, G.3    Van Overbeek, M.4    Ellenberg, J.5    Sibarita, J.B.6    Doye, V.7
  • 36
    • 80052596764 scopus 로고    scopus 로고
    • Formation of the postmitotic nuclear envelope from extended ER cisternae precedes nuclear pore assembly
    • Lu L., Ladinsky M.S., Kirchhausen T. Formation of the postmitotic nuclear envelope from extended ER cisternae precedes nuclear pore assembly. J. Cell Biol. 2011, 194:425-440.
    • (2011) J. Cell Biol. , vol.194 , pp. 425-440
    • Lu, L.1    Ladinsky, M.S.2    Kirchhausen, T.3
  • 37
    • 33845713718 scopus 로고    scopus 로고
    • Katanin controls mitotic and meiotic spindle length
    • McNally K., Audhya A., Oegema K., McNally F.J. Katanin controls mitotic and meiotic spindle length. J. Cell Biol. 2006, 175:881-891.
    • (2006) J. Cell Biol. , vol.175 , pp. 881-891
    • McNally, K.1    Audhya, A.2    Oegema, K.3    McNally, F.J.4
  • 39
    • 0030587611 scopus 로고    scopus 로고
    • Onset of C. elegans gastrulation is blocked by inhibition of embryonic transcription with an RNA polymerase antisense RNA
    • Powell-Coffman J.A., Knight J., Wood W.B. Onset of C. elegans gastrulation is blocked by inhibition of embryonic transcription with an RNA polymerase antisense RNA. Dev. Biol. 1996, 178:472-483.
    • (1996) Dev. Biol. , vol.178 , pp. 472-483
    • Powell-Coffman, J.A.1    Knight, J.2    Wood, W.B.3
  • 40
    • 0035099902 scopus 로고    scopus 로고
    • Creation of low-copy integrated transgenic lines in Caenorhabditis elegans
    • Praitis V., Casey E., Collar D., Austin J. Creation of low-copy integrated transgenic lines in Caenorhabditis elegans. Genetics 2001, 157:1217-1226.
    • (2001) Genetics , vol.157 , pp. 1217-1226
    • Praitis, V.1    Casey, E.2    Collar, D.3    Austin, J.4
  • 41
    • 2342513330 scopus 로고    scopus 로고
    • Dynamics of nuclear pore complex organization through the cell cycle
    • Rabut G., Lenart P., Ellenberg J. Dynamics of nuclear pore complex organization through the cell cycle. Curr. Opin. Cell Biol. 2004, 16:314-321.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 314-321
    • Rabut, G.1    Lenart, P.2    Ellenberg, J.3
  • 42
    • 0030071186 scopus 로고    scopus 로고
    • Nuclear pore clustering is a consistent feature of apoptosis in vitro
    • Reipert S., Reipert B.M., Hickman J.A., Allen T.D. Nuclear pore clustering is a consistent feature of apoptosis in vitro. Cell Death Differ. 1996, 3:131-139.
    • (1996) Cell Death Differ. , vol.3 , pp. 131-139
    • Reipert, S.1    Reipert, B.M.2    Hickman, J.A.3    Allen, T.D.4
  • 43
    • 0036000025 scopus 로고    scopus 로고
    • Targeting of rough endoplasmic reticulum membrane proteins and ribosomes in invertebrate neurons
    • Rolls M.M., Hall D.H., Victor M., Stelzer E.H., Rapoport T.A. Targeting of rough endoplasmic reticulum membrane proteins and ribosomes in invertebrate neurons. Mol. Biol. Cell 2002, 13:1778-1791.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1778-1791
    • Rolls, M.M.1    Hall, D.H.2    Victor, M.3    Stelzer, E.H.4    Rapoport, T.A.5
  • 44
    • 0033539171 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle
    • Seto A.G., Zaug A.J., Sobel S.G., Wolin S.L., Cech T.R. Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle. Nature 1999, 401:177-180.
    • (1999) Nature , vol.401 , pp. 177-180
    • Seto, A.G.1    Zaug, A.J.2    Sobel, S.G.3    Wolin, S.L.4    Cech, T.R.5
  • 45
    • 0030790516 scopus 로고    scopus 로고
    • Transcriptionally repressed germ cells lack a subpopulation of phosphorylated RNA polymerase II in early embryos of Caenorhabditis elegans and Drosophila melanogaster
    • Seydoux G., Dunn M.A. Transcriptionally repressed germ cells lack a subpopulation of phosphorylated RNA polymerase II in early embryos of Caenorhabditis elegans and Drosophila melanogaster. Development. 1997, 124:2191-2201.
    • (1997) Development. , vol.124 , pp. 2191-2201
    • Seydoux, G.1    Dunn, M.A.2
  • 46
    • 0036848091 scopus 로고    scopus 로고
    • The SR protein SRp38 represses splicing in M phase cells
    • Shin C., Manley J.L. The SR protein SRp38 represses splicing in M phase cells. Cell 2002, 111:407-417.
    • (2002) Cell , vol.111 , pp. 407-417
    • Shin, C.1    Manley, J.L.2
  • 47
    • 79960233453 scopus 로고    scopus 로고
    • POM121 and Sun1 play a role in early steps of interphase NPC assembly
    • Talamas J.A., Hetzer M.W. POM121 and Sun1 play a role in early steps of interphase NPC assembly. J. Cell Biol. 2011, 194:27-37.
    • (2011) J. Cell Biol. , vol.194 , pp. 27-37
    • Talamas, J.A.1    Hetzer, M.W.2
  • 48
    • 77951250065 scopus 로고    scopus 로고
    • The C. elegans homolog of nucleoporin Nup98 is required for the integrity and function of germline P granules
    • Voronina E., Seydoux G. The C. elegans homolog of nucleoporin Nup98 is required for the integrity and function of germline P granules. Development 2010, 137:1441-1450.
    • (2010) Development , vol.137 , pp. 1441-1450
    • Voronina, E.1    Seydoux, G.2
  • 49
    • 33947236787 scopus 로고    scopus 로고
    • Transcription reactivation steps stimulated by oocyte maturation in C. elegans
    • Walker A.K., Boag P.R., Blackwell T.K. Transcription reactivation steps stimulated by oocyte maturation in C. elegans. Dev. Biol. 2007, 304:382-393.
    • (2007) Dev. Biol. , vol.304 , pp. 382-393
    • Walker, A.K.1    Boag, P.R.2    Blackwell, T.K.3
  • 50
    • 0035370526 scopus 로고    scopus 로고
    • Spliceosomal UsnRNP biogenesis, structure and function
    • Will C.L., Luhrmann R. Spliceosomal UsnRNP biogenesis, structure and function. Curr. Opin. Cell Biol. 2001, 13:290-301.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 290-301
    • Will, C.L.1    Luhrmann, R.2
  • 51
    • 0030776030 scopus 로고    scopus 로고
    • Nuclear pore complex number and distribution throughout the Saccharomyces cerevisiae cell cycle by three-dimensional reconstruction from electron micrographs of nuclear envelopes
    • Winey M., Yarar D., Giddings T.H., Mastronarde D.N. Nuclear pore complex number and distribution throughout the Saccharomyces cerevisiae cell cycle by three-dimensional reconstruction from electron micrographs of nuclear envelopes. Mol. Biol. Cell 1997, 8:2119-2132.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2119-2132
    • Winey, M.1    Yarar, D.2    Giddings, T.H.3    Mastronarde, D.N.4
  • 52
    • 0030955703 scopus 로고    scopus 로고
    • Integral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosis
    • Yang L., Guan T., Gerace L. Integral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosis. J. Cell Biol. 1997, 137:1199-1210.
    • (1997) J. Cell Biol. , vol.137 , pp. 1199-1210
    • Yang, L.1    Guan, T.2    Gerace, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.