메뉴 건너뛰기




Volumn 198, Issue 6, 2012, Pages 981-990

Mitotic lamin disassembly is triggered by lipid-mediated signaling

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE 1; DIACYLGLYCEROL; LAMIN; LAMIN B1; LIPID; PROTEIN KINASE C; UNCLASSIFIED DRUG;

EID: 84869139686     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201205103     Document Type: Article
Times cited : (59)

References (58)
  • 1
    • 0037059611 scopus 로고    scopus 로고
    • Nuclear envelope breakdown proceeds by microtubule-induced tearing of the lamina
    • Beaudouin, J., D. Gerlich, N. Daigle, R. Eils, and J. Ellenberg. 2002. Nuclear envelope breakdown proceeds by microtubule-induced tearing of the lamina. Cell. 108:83-96. http://dx.doi.org/10.1016/S0092-8674(01)00627-4
    • (2002) Cell , vol.108 , pp. 83-96
    • Beaudouin, J.1    Gerlich, D.2    Daigle, N.3    Eils, R.4    Ellenberg, J.5
  • 3
    • 0023664184 scopus 로고
    • Cell cycle-dependent methyl esterification of lamin B
    • Chelsky, D., J.F. Olson, and D.E. Koshland Jr. 1987. Cell cycle-dependent methyl esterification of lamin B. J. Biol. Chem. 262:4303-4309.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4303-4309
    • Chelsky, D.1    Olson, J.F.2    Koshland Jr., D.E.3
  • 4
    • 78651385378 scopus 로고    scopus 로고
    • Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae: identification of SER(602), THR(723), and SER(744) as the sites phosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase
    • Choi, H.-S., W.-M. Su, J.M. Morgan, G.-S. Han, Z. Xu, E. Karanasios, S. Siniossoglou, and G.M. Carman. 2011. Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae: identification of SER(602), THR(723), and SER(744) as the sites phosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase. J. Biol. Chem. 286:1486-1498. http://dx.doi.org/10.1074/jbc.M110.155598
    • (2011) J. Biol. Chem. , vol.286 , pp. 1486-1498
    • Choi, H.-S.1    Su, W.-M.2    Morgan, J.M.3    Han, G.-S.4    Xu, Z.5    Karanasios, E.6    Siniossoglou, S.7    Carman, G.M.8
  • 5
    • 0032925541 scopus 로고    scopus 로고
    • Sequential PKC- and Cdc2-mediated phosphorylation events elicit zebrafish nuclear envelope disassembly
    • Collas, P. 1999. Sequential PKC- and Cdc2-mediated phosphorylation events elicit zebrafish nuclear envelope disassembly. J. Cell Sci. 112:977-987.
    • (1999) J. Cell Sci. , vol.112 , pp. 977-987
    • Collas, P.1
  • 6
    • 0030771437 scopus 로고    scopus 로고
    • Protein kinase C-mediated interphase lamin B phosphorylation and solubilization
    • Collas, P., L. Thompson, A.P. Fields, D.L. Poccia, and J.C. Courvalin. 1997. Protein kinase C-mediated interphase lamin B phosphorylation and solubilization. J. Biol. Chem. 272:21274-21280. http://dx.doi.org/10.1074/jbc.272.34.21274
    • (1997) J. Biol. Chem , vol.272 , pp. 21274-21280
    • Collas, P.1    Thompson, L.2    Fields, A.P.3    Poccia, D.L.4    Courvalin, J.C.5
  • 7
    • 36048958871 scopus 로고    scopus 로고
    • Visual snapshots of intracellular kinase activity at the onset of mitosis
    • Dai, Z., N.G. Dulyaninova, S. Kumar, A.R. Bresnick, and D.S. Lawrence. 2007. Visual snapshots of intracellular kinase activity at the onset of mitosis. Chem. Biol. 14:1254-1260. http://dx.doi.org/10.1016/j.chembiol.2007 .10.007
    • (2007) Chem. Biol , vol.14 , pp. 1254-1260
    • Dai, Z.1    Dulyaninova, N.G.2    Kumar, S.3    Bresnick, A.R.4    Lawrence, D.S.5
  • 8
    • 0035833254 scopus 로고    scopus 로고
    • Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells
    • Daigle, N., J. Beaudouin, L. Hartnell, G. Imreh, E. Hallberg, J. Lippincott-Schwartz, and J. Ellenberg. 2001. Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells. J. Cell Biol. 154:71-84. http://dx.doi.org/10.1083/jcb.200101089
    • (2001) J. Cell Biol , vol.154 , pp. 71-84
    • Daigle, N.1    Beaudouin, J.2    Hartnell, L.3    Imreh, G.4    Hallberg, E.5    Lippincott-Schwartz, J.6    Ellenberg, J.7
  • 9
    • 0036500525 scopus 로고    scopus 로고
    • Generation of diacylglycerol molecular species through the cell cycle: a role for 1-stearoyl 2-arachidonyl glycerol in the activation of nuclear protein kinase C-betaII at G2/M
    • Deacon, E.M., T.R. Pettitt, P. Webb, T. Cross, H. Chahal, M.J.O. Wakelam, and J.M. Lord. 2002. Generation of diacylglycerol molecular species through the cell cycle: a role for 1-stearoyl, 2-arachidonyl glycerol in the activation of nuclear protein kinase C-betaII at G2/M. J. Cell Sci. 115:983-989.
    • (2002) J. Cell Sci. , vol.115 , pp. 983-989
    • Deacon, E.M.1    Pettitt, T.R.2    Webb, P.3    Cross, T.4    Chahal, H.5    Wakelam, M.J.O.6    Lord, J.M.7
  • 10
    • 9244262503 scopus 로고    scopus 로고
    • Partial nuclear pore complex disassembly during closed mitosis in Aspergillus nidulans
    • De Souza, C.P.C., A.H. Osmani, S.B. Hashmi, and S.A. Osmani. 2004. Partial nuclear pore complex disassembly during closed mitosis in Aspergillus nidulans. Curr. Biol. 14:1973-1984. http://dx.doi.org/10.1016/j.cub.2004.10.050
    • (2004) Curr. Biol , vol.14 , pp. 1973-1984
    • De Souza, C.P.C.1    Osmani, A.H.2    Hashmi, S.B.3    Osmani, S.A.4
  • 11
    • 33947542353 scopus 로고    scopus 로고
    • Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns
    • Donkor, J., M. Sariahmetoglu, J. Dewald, D.N. Brindley, and K. Reue. 2007. Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns. J. Biol. Chem. 282:3450-3457. http://dx.doi.org/10.1074/jbc.M610745200
    • (2007) J. Biol. Chem , vol.282 , pp. 3450-3457
    • Donkor, J.1    Sariahmetoglu, M.2    Dewald, J.3    Brindley, D.N.4    Reue, K.5
  • 14
    • 0030846763 scopus 로고    scopus 로고
    • Nuclear envelope breakdown in mammalian cells involves stepwise lamina disassembly and microtubule-drive deformation of the nuclear membrane
    • Georgatos, S.D., A. Pyrpasopoulou, and P.A. Theodoropoulos. 1997. Nuclear envelope breakdown in mammalian cells involves stepwise lamina disassembly and microtubule-drive deformation of the nuclear membrane. J. Cell Sci. 110:2129-2140.
    • (1997) J. Cell Sci. , vol.110 , pp. 2129-2140
    • Georgatos, S.D.1    Pyrpasopoulou, A.2    Theodoropoulos, P.A.3
  • 15
    • 0018840796 scopus 로고
    • The nuclear envelope lamina is reversibly depolymerized during mitosis
    • Gerace, L., and G. Blobel. 1980. The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell. 19:277-287. http://dx.doi.org/10.1016/0092-8674(80)90409-2
    • (1980) Cell , vol.19 , pp. 277-287
    • Gerace, L.1    Blobel, G.2
  • 16
    • 0018093261 scopus 로고
    • Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction Interphase and mitotic distribution
    • Gerace, L., A. Blum, and G. Blobel. 1978. Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction. Interphase and mitotic distribution. J. Cell Biol. 79:546-566. http://dx.doi.org/10.1083/jcb.79.2.546
    • (1978) J. Cell Biol , vol.79 , pp. 546-566
    • Gerace, L.1    Blum, A.2    Blobel, G.3
  • 17
    • 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., J. Liu, and O. Cohen-Fix. 2009. 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. 122:1970-1978. http://dx.doi.org/10.1242/jcs.044743
    • (2009) J. Cell Sci , vol.122 , pp. 1970-1978
    • Golden, A.1    Liu, J.2    Cohen-Fix, O.3
  • 18
    • 68949170697 scopus 로고    scopus 로고
    • Lipin is required for efficient breakdown of the nuclear envelope in Caenorhabditis elegans
    • Gorjánácz, M., and I.W. Mattaj. 2009. Lipin is required for efficient breakdown of the nuclear envelope in Caenorhabditis elegans. J. Cell Sci. 122:1963-1969. http://dx.doi.org/10.1242/jcs.044750
    • (2009) J. Cell Sci. , vol.122 , pp. 1963-1969
    • Gorjánácz, M.1    Mattaj, I.W.2
  • 20
    • 57649213401 scopus 로고    scopus 로고
    • Temporal and spatial regulation of the phosphatidate phosphatases lipin 1 and 2
    • Grimsey, N., G.-S. Han, L. O'Hara, J.J. Rochford, G.M. Carman, and S. Siniossoglou. 2008. Temporal and spatial regulation of the phosphatidate phosphatases lipin 1 and 2. J. Biol. Chem. 283:29166-29174. http://dx.doi.org/10.1074/jbc.M804278200
    • (2008) J. Biol. Chem , vol.283 , pp. 29166-29174
    • Grimsey, N.1    Han, G.-S.2    O'Hara, L.3    Rochford, J.J.4    Carman, G.M.5    Siniossoglou, S.6
  • 21
    • 60749108426 scopus 로고    scopus 로고
    • Orchestrating nuclear envelope disassembly and reassembly during mitosis
    • Güttinger, S., E. Laurell, and U. Kutay. 2009. Orchestrating nuclear envelope disassembly and reassembly during mitosis. Nat. Rev. Mol. Cell Biol. 10:178-191. http://dx.doi.org/10.1038/nrm2641
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 178-191
    • Güttinger, S.1    Laurell, E.2    Kutay, U.3
  • 22
    • 33646920976 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme
    • Han, G.-S., W.-I. Wu, and G.M. Carman. 2006. The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme. J. Biol. Chem. 281:9210-9218. http://dx.doi.org/10.1074/jbc.M600425200
    • (2006) J. Biol. Chem , vol.281 , pp. 9210-9218
    • Han, G.-S.1    Wu, W.-I.2    Carman, G.M.3
  • 23
    • 84856296166 scopus 로고    scopus 로고
    • Nuclear envelope phosphatase 1-regulatory subunit 1 (formerly TMEM188) is the metazoan Spo7p ortholog and functions in the lipin activation pathway
    • Han, S., S. Bahmanyar, P. Zhang, N. Grishin, K. Oegema, R. Crooke, M. Graham, K. Reue, J.E. Dixon, and J.M. Goodman. 2012. Nuclear envelope phosphatase 1-regulatory subunit 1 (formerly TMEM188) is the metazoan Spo7p ortholog and functions in the lipin activation pathway. J. Biol. Chem. 287:3123-3137. http://dx.doi.org/10.1074/jbc.M111.324350
    • (2012) J. Biol. Chem , vol.287 , pp. 3123-3137
    • Han, S.1    Bahmanyar, S.2    Zhang, P.3    Grishin, N.4    Oegema, K.5    Crooke, R.6    Graham, M.7    Reue, K.8    Dixon, J.E.9    Goodman, J.M.10
  • 24
    • 37549000595 scopus 로고    scopus 로고
    • Colorimetric determination of pure Mg(2+)-dependent phosphatidate phosphatase activity
    • Havriluk, T., F. Lozy, S. Siniossoglou, and G.M. Carman. 2008. Colorimetric determination of pure Mg(2+)-dependent phosphatidate phosphatase activity. Anal. Biochem. 373:392-394. http://dx.doi.org/10.1016/j.ab.2007.08.037
    • (2008) Anal. Biochem , vol.373 , pp. 392-394
    • Havriluk, T.1    Lozy, F.2    Siniossoglou, S.3    Carman, G.M.4
  • 25
    • 0025352896 scopus 로고
    • Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis
    • Heald, R., and F. McKeon. 1990. Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell. 61:579-589. http://dx.doi.org/10.1016/0092-8674(90)90470-Y
    • (1990) Cell , vol.61 , pp. 579-589
    • Heald, R.1    McKeon, F.2
  • 27
    • 28444472419 scopus 로고    scopus 로고
    • Pushing the envelope: structure, function, and dynamics of the nuclear periphery
    • Hetzer, M.W., T.C. Walther, and I.W. Mattaj. 2005. Pushing the envelope: structure, function, and dynamics of the nuclear periphery. Annu. Rev. Cell Dev. Biol. 21:347-380. http://dx.doi.org/10.1146/annurev.cellbio.21.090704.151152
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 347-380
    • Hetzer, M.W.1    Walther, T.C.2    Mattaj, I.W.3
  • 28
    • 0027502241 scopus 로고
    • Identification of protein kinase C (PKC) phosphorylation sites on human lamin B Potential role of PKC in nuclear lamina structural dynamics
    • Hocevar, B.A., D.J. Burns, and A.P. Fields. 1993. Identification of protein kinase C (PKC) phosphorylation sites on human lamin B. Potential role of PKC in nuclear lamina structural dynamics. J. Biol. Chem. 268:7545-7552.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7545-7552
    • Hocevar, B.A.1    Burns, D.J.2    Fields, A.P.3
  • 29
    • 78049319504 scopus 로고    scopus 로고
    • A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase
    • Karanasios, E., G.-S. Han, Z. Xu, G.M. Carman, and S. Siniossoglou. 2010. A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase. Proc. Natl. Acad. Sci. USA. 107:17539-17544. http://dx.doi.org/10.1073/pnas.1007974107
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17539-17544
    • Karanasios, E.1    Han, G.-S.2    Xu, Z.3    Carman, G.M.4    Siniossoglou, S.5
  • 31
    • 79951683953 scopus 로고    scopus 로고
    • Phosphorylation of Nup98 by multiple kinases is crucial for NPC disassembly during mitotic entry
    • Laurell, E., K. Beck, K. Krupina, G. Theerthagiri, B. Bodenmiller, P. Horvath, R. Aebersold, W. Antonin, and U. Kutay. 2011. Phosphorylation of Nup98 by multiple kinases is crucial for NPC disassembly during mitotic entry. Cell. 144:539-550. http://dx.doi.org/10.1016/j.cell.2011.01.012
    • (2011) Cell , vol.144 , pp. 539-550
    • Laurell, E.1    Beck, K.2    Krupina, K.3    Theerthagiri, G.4    Bodenmiller, B.5    Horvath, P.6    Aebersold, R.7    Antonin, W.8    Kutay, U.9
  • 32
    • 0031786125 scopus 로고    scopus 로고
    • The sevenfold way of PKC regulation
    • Liu, W.S., and C.A. Heckman. 1998. The sevenfold way of PKC regulation. Cell. Signal. 10:529-542. http://dx.doi.org/10.1016/S0898-6568(98)00012-6
    • (1998) Cell. Signal , vol.10 , pp. 529-542
    • Liu, W.S.1    Heckman, C.A.2
  • 34
    • 0031037714 scopus 로고    scopus 로고
    • Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5
    • Meijer, L., A. Borgne, O. Mulner, J.P. Chong, J.J. Blow, N. Inagaki, M. Inagaki, J.G. Delcros, and J.P. Moulinoux. 1997. Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5. Eur. J. Biochem. 243:527-536. http://dx.doi.org/10.1111/j.1432-1033.1997.t01-2-00527.x
    • (1997) Eur. J. Biochem , vol.243 , pp. 527-536
    • Meijer, L.1    Borgne, A.2    Mulner, O.3    Chong, J.P.4    Blow, J.J.5    Inagaki, N.6    Inagaki, M.7    Delcros, J.G.8    Moulinoux, J.P.9
  • 35
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C superfamily
    • Mellor, H., and P.J. Parker. 1998. The extended protein kinase C superfamily. Biochem. J. 332:281-292.
    • (1998) Biochem. J. , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 36
    • 34547959246 scopus 로고    scopus 로고
    • An in vitro nuclear disassembly system reveals a role for the RanGTPase system and microtubule-dependent steps in nuclear envelope breakdown
    • Mühlhäusser, P., and U. Kutay. 2007. An in vitro nuclear disassembly system reveals a role for the RanGTPase system and microtubule-dependent steps in nuclear envelope breakdown. J. Cell Biol. 178:595-610. http://dx.doi.org/10.1083/jcb.200703002
    • (2007) J. Cell Biol , vol.178 , pp. 595-610
    • Mühlhäusser, P.1    Kutay, U.2
  • 37
    • 33646057010 scopus 로고    scopus 로고
    • High-throughput RNAi screening by time-lapse imaging of live human cells
    • Neumann, B., M. Held, U. Liebel, H. Erfle, P. Rogers, R. Pepperkok, and J. Ellenberg. 2006. High-throughput RNAi screening by time-lapse imaging of live human cells. Nat. Methods. 3:385-390. http://dx.doi.org/10.1038/nmeth876
    • (2006) Nat. Methods , vol.3 , pp. 385-390
    • Neumann, B.1    Held, M.2    Liebel, U.3    Erfle, H.4    Rogers, P.5    Pepperkok, R.6    Ellenberg, J.7
  • 39
    • 0003982971 scopus 로고    scopus 로고
    • Second edition. Springer-Verlag New York Inc., New York
    • Nocedal, J., and S.J. Wright. 2006. Numerical optimization. Second edition. Springer-Verlag New York Inc., New York. 664 pp.
    • (2006) Numerical optimization , pp. 664
    • Nocedal, J.1    Wright, S.J.2
  • 40
    • 48949102056 scopus 로고    scopus 로고
    • Role of nuclear lamins in nuclear organization, cellular signaling, and inherited diseases
    • Parnaik, V.K. 2008. Role of nuclear lamins in nuclear organization, cellular signaling, and inherited diseases. Int. Rev. Cell Mol. Biol. 266:157-206. http://dx.doi.org/10.1016/S1937-6448(07)66004-3
    • (2008) Int. Rev. Cell Mol. Biol , vol.266 , pp. 157-206
    • Parnaik, V.K.1
  • 41
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations
    • Pearson, R.B., and B.E. Kemp. 1991. Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. Methods Enzymol. 200:62-81. http://dx.doi.org/10.1016/0076-6879(91)00127-I
    • (1991) Methods Enzymol , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 42
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter, M., J. Nakagawa, M. Dorée, J.C. Labbé, and E.A. Nigg. 1990. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell. 61:591-602. http://dx.doi.org/10.1016/ 0092-8674(90)90471-P
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Dorée, M.3    Labbé, J.C.4    Nigg, E.A.5
  • 43
    • 0025736038 scopus 로고
    • Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase
    • Peter, M., E. Heitlinger, M. Häner, U. Aebi, and E.A. Nigg. 1991. Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase. EMBO J. 10:1535-1544.
    • (1991) EMBO J , vol.10 , pp. 1535-1544
    • Peter, M.1    Heitlinger, E.2    Häner, M.3    Aebi, U.4    Nigg, E.A.5
  • 44
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl, M.W., G.W. Horgan, and L. Dempfle. 2002. Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res. 30:e36. http://dx.doi.org/10.1093/nar/30.9.e36
    • (2002) Nucleic Acids Res , vol.30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 46
    • 33747164514 scopus 로고    scopus 로고
    • PKC?: a versatile key for decoding the cellular calcium toolkit
    • Reither, G., M. Schaefer, and P. Lipp. 2006. PKC?: a versatile key for decoding the cellular calcium toolkit. J. Cell Biol. 174:521-533. http://dx.doi.org/10.1083/jcb.200604033
    • (2006) J. Cell Biol , vol.174 , pp. 521-533
    • Reither, G.1    Schaefer, M.2    Lipp, P.3
  • 48
    • 0037059618 scopus 로고    scopus 로고
    • Cytoplasmic dynein as a facilitator of nuclear envelope breakdown
    • Salina, D., K. Bodoor, D.M. Eckley, T.A. Schroer, J.B. Rattner, and B. Burke. 2002. Cytoplasmic dynein as a facilitator of nuclear envelope breakdown. Cell. 108:97-107. http://dx.doi.org/10.1016/S0092-8674(01)00628-6
    • (2002) Cell , vol.108 , pp. 97-107
    • Salina, D.1    Bodoor, K.2    Eckley, D.M.3    Schroer, T.A.4    Rattner, J.B.5    Burke, B.6
  • 49
    • 21244480972 scopus 로고    scopus 로고
    • The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth
    • Santos-Rosa, H., J. Leung, N. Grimsey, S. Peak-Chew, and S. Siniossoglou. 2005. The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth. EMBO J. 24:1931-1941. http://dx.doi.org/10.1038/ sj.emboj.7600672
    • (2005) EMBO J , vol.24 , pp. 1931-1941
    • Santos-Rosa, H.1    Leung, J.2    Grimsey, N.3    Peak-Chew, S.4    Siniossoglou, S.5
  • 50
    • 0035972145 scopus 로고    scopus 로고
    • Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization
    • Schirmer, E.C., T. Guan, and L. Gerace. 2001. Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization. J. Cell Biol. 153:479-489. http://dx.doi.org/10.1083/jcb.153.3.479
    • (2001) J. Cell Biol , vol.153 , pp. 479-489
    • Schirmer, E.C.1    Guan, T.2    Gerace, L.3
  • 52
    • 0031037074 scopus 로고    scopus 로고
    • Identification of a conserved phosphorylation site modulating nuclear lamin polymerization
    • Stuurman, N. 1997. Identification of a conserved phosphorylation site modulating nuclear lamin polymerization. FEBS Lett. 401:171-174. http://dx.doi.org/10.1016/S0014-5793(96)01464-0
    • (1997) FEBS Lett , vol.401 , pp. 171-174
    • Stuurman, N.1
  • 53
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: their structure, assembly, and interactions
    • Stuurman, N., S. Heins, and U. Aebi. 1998. Nuclear lamins: their structure, assembly, and interactions. J. Struct. Biol. 122:42-66. http://dx.doi.org/10.1006/jsbi.1998.3987
    • (1998) J. Struct. Biol , vol.122 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 54
    • 0030722721 scopus 로고    scopus 로고
    • A role for nuclear phosphatidylinositolspecific phospholipase C in the G2/M phase transition
    • Sun, B., N.R. Murray, and A.P. Fields. 1997. A role for nuclear phosphatidylinositolspecific phospholipase C in the G2/M phase transition. J. Biol. Chem. 272:26313-26317. http://dx.doi.org/10.1074/jbc.272.42.26313
    • (1997) J. Biol. Chem , vol.272 , pp. 26313-26317
    • Sun, B.1    Murray, N.R.2    Fields, A.P.3
  • 55
    • 1842856797 scopus 로고    scopus 로고
    • An evolutionarily conserved fission yeast protein, Ned1, implicated in normal nuclear morphology and chromosome stability, interacts with Dis3 Pim1/RCC1 and an essential nucleoporin
    • Tange, Y., A. Hirata, and O. Niwa. 2002. An evolutionarily conserved fission yeast protein, Ned1, implicated in normal nuclear morphology and chromosome stability, interacts with Dis3, Pim1/RCC1 and an essential nucleoporin. J. Cell Sci. 115:4375-4385. http://dx.doi.org/10.1242/ jcs.00135
    • (2002) J. Cell Sci , vol.115 , pp. 4375-4385
    • Tange, Y.1    Hirata, A.2    Niwa, O.3
  • 56
    • 0029666264 scopus 로고    scopus 로고
    • BetaII protein kinase C is required for the G2/M phase transition of cell cycle
    • Thompson, L.J., and A.P. Fields. 1996. BetaII protein kinase C is required for the G2/M phase transition of cell cycle. J. Biol. Chem. 271:15045-15053. http://dx.doi.org/10.1074/jbc.271.25.15045
    • (1996) J. Biol. Chem , vol.271 , pp. 15045-15053
    • Thompson, L.J.1    Fields, A.P.2
  • 57
    • 77950525573 scopus 로고    scopus 로고
    • Automatic identification and clustering of chromosome phenotypes in a genome wide RNAi screen by timelapse imaging
    • Walter, T., M. Held, B. Neumann, J.-K. Hériché, C. Conrad, R. Pepperkok, and J. Ellenberg. 2010. Automatic identification and clustering of chromosome phenotypes in a genome wide RNAi screen by timelapse imaging. J. Struct. Biol. 170:1-9. http://dx.doi.org/10.1016/j.jsb.2009.10.004
    • (2010) J. Struct. Biol , vol.170 , pp. 1-9
    • Walter, T.1    Held, M.2    Neumann, B.3    Hériché, J.-K.4    Conrad, C.5    Pepperkok, R.6    Ellenberg, J.7
  • 58
    • 0025285068 scopus 로고
    • Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C
    • Ward, G.E., and M.W. Kirschner. 1990. Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C. Cell. 61:561-577. http://dx.doi.org/10.1016/0092-8674(90)90469-U
    • (1990) Cell , vol.61 , pp. 561-577
    • Ward, G.E.1    Kirschner, M.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.