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Volumn 23, Issue 23, 2012, Pages 4579-4591

Myosin Vs organize actin cables in fission yeast

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; KINESIN; KINESIN 7; METHENAMINE; MYOSIN; MYOSIN 52; UNCLASSIFIED DRUG;

EID: 84870563175     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-07-0499     Document Type: Article
Times cited : (35)

References (58)
  • 1
    • 0031818471 scopus 로고    scopus 로고
    • Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe
    • DOI 10.1002/(SICI)1097-0061(199807)14:10<943::AID-YEA292>3.0.CO;2-Y
    • Bahler J, Wu JQ, Longtine MS, Shah NG, McKenzie A, Steever AB, Wach A, Philippsen P, Pringle JR (1998). Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe. Yeast 14, 943-951. (Pubitemid 28328000)
    • (1998) Yeast , vol.14 , Issue.10 , pp. 943-951
    • Bahler, J.1    Wu, J.-Q.2    Longtine, M.S.3    Shah, N.G.4    McKenzie III, A.5    Steever, A.B.6    Wach, A.7    Philippsen, P.8    Pringle, J.R.9
  • 2
    • 0026438291 scopus 로고
    • A new tropomyosin essential for cytokinesis in the fission yeast S. pombe
    • Balasubramanian MK, Helfman DM, Hemmingsen SM (1992). A new tropomyosin essential for cytokinesis in the fission yeast S. pombe. Nature 360, 84-87.
    • (1992) Nature , vol.360 , pp. 84-87
    • Balasubramanian, M.K.1    Helfman, D.M.2    Hemmingsen, S.M.3
  • 3
    • 0030611667 scopus 로고    scopus 로고
    • Ma13, the fission yeast homologue of the human APC-interacting protein EB-1 is required for microtubule integrity and the maintenance of cell form
    • DOI 10.1083/jcb.139.3.717
    • Beinhauer JD, Hagan IM, Hegemann JH, Fleig U (1997). Mal3, the fission yeast homologue of the human APC-interacting protein EB-1 is required for microtubule integrity and the maintenance of cell form. J Cell Biol 139, 717-728. (Pubitemid 27485837)
    • (1997) Journal of Cell Biology , vol.139 , Issue.3 , pp. 717-728
    • Beinhauer, J.D.1    Hagan, I.M.2    Hegemann, J.H.3    Fleig, U.4
  • 4
    • 78651106804 scopus 로고    scopus 로고
    • Actin cables and the exocyst form two independent morphogenesis pathways in the fission yeast
    • Bendezu FO, Martin SG (2011). Actin cables and the exocyst form two independent morphogenesis pathways in the fission yeast. Mol Biol Cell 22, 44-53.
    • (2011) Mol Biol Cell , vol.22 , pp. 44-53
    • Bendezu, F.O.1    Martin, S.G.2
  • 5
    • 0036122307 scopus 로고    scopus 로고
    • Myosin-X is an unconventional myosin that undergoes intrafilopodial motility
    • DOI 10.1038/ncb762
    • Berg JS, Cheney RE (2002). Myosin-X is an unconventional myosin that undergoes intrafilopodial motility. Nat Cell Biol 4, 246-250. (Pubitemid 34218199)
    • (2002) Nature Cell Biology , vol.4 , Issue.3 , pp. 246-250
    • Berg, J.S.1    Cheney, R.E.2
  • 7
    • 34248217508 scopus 로고    scopus 로고
    • Spatial regulation of exocytosis and cell polarity: Yeast as a model for animal cells
    • DOI 10.1016/j.febslet.2007.03.043, PII S0014579307003183, Membrane Trafficking
    • Brennwald P, Rossi G (2007). Spatial regulation of exocytosis and cell polarity: yeast as a model for animal cells. FEBS Lett 581, 2119-2124. (Pubitemid 46709909)
    • (2007) FEBS Letters , vol.581 , Issue.11 , pp. 2119-2124
    • Brennwald, P.1    Rossi, G.2
  • 8
    • 34248170173 scopus 로고    scopus 로고
    • Yeast formins Bni1 and Bnr1 utilize different modes of cortical interaction during the assembly of actin cables
    • DOI 10.1091/mbc.E06-09-0820
    • Buttery SM, Yoshida S, Pellman D (2007). Yeast formins Bni1 and Bnr1 utilize different modes of cortical interaction during the assembly of actin cables. Mol Biol Cell 18, 1826-1838. (Pubitemid 46717563)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.5 , pp. 1826-1838
    • Buttery, S.M.1    Yoshida, S.2    Pellman, D.3
  • 10
    • 72949110575 scopus 로고    scopus 로고
    • Unleashing formins to remodel the actin and microtubule cytoskeletons
    • Chesarone MA, DuPage AG, Goode BL (2011). Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat Rev Mol Cell Biol 11, 62-74.
    • (2011) Nat Rev Mol Cell Biol , vol.11 , pp. 62-74
    • Chesarone, M.A.1    DuPage, A.G.2    Goode, B.L.3
  • 11
    • 79961235785 scopus 로고    scopus 로고
    • The myosin passenger protein Smy1 controls actin cable structure and dynamics by acting as a formin damper
    • Chesarone-Cataldo M, Guerin C, Yu JH, Wedlich-Soldner R, Blanchoin L, Goode BL (2011). The myosin passenger protein Smy1 controls actin cable structure and dynamics by acting as a formin damper. Dev Cell 21, 217-230.
    • (2011) Dev Cell , vol.21 , pp. 217-230
    • Chesarone-Cataldo, M.1    Guerin, C.2    Yu, J.H.3    Wedlich-Soldner, R.4    Blanchoin, L.5    Goode, B.L.6
  • 12
    • 77957834345 scopus 로고    scopus 로고
    • Differential regulation of unconventional fission yeast myosins via the actin track
    • Clayton JE, Sammons MR, Stark BC, Hodges AR, Lord M (2010). Differential regulation of unconventional fission yeast myosins via the actin track. Curr Biol 20, 1423-1431.
    • (2010) Curr Biol , vol.20 , pp. 1423-1431
    • Clayton, J.E.1    Sammons, M.R.2    Stark, B.C.3    Hodges, A.R.4    Lord, M.5
  • 13
    • 33746528109 scopus 로고    scopus 로고
    • Asymmetric Microtubule Pushing Forces in Nuclear Centering
    • DOI 10.1016/j.cub.2006.06.026, PII S0960982206017532
    • Daga RR, Yonetani A, Chang F (2006). Asymmetric microtubule pushing forces in nuclear centering. Curr Biol 16, 1544-1550. (Pubitemid 44142980)
    • (2006) Current Biology , vol.16 , Issue.15 , pp. 1544-1550
    • Daga, R.R.1    Yonetani, A.2    Chang, F.3
  • 14
    • 70849102262 scopus 로고    scopus 로고
    • Fission yeast Myo51 is a meiotic spindle pole body component with discrete roles during cell fusion and spore formation
    • Doyle A, Martin-Garcia R, Coulton AT, Bagley S, Mulvihill DP (2009). Fission yeast Myo51 is a meiotic spindle pole body component with discrete roles during cell fusion and spore formation. J Cell Sci 122, 4330-4340.
    • (2009) J Cell Sci , vol.122 , pp. 4330-4340
    • Doyle, A.1    Martin-Garcia, R.2    Coulton, A.T.3    Bagley, S.4    Mulvihill, D.P.5
  • 15
    • 40049092263 scopus 로고    scopus 로고
    • Opposite effects of overexpressed myosin Va or heavy meromyosin Va on vesicle distribution, cytoskeleton organization, and cell motility in nonmuscle cells
    • DOI 10.1002/cm.20255
    • Eppinga RD, Peng IF, Lin JLC, Wu CF, Lin JJC (2008). Opposite effects of overexpressed myosin Va or heavy meromyosin Va on vesicle distribution, cytoskeleton organization, and cell motility in nonmuscle cells. Cell Motil Cytoskeleton 65, 197-215. (Pubitemid 351323741)
    • (2008) Cell Motility and the Cytoskeleton , vol.65 , Issue.3 , pp. 197-215
    • Eppinga, R.D.1    Peng, I.-F.2    Lin, J.L.-C.3    Wu, C.-F.4    Lin, J.J.-C.5
  • 16
    • 84870557616 scopus 로고    scopus 로고
    • Identification of for3, a S. pombe formin-homology gene involved in cell polarity, actin cable formation, and symmetric cell division
    • Feierbach B, Chang F (2001). Identification of for3, a S. pombe formin-homology gene involved in cell polarity, actin cable formation, and symmetric cell division. Mol Biol Cell 12, 49A.
    • (2001) Mol Biol Cell , vol.12
    • Feierbach, B.1    Chang, F.2
  • 17
    • 27144491107 scopus 로고    scopus 로고
    • Endocytosis in fission yeast is spatially associated with the actin cytoskeleton during polarised cell growth and cytokinesis
    • DOI 10.1242/jcs.02530
    • Gachet Y, Hyams JS (2005). Endocytosis in fission yeast is spatially associated with the actin cytoskeleton during polarised cell growth and cytokinesis. J Cell Sci 118, 4231-4242. (Pubitemid 41488960)
    • (2005) Journal of Cell Science , vol.118 , Issue.18 , pp. 4231-4242
    • Gachet, Y.1    Hyams, J.S.2
  • 18
    • 20544459380 scopus 로고    scopus 로고
    • Structurally conserved interaction of Lgl family with SNAREs is critical to their cellular function
    • DOI 10.1016/j.cub.2005.05.046, PII S0960982205005610
    • Gangar A, Rossi G, Andreeva A, Hales R, Brennwald P (2005). Structurally conserved interaction of Lgl family with SNAREs is critical to their cellular function. Curr Biol 15, 1136-1142. (Pubitemid 40841358)
    • (2005) Current Biology , vol.15 , Issue.12 , pp. 1136-1142
    • Gangar, A.1    Rossi, G.2    Andreeva, A.3    Hales, R.4    Brennwald, P.5
  • 19
    • 38349047918 scopus 로고    scopus 로고
    • In vivo movement of the type V myosin Myo52 requires dimerisation but is independent of the neck domain
    • Grallert A, Martin-Garcia R, Bagley S, Mulvihill DP (2007). In vivo movement of the type V myosin Myo52 requires dimerisation but is independent of the neck domain. J Cell Sci 120, 4093-4098.
    • (2007) J Cell Sci , vol.120 , pp. 4093-4098
    • Grallert, A.1    Martin-Garcia, R.2    Bagley, S.3    Mulvihill, D.P.4
  • 20
    • 84355161386 scopus 로고    scopus 로고
    • Walking to work: Roles for class V myosins as cargo transporters
    • Hammer JA, Sellers JR (2012). Walking to work: roles for class V myosins as cargo transporters. Nat Rev Mol Cell Biol 13, 13-26.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 13-26
    • Hammer, J.A.1    Sellers, J.R.2
  • 21
    • 33645797841 scopus 로고    scopus 로고
    • Genetic and functional interaction between Ryh1 and Ypt3: Two Rab GTPases that function in S. pombe secretory pathway
    • He Y, Sugiura R, Ma Y, Kita A, Deng L, Takegawa K, Matsuoka K, Shuntoh H, Kuno T (2006). Genetic and functional interaction between Ryh1 and Ypt3: two Rab GTPases that function in S. pombe secretory pathway. Genes Cells 11, 207-221.
    • (2006) Genes Cells , vol.11 , pp. 207-221
    • He, Y.1    Sugiura, R.2    Ma, Y.3    Kita, A.4    Deng, L.5    Takegawa, K.6    Matsuoka, K.7    Shuntoh, H.8    Kuno, T.9
  • 22
    • 33845689351 scopus 로고    scopus 로고
    • Roles of type II myosin and a tropomyosin isoform in retrograde actin flow in budding yeast
    • DOI 10.1083/jcb.200609155
    • Huckaba TM, Lipkin T, Pon LA (2006). Roles of type II myosin and a tropomyosin isoform in retrograde actin flow in budding yeast. J Cell Biol 175, 957-969. (Pubitemid 44969201)
    • (2006) Journal of Cell Biology , vol.175 , Issue.6 , pp. 957-969
    • Huckaba, T.M.1    Lipkin, T.2    Pon, L.A.3
  • 23
    • 26944432407 scopus 로고    scopus 로고
    • Directionality of F-actin cables changes during the fission yeast cell cycle
    • DOI 10.1038/ncb1295, PII N1295
    • Kamasaki T, Arai R, Osumi M, Mabuchi I (2005). Directionality of F-actin cables changes during the fission yeast cell cycle. Nat Cell Biol 7, 916-917. (Pubitemid 41486293)
    • (2005) Nature Cell Biology , vol.7 , Issue.9 , pp. 916-917
    • Kamasaki, T.1    Arai, R.2    Osumi, M.3    Mabuchi, I.4
  • 24
    • 11144341960 scopus 로고    scopus 로고
    • The nuclear kinase Lsk1p positively regulates the septation initiation network and promotes the successful completion of cytokinesis in response to perturbation of the actomyosin ring in Schizosaccharomyces pombe
    • DOI 10.1091/mbc.E04-06-0502
    • Karagiannis J, Bimbo A, Rajagopalan S, Liu JH, Balasubramanian MK (2005). The nuclear kinase Lsk1p positively regulates the septation initiation network and promotes the successful completion of cytokinesis in response to perturbation of the actomyosin ring in Schizosaccharomyces pombe. Mol Biol Cell 16, 358-371. (Pubitemid 40024317)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.1 , pp. 358-371
    • Karagiannis, J.1    Bimbo, A.2    Rajagopalan, S.3    Liu, J.4    Balasubramanian, M.K.5
  • 25
    • 11244345198 scopus 로고    scopus 로고
    • Processive capping by formin suggests a force-driven mechanism of actin polymerization
    • DOI 10.1083/jcb.200410017
    • Kozlov MM, Bershadsky AD (2004). Processive capping by formin suggests a force-driven mechanism of actin polymerization. J Cell Biol 167, 1011-1017. (Pubitemid 40066617)
    • (2004) Journal of Cell Biology , vol.167 , Issue.6 , pp. 1011-1017
    • Kozlov, M.M.1    Bershadsky, A.D.2
  • 26
    • 38849084743 scopus 로고    scopus 로고
    • The tail that wags the dog: The globular tail domain defines the function of myosin V/XI
    • Li JF, Nebenfuhr A (2008). The tail that wags the dog: the globular tail domain defines the function of myosin V/XI. Traffic 9, 290-298.
    • (2008) Traffic , vol.9 , pp. 290-298
    • Li, J.F.1    Nebenfuhr, A.2
  • 27
    • 57349092518 scopus 로고    scopus 로고
    • Direct interaction between a myosin V motor and the Rab GTPases Ypt31/32 is required for polarized secretion
    • Lipatova Z, Tokarev AA, Jin Y, Mulholland J, Weisman LS, Segev N (2008). Direct interaction between a myosin V motor and the Rab GTPases Ypt31/32 is required for polarized secretion. Mol Biol Cell 19, 4177-4187.
    • (2008) Mol Biol Cell , vol.19 , pp. 4177-4187
    • Lipatova, Z.1    Tokarev, A.A.2    Jin, Y.3    Mulholland, J.4    Weisman, L.S.5    Segev, N.6
  • 28
    • 84155163220 scopus 로고    scopus 로고
    • Shaping fission yeast cells by rerouting actin-based transport on microtubules
    • Lo Presti L, Martin SG (2011). Shaping fission yeast cells by rerouting actin-based transport on microtubules. Curr Biol 21, 2064-2069.
    • (2011) Curr Biol , vol.21 , pp. 2064-2069
    • Lo Presti, L.1    Martin, S.G.2
  • 29
    • 33745003433 scopus 로고    scopus 로고
    • Dynamics of the Formin For3p in Actin Cable Assembly
    • DOI 10.1016/j.cub.2006.04.040, PII S0960982206015375
    • Martin SG, Chang F (2006). Dynamics of the formin For3p in actin cable assembly. Curr Biol 16, 1161-1170. (Pubitemid 43867291)
    • (2006) Current Biology , vol.16 , Issue.12 , pp. 1161-1170
    • Martin, S.G.1    Chang, F.2
  • 30
    • 16244409515 scopus 로고    scopus 로고
    • Tea4p links microtubule plus ends with the formin for3p in the establishment of cell polarity
    • DOI 10.1016/j.devcel.2005.02.008, PII S153458070500078X
    • Martin SG, McDonald WH, Yates JR, Chang F (2005). Tea4p links microtubule plus ends with the formin For3p in the establishment of cell polarity. Dev Cell 8, 479-491. (Pubitemid 40450738)
    • (2005) Developmental Cell , vol.8 , Issue.4 , pp. 479-491
    • Martin, S.G.1    McDonald, W.H.2    Yates III, J.R.3    Chang, F.4
  • 32
    • 70450246898 scopus 로고    scopus 로고
    • Myosin V spatially regulates microtubule dynamics and promotes the ubiquitin-dependent degradation of the fission yeast CLIP-170 homologue, Tip1
    • Martin-Garcia R, Mulvihill DP (2009). Myosin V spatially regulates microtubule dynamics and promotes the ubiquitin-dependent degradation of the fission yeast CLIP-170 homologue, Tip1. J Cell Sci 122, 3862-3872.
    • (2009) J Cell Sci , vol.122 , pp. 3862-3872
    • Martin-Garcia, R.1    Mulvihill, D.P.2
  • 33
    • 33749258375 scopus 로고    scopus 로고
    • The yeast actin cytoskeleton: From cellular function to biochemical mechanism
    • DOI 10.1128/MMBR.00013-06
    • Moseley JB, Goode BL (2006). The yeast actin cytoskeleton: from cellular function to biochemical mechanism. Microbiol Mol Biol Rev 70, 605-645. (Pubitemid 44484687)
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.3 , pp. 605-645
    • Moseley, J.B.1    Goode, B.L.2
  • 34
    • 0034768448 scopus 로고    scopus 로고
    • Identification of two type V myosins in fission yeast, one of which functions in polarized cell growth and moves rapidly in the cell
    • Motegi F, Arai R, Mabuchi I (2001). Identification of two type V myosins in fission yeast, one of which functions in polarized cell growth and moves rapidly in the cell. Mol Biol Cell 12, 1367-1380. (Pubitemid 33044417)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.5 , pp. 1367-1380
    • Motegi, F.1    Arai, R.2    Mabuchi, I.3
  • 35
    • 33644872713 scopus 로고    scopus 로고
    • A critical role for the type V Myosin, Myo52, in septum deposition and cell fission during cytokinesis in Schizosaccharomyces pombe
    • DOI 10.1002/cm.20113
    • Mulvihill DP, Edwards SR, Hyams JS (2006). A critical role for the type V myosin, Myo52, in septum deposition and cell fission during cytokinesis in Schizosaccharomyces pombe. Cell Motil Cytoskeleton 63, 149-161. (Pubitemid 43376369)
    • (2006) Cell Motility and the Cytoskeleton , vol.63 , Issue.3 , pp. 149-161
    • Mulvihill, D.P.1    Edwards, S.R.2    Hyams, J.S.3
  • 36
    • 0035943108 scopus 로고    scopus 로고
    • Myosin V-mediated vacuole distribution and fusion in fission yeast
    • DOI 10.1016/S0960-9822(01)00322-0
    • Mulvihill DP, Pollard PJ, Win TZ, Hyams JS (2001). Myosin V-mediated vacuole distribution and fusion in fission yeast. Curr Biol 11, 1124-1127. (Pubitemid 32675765)
    • (2001) Current Biology , vol.11 , Issue.14 , pp. 1124-1127
    • Mulvihill, D.P.1    Pollard, P.J.2    Win, T.Z.3    Hyams, J.S.4
  • 37
    • 12244291296 scopus 로고    scopus 로고
    • The small GTPase Rho3 and the diaphanous/formin For3 function in polarized cell growth in fission yeast
    • DOI 10.1242/jcs.00150
    • Nakano K, Imai J, Arai R, Toh EA, Matsui Y, Mabuchi I (2002). The small GTPase Rho3 and the diaphanous/formin For3 function in polarized cell growth in fission yeast. J Cell Sci 115, 4629-4639. (Pubitemid 36004422)
    • (2002) Journal of Cell Science , vol.115 , Issue.23 , pp. 4629-4639
    • Nakano, K.1    Imai, J.2    Arai, R.3    Toh-e, A.4    Matsui, Y.5    Mabuchi, I.6
  • 38
    • 77950613612 scopus 로고    scopus 로고
    • Myosin motor function: The ins and outs of actin-based membrane protrusions
    • Nambiar R, McConnell RE, Tyska MJ (2010). Myosin motor function: the ins and outs of actin-based membrane protrusions. Cell Mol Life Sci 67, 1239-1254.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 1239-1254
    • Nambiar, R.1    McConnell, R.E.2    Tyska, M.J.3
  • 39
    • 77955896359 scopus 로고    scopus 로고
    • Class XI myosins are required for development, cell expansion, and F-actin organization in Arabidopsis
    • Peremyslov VV, Prokhnevsky AI, Dolja VV (2010). Class XI myosins are required for development, cell expansion, and F-actin organization in Arabidopsis. Plant Cell 22, 1883-1897.
    • (2010) Plant Cell , vol.22 , pp. 1883-1897
    • Peremyslov, V.V.1    Prokhnevsky, A.I.2    Dolja, V.V.3
  • 42
    • 0032938745 scopus 로고    scopus 로고
    • Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70
    • Robinson NCG, Guo L, Imai J, Toh-E A, Matsui Y, Tamanoi F (1999). Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70. Mol Cell Biol 19, 3580-3587. (Pubitemid 29193817)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.5 , pp. 3580-3587
    • Robinson, N.G.G.1    Guo, L.2    Imai, J.3    Toh-E, A.4    Matsui, Y.5    Tamanoi, F.6
  • 44
    • 79952853575 scopus 로고    scopus 로고
    • Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis
    • Rossi G, Brennwald P (2011). Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis. Mol Biol Cell 22, 842-857.
    • (2011) Mol Biol Cell , vol.22 , pp. 842-857
    • Rossi, G.1    Brennwald, P.2
  • 45
    • 74949100104 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides
    • Saarikangas J, Zhao HX, Lappalainen P (2010). Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides. Physiol Rev 90, 259-289.
    • (2010) Physiol Rev , vol.90 , pp. 259-289
    • Saarikangas, J.1    Zhao, H.X.2    Lappalainen, P.3
  • 46
    • 80054714234 scopus 로고    scopus 로고
    • The functionally distinct fission yeast formins have specific actin-assembly properties
    • Scott BJ, Neidt EM, Kovar DR (2011). The functionally distinct fission yeast formins have specific actin-assembly properties. Mol Biol Cell 22, 3826-3839.
    • (2011) Mol Biol Cell , vol.22 , pp. 3826-3839
    • Scott, B.J.1    Neidt, E.M.2    Kovar, D.R.3
  • 47
    • 34347383511 scopus 로고    scopus 로고
    • Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex
    • DOI 10.1038/ncb1604, PII NCB1604
    • Stelter P, Kunze R, Flemming D, Hopfner D, Diepholz M, Philippsen P, Bottcher B, Hurt E (2007). Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex. Nat Cell Biol 9, 788-796. (Pubitemid 47019465)
    • (2007) Nature Cell Biology , vol.9 , Issue.7 , pp. 788-796
    • Stelter, P.1    Kunze, R.2    Flemming, D.3    Hopfner, D.4    Diepholz, M.5    Philippsen, P.6    Bottcher, B.7    Hurt, E.8
  • 48
    • 70350304803 scopus 로고    scopus 로고
    • Fission yeast IQGAP arranges actin filaments into the cytokinetic contractile ring
    • Takaine M, Numata O, Nakano K (2009). Fission yeast IQGAP arranges actin filaments into the cytokinetic contractile ring. EMBO J 28, 3117-3131.
    • (2009) EMBO J , vol.28 , pp. 3117-3131
    • Takaine, M.1    Numata, O.2    Nakano, K.3
  • 49
    • 21844445841 scopus 로고    scopus 로고
    • Nuclear and division-plane positioning revealed by optical micromanipulation
    • DOI 10.1016/j.cub.2005.05.052, PII S0960982205005671
    • Tolic-Norrelykke IM, Sacconi L, Stringari C, Raabe I, Pavone FS (2005). Nuclear and division-plane positioning revealed by optical micromanipulation. Curr Biol 15, 1212-1216. (Pubitemid 40950519)
    • (2005) Current Biology , vol.15 , Issue.13 , pp. 1212-1216
    • Tolic-Norrelykke, I.M.1    Sacconi, L.2    Stringari, C.3    Raabe, I.4    Pavone, F.S.5
  • 50
    • 0035897404 scopus 로고    scopus 로고
    • A mechanism for nuclear positioning in fission yeast based on microtubule pushing
    • DOI 10.1083/jcb.153.2.397
    • Tran PT, Marsh L, Doye V, Inoué S, Chang F (2001). A mechanism for nuclear positioning in fission yeast based on microtubule pushing. J Cell Biol 153, 397-411. (Pubitemid 34280223)
    • (2001) Journal of Cell Biology , vol.153 , Issue.2 , pp. 397-411
    • Tran, P.T.1    Marsh, L.2    Doye, V.3    Inoue, S.4    Chang, F.5
  • 51
    • 43049183000 scopus 로고    scopus 로고
    • Myosin V from head to tail
    • Trybus KM (2008). Myosin V from head to tail. Cell Mol Life Sci 65, 1378-1389.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1378-1389
    • Trybus, K.M.1
  • 53
    • 0029610382 scopus 로고
    • Fission yeast cell morphogenesis: Identification of new genes and analysis of their role during the cell cycle
    • DOI 10.1083/jcb.131.6.1529
    • Verde F, Mata J, Nurse P (1995). Fission yeast-cell morphogenesis - identification of new genes and analysis of their role during the cell-cycle. J Cell Biol 131, 1529-1538. (Pubitemid 26001756)
    • (1995) Journal of Cell Biology , vol.131 , Issue.6 I , pp. 1529-1538
    • Verde, F.1    Mata, J.2    Nurse, P.3
  • 55
    • 78650515235 scopus 로고    scopus 로고
    • Myosin-Va transports the endoplasmic reticulum into the dendritic spines of Purkinje neurons
    • Wagner W, Brenowitz SD, Hammer JA (2011). Myosin-Va transports the endoplasmic reticulum into the dendritic spines of Purkinje neurons. Nat Cell Biol 13, 40-48.
    • (2011) Nat Cell Biol , vol.13 , pp. 40-48
    • Wagner, W.1    Brenowitz, S.D.2    Hammer, J.A.3
  • 56
    • 0035150529 scopus 로고    scopus 로고
    • Two type V myosins with non-overlapping functions in the fission yeast Schizosaccharomyces pombe: Myo52 is concerned with growth polarity and cytokinesis, Myo51 is a component of the cytokinetic actin ring
    • Win TZ, Gachet Y, Mulvihill DP, May KM, Hyams JS (2001). Two type V myosins with non-overlapping functions in the fission yeast Schizosaccharomyces pombe: Myo52 is concerned with growth polarity and cytokinesis, Myo51 is a component of the cytokinetic actin ring. J Cell Sci 114, 69-79.
    • (2001) J Cell Sci , vol.114 , pp. 69-79
    • Win, T.Z.1    Gachet, Y.2    Mulvihill, D.P.3    May, K.M.4    Hyams, J.S.5
  • 57
    • 66349129521 scopus 로고    scopus 로고
    • Unconventional myosins acting unconventionally
    • Woolner S, Bement WM (2009). Unconventional myosins acting unconventionally. Trends Cell Biol 19, 245-252.
    • (2009) Trends Cell Biol , vol.19 , pp. 245-252
    • Woolner, S.1    Bement, W.M.2


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