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Volumn 187, Issue 7, 2009, Pages 1055-1069

Actin remodeling by ADF/cofilin is required for cargo sorting at the trans-Golgi network

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; COFILIN; MEMBRANE PROTEIN; PROTEIN; PROTEIN ADF; UNCLASSIFIED DRUG;

EID: 76149090527     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200908040     Document Type: Article
Times cited : (91)

References (48)
  • 1
    • 0242298589 scopus 로고    scopus 로고
    • The Rab8 GTPase selectively regulates AP-1B - dependent basolateral transport in polarized Madin-Darby canine kidney cells
    • doi:10.1083/jcb.200307046
    • Ang, A.L., H. Fölsch, U.M. Koivisto, M. Pypaert, and I. Mellman. 2003. The Rab8 GTPase selectively regulates AP-1B - dependent basolateral transport in polarized Madin-Darby canine kidney cells. J. Cell Biol. 163:339-350. doi:10.1083/jcb.200307046
    • (2003) J. Cell Biol , vol.163 , pp. 339-350
    • Ang, A.L.1    Fölsch, H.2    Koivisto, U.M.3    Pypaert, M.4    Mellman, I.5
  • 2
    • 8444221583 scopus 로고    scopus 로고
    • Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells
    • doi:10.1083/jcb.200408165
    • Ang, A.L., T. Taguchi, S. Francis, H. Fölsch, L.J. Murrells, M. Pypaert, G. Warren, and I. Mellman. 2004. Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells. J. Cell Biol. 167:531-543. doi:10.1083/jcb.200408165
    • (2004) J. Cell Biol , vol.167 , pp. 531-543
    • Ang, A.L.1    Taguchi, T.2    Francis, S.3    Fölsch, H.4    Murrells, L.J.5    Pypaert, M.6    Warren, G.7    Mellman, I.8
  • 3
    • 0032565962 scopus 로고    scopus 로고
    • Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase
    • doi:10.1038/31729
    • Arber, S., F.A. Barbayannis, H. Hanser, C. Schneider, C.A. Stanyon, O. Bernard, and P. Caroni. 1998. Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature. 393:805-809. doi:10.1038/31729
    • (1998) Nature , vol.393 , pp. 805-809
    • Arber, S.1    Barbayannis, F.A.2    Hanser, H.3    Schneider, C.4    Stanyon, C.A.5    Bernard, O.6    Caroni, P.7
  • 4
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • doi:10.1146/annurev.cellbio.15.1.185
    • Bamburg, J.R. 1999. Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu. Rev. Cell Dev. Biol. 15:185-230. doi:10.1146/annurev.cellbio.15.1.185
    • (1999) Annu. Rev. Cell Dev. Biol , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 6
    • 14044272872 scopus 로고    scopus 로고
    • Live imaging of bidirectional traffic from the ERGIC
    • doi:10.1242/jcs.01615
    • Ben-Tekaya, H., K. Miura, R. Pepperkok, and H.P. Hauri. 2005. Live imaging of bidirectional traffic from the ERGIC. J. Cell Sci. 118:357-367. doi:10.1242/jcs.01615
    • (2005) J. Cell Sci , vol.118 , pp. 357-367
    • Ben-Tekaya, H.1    Miura, K.2    Pepperkok, R.3    Hauri, H.P.4
  • 7
    • 37249016585 scopus 로고    scopus 로고
    • Dimeric PKD regulates membrane fission to form transport carriers at the TGN
    • Bossard, C., D. Bresson, R.S. Polishchuk, and V. Malhotra. 2007. Dimeric PKD regulates membrane fission to form transport carriers at the TGN. J. Cell Biol. 179:1123-1131.
    • (2007) J. Cell Biol , vol.179 , pp. 1123-1131
    • Bossard, C.1    Bresson, D.2    Polishchuk, R.S.3    Malhotra, V.4
  • 8
    • 64049091643 scopus 로고    scopus 로고
    • Cofilin dissociates Arp2/3 complex and branches from actin filaments
    • doi:10.1016/j.cub.2009.02.060
    • Chan, C., C.C. Beltzner, and T.D. Pollard. 2009. Cofilin dissociates Arp2/3 complex and branches from actin filaments. Curr. Biol. 19:537-545. doi:10.1016/j.cub.2009.02.060
    • (2009) Curr. Biol , vol.19 , pp. 537-545
    • Chan, C.1    Beltzner, C.C.2    Pollard, T.D.3
  • 9
    • 57449099865 scopus 로고    scopus 로고
    • Cox, J., and M. Mann. 2008. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26:1367-1372. doi:10.1038/nbt.1511
    • Cox, J., and M. Mann. 2008. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26:1367-1372. doi:10.1038/nbt.1511
  • 10
    • 0031863118 scopus 로고    scopus 로고
    • Golgi-disturbing agents
    • doi:10.1007/s004180050256
    • Dinter, A., and E.G. Berger. 1998. Golgi-disturbing agents. Histochem. Cell Biol. 109:571-590. doi:10.1007/s004180050256
    • (1998) Histochem. Cell Biol , vol.109 , pp. 571-590
    • Dinter, A.1    Berger, E.G.2
  • 11
    • 33644873004 scopus 로고    scopus 로고
    • Actin dynamics at the Golgi complex in mammalian cells
    • doi:10.1016/j.ceb.2006.02.007
    • Egea, G., F. Lázaro-Diéguez, and M. Vilella. 2006. Actin dynamics at the Golgi complex in mammalian cells. Curr. Opin. Cell Biol. 18:168-178. doi:10.1016/j.ceb.2006.02.007
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 168-178
    • Egea, G.1    Lázaro-Diéguez, F.2    Vilella, M.3
  • 12
    • 0032692619 scopus 로고    scopus 로고
    • A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells
    • doi:10.1016/S0092-8674(00)81650-5
    • Fölsch, H., H. Ohno, J.S. Bonifacino, and I. Mellman. 1999. A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. Cell. 99:189-198. doi:10.1016/S0092-8674(00)81650-5
    • (1999) Cell , vol.99 , pp. 189-198
    • Fölsch, H.1    Ohno, H.2    Bonifacino, J.S.3    Mellman, I.4
  • 13
    • 67649891328 scopus 로고    scopus 로고
    • Taking the scenic route: Biosynthetic traffic to the plasma membrane in polarized epithelial cells
    • doi:10.1111/j.1600-0854.2009.00927.x
    • Fölsch, H., P.E. Mattila, and O.A. Weisz. 2009. Taking the scenic route: biosynthetic traffic to the plasma membrane in polarized epithelial cells. Traffic. 10:972-981. doi:10.1111/j.1600-0854.2009.00927.x
    • (2009) Traffic , vol.10 , pp. 972-981
    • Fölsch, H.1    Mattila, P.E.2    Weisz, O.A.3
  • 14
    • 0344304559 scopus 로고    scopus 로고
    • Mammalian GGAs act together to sort mannose 6-phosphate receptors
    • doi:10.1083/jcb.200308038
    • Ghosh, P., J. Griffith, H.J. Geuze, and S. Kornfeld. 2003. Mammalian GGAs act together to sort mannose 6-phosphate receptors. J. Cell Biol. 163:755-766. doi:10.1083/jcb.200308038
    • (2003) J. Cell Biol , vol.163 , pp. 755-766
    • Ghosh, P.1    Griffith, J.2    Geuze, H.J.3    Kornfeld, S.4
  • 15
    • 0021978631 scopus 로고
    • Processing of human cathepsin D in lysosomes in vitro
    • Gieselmann, V., A. Hasilik, and K. von Figura. 1985. Processing of human cathepsin D in lysosomes in vitro. J. Biol. Chem. 260:3215-3220.
    • (1985) J. Biol. Chem , vol.260 , pp. 3215-3220
    • Gieselmann, V.1    Hasilik, A.2    von Figura, K.3
  • 16
    • 0032433851 scopus 로고    scopus 로고
    • The curious status of the Golgi apparatus
    • doi:10.1016/S0092-8674(00)81713-4
    • Glick, B.S., and V. Malhotra. 1998. The curious status of the Golgi apparatus. Cell. 95:883-889. doi:10.1016/S0092-8674(00)81713-4
    • (1998) Cell , vol.95 , pp. 883-889
    • Glick, B.S.1    Malhotra, V.2
  • 17
    • 70350230237 scopus 로고    scopus 로고
    • Membrane traffic within the Golgi apparatus
    • Glick, B.S., and A. Nakano. 2009. Membrane traffic within the Golgi apparatus. Annu. Rev. Cell Dev. Biol. 25:113-132.
    • (2009) Annu. Rev. Cell Dev. Biol , vol.25 , pp. 113-132
    • Glick, B.S.1    Nakano, A.2
  • 18
    • 57149125825 scopus 로고    scopus 로고
    • Nanoclusters of GPI-anchored proteins are formed by cortical actin-driven activity
    • doi:10.1016/j.cell.2008.11.032
    • Goswami, D., K. Gowrishankar, S. Bilgrami, S. Ghosh, R. Raghupathy, R. Chadda, R. Vishwakarma, M. Rao, and S. Mayor. 2008. Nanoclusters of GPI-anchored proteins are formed by cortical actin-driven activity. Cell. 135:1085-1097. doi:10.1016/j.cell.2008.11.032
    • (2008) Cell , vol.135 , pp. 1085-1097
    • Goswami, D.1    Gowrishankar, K.2    Bilgrami, S.3    Ghosh, S.4    Raghupathy, R.5    Chadda, R.6    Vishwakarma, R.7    Rao, M.8    Mayor, S.9
  • 19
    • 40649095957 scopus 로고    scopus 로고
    • Quantitative proteomics using stable isotope labeling with amino acids in cell culture
    • doi:10.1038/nprot.2008.2
    • Harsha, H.C., H. Molina, and A. Pandey. 2008. Quantitative proteomics using stable isotope labeling with amino acids in cell culture. Nat. Protoc. 3:505-516. doi:10.1038/nprot.2008.2
    • (2008) Nat. Protoc , vol.3 , pp. 505-516
    • Harsha, H.C.1    Molina, H.2    Pandey, A.3
  • 20
    • 48549103375 scopus 로고    scopus 로고
    • WHAMMing into the Golgi
    • doi:10.1016/j.devcel.2008.07.011
    • Hayes, G.L., and S.R. Pfeffer. 2008. WHAMMing into the Golgi. Dev. Cell. 15:171-172. doi:10.1016/j.devcel.2008.07.011
    • (2008) Dev. Cell , vol.15 , pp. 171-172
    • Hayes, G.L.1    Pfeffer, S.R.2
  • 21
    • 12844269159 scopus 로고    scopus 로고
    • Actindepolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells
    • doi:10.1091/mbc.E04-07-0555
    • Hotulainen, P., E. Paunola, M.K. Vartiainen, and P. Lappalainen. 2005. Actindepolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells. Mol. Biol. Cell. 16:649-664. doi:10.1091/mbc.E04-07-0555
    • (2005) Mol. Biol. Cell , vol.16 , pp. 649-664
    • Hotulainen, P.1    Paunola, E.2    Vartiainen, M.K.3    Lappalainen, P.4
  • 22
    • 66149154285 scopus 로고    scopus 로고
    • The effects of ADF/cofilin and profilin on the conformation of the ATP-binding cleft of monomeric actin
    • doi:10.1016/j.bpj.2008.12.3906
    • Kardos, R., K. Pozsonyi, E. Nevalainen, P. Lappalainen, M. Nyitrai, and G. Hild. 2009. The effects of ADF/cofilin and profilin on the conformation of the ATP-binding cleft of monomeric actin. Biophys. J. 96:2335-2343. doi:10.1016/j.bpj.2008.12.3906
    • (2009) Biophys. J , vol.96 , pp. 2335-2343
    • Kardos, R.1    Pozsonyi, K.2    Nevalainen, E.3    Lappalainen, P.4    Nyitrai, M.5    Hild, G.6
  • 23
    • 0024441817 scopus 로고
    • The biogenesis of lysosomes
    • doi:10.1146/annurev.cb.05.110189.002411
    • Kornfeld, S., and I. Mellman. 1989. The biogenesis of lysosomes. Annu. Rev. Cell Biol. 5:483-525. doi:10.1146/annurev.cb.05.110189.002411
    • (1989) Annu. Rev. Cell Biol , vol.5 , pp. 483-525
    • Kornfeld, S.1    Mellman, I.2
  • 24
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • doi:10.1038/8977
    • Kroschewski, R., A. Hall, and I. Mellman. 1999. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat. Cell Biol. 1:8-13. doi:10.1038/8977
    • (1999) Nat. Cell Biol , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 25
    • 48249121534 scopus 로고    scopus 로고
    • Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbedend cappers
    • doi:10.1083/jcb.200801027
    • Kueh, H.Y., G.T. Charras, T.J. Mitchison, and W.M. Brieher. 2008. Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbedend cappers. J. Cell Biol. 182:341-353. doi:10.1083/jcb.200801027
    • (2008) J. Cell Biol , vol.182 , pp. 341-353
    • Kueh, H.Y.1    Charras, G.T.2    Mitchison, T.J.3    Brieher, W.M.4
  • 26
    • 34547125988 scopus 로고    scopus 로고
    • Variable actin dynamics requirement for the exit of different cargo from the trans-Golgi network
    • doi:10.1016/j.febslet.2007.07.015
    • Lázaro-Diéguez, F., C. Colonna, M. Cortegano, M. Calvo, S.E. Martínez, and G. Egea. 2007. Variable actin dynamics requirement for the exit of different cargo from the trans-Golgi network. FEBS Lett. 581:3875-3881. doi:10.1016/j.febslet.2007.07.015
    • (2007) FEBS Lett , vol.581 , pp. 3875-3881
    • Lázaro-Diéguez, F.1    Colonna, C.2    Cortegano, M.3    Calvo, M.4    Martínez, S.E.5    Egea, G.6
  • 27
    • 8444242974 scopus 로고    scopus 로고
    • Bi-directional protein transport between the ER and Golgi
    • doi:10.1146/annurev.cellbio.20.010403.105307
    • Lee, M.C., E.A. Miller, J. Goldberg, L. Orci, and R. Schekman. 2004. Bi-directional protein transport between the ER and Golgi. Annu. Rev. Cell Dev. Biol. 20:87-123. doi:10.1146/annurev.cellbio.20.010403.105307
    • (2004) Annu. Rev. Cell Dev. Biol , vol.20 , pp. 87-123
    • Lee, M.C.1    Miller, E.A.2    Goldberg, J.3    Orci, L.4    Schekman, R.5
  • 28
    • 66949156095 scopus 로고    scopus 로고
    • Apical secretion in epithelial tubes of the Drosophila embryo is directed by the Formin-family protein Diaphanous
    • doi:10.1016/j.devcel.2009.04.010
    • Massarwa, R., E.D. Schejter, and B.Z. Shilo. 2009. Apical secretion in epithelial tubes of the Drosophila embryo is directed by the Formin-family protein Diaphanous. Dev. Cell. 16:877-888. doi:10.1016/j.devcel.2009.04.010
    • (2009) Dev. Cell , vol.16 , pp. 877-888
    • Massarwa, R.1    Schejter, E.D.2    Shilo, B.Z.3
  • 29
    • 33745341846 scopus 로고    scopus 로고
    • Live imaging of yeast Golgi cisternal maturation
    • doi:10.1038/nature04737
    • Matsuura-Tokita, K., M. Takeuchi, A. Ichihara, K. Mikuriya, and A. Nakano. 2006. Live imaging of yeast Golgi cisternal maturation. Nature. 441:1007-1010. doi:10.1038/nature04737
    • (2006) Nature , vol.441 , pp. 1007-1010
    • Matsuura-Tokita, K.1    Takeuchi, M.2    Ichihara, A.3    Mikuriya, K.4    Nakano, A.5
  • 30
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • doi:10.1016/S0092- 8674(00)81687-6
    • Mellman, I., and G. Warren. 2000. The road taken: past and future foundations of membrane traffic. Cell. 100:99-112. doi:10.1016/S0092- 8674(00)81687-6
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 31
    • 0037076273 scopus 로고    scopus 로고
    • The delta subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface
    • doi:10.1073/pnas.092150699
    • Nishimura, N., H. Plutner, K. Hahn, and W.E. Balch. 2002. The delta subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface. Proc. Natl. Acad. Sci. USA. 99:6755-6760. doi:10.1073/pnas.092150699
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6755-6760
    • Nishimura, N.1    Plutner, H.2    Hahn, K.3    Balch, W.E.4
  • 32
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • doi:10.1016/S0092- 8674(01)00638-9
    • Niwa, R., K. Nagata-Ohashi, M. Takeichi, K. Mizuno, and T. Uemura. 2002. Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell. 108:233-246. doi:10.1016/S0092- 8674(01)00638-9
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 33
    • 0034610013 scopus 로고    scopus 로고
    • A Drosophila homolog of LIM-kinase phosphorylates cofilin and induces actin cytoskeletal reorganization
    • doi:10.1006/bbrc.2000.3599
    • Ohashi, K., T. Hosoya, K. Takahashi, H. Hing, and K. Mizuno. 2000. A Drosophila homolog of LIM-kinase phosphorylates cofilin and induces actin cytoskeletal reorganization. Biochem. Biophys. Res. Commun. 276:1178-1185. doi:10.1006/bbrc.2000.3599
    • (2000) Biochem. Biophys. Res. Commun , vol.276 , pp. 1178-1185
    • Ohashi, K.1    Hosoya, T.2    Takahashi, K.3    Hing, H.4    Mizuno, K.5
  • 34
    • 34748872096 scopus 로고    scopus 로고
    • Cofilin recruitment and function during actin-mediated endocytosis dictated by actin nucleotide state
    • doi:10.1083/jcb.200703092
    • Okreglak, V., and D.G. Drubin. 2007. Cofilin recruitment and function during actin-mediated endocytosis dictated by actin nucleotide state. J. Cell Biol. 178:1251-1264. doi:10.1083/jcb.200703092
    • (2007) J. Cell Biol , vol.178 , pp. 1251-1264
    • Okreglak, V.1    Drubin, D.G.2
  • 35
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • doi:10.1038/nprot.2006.427
    • Ong, S.E., and M. Mann. 2006. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat. Protoc. 1:2650-2660. doi:10.1038/nprot.2006.427
    • (2006) Nat. Protoc , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 36
    • 44849128559 scopus 로고    scopus 로고
    • Transport through the Golgi apparatus by rapid partitioning within a two-phase membrane system
    • doi:10.1016/j.cell.2008.04.044
    • Patterson, G.H., K. Hirschberg, R.S. Polishchuk, D. Gerlich, R.D. Phair, and J. Lippincott-Schwartz. 2008. Transport through the Golgi apparatus by rapid partitioning within a two-phase membrane system. Cell. 133:1055-1067. doi:10.1016/j.cell.2008.04.044
    • (2008) Cell , vol.133 , pp. 1055-1067
    • Patterson, G.H.1    Hirschberg, K.2    Polishchuk, R.S.3    Gerlich, D.4    Phair, R.D.5    Lippincott-Schwartz, J.6
  • 37
    • 0034627793 scopus 로고    scopus 로고
    • Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane
    • doi:10.1083/jcb.148.1.45
    • Polishchuk, R.S., E.V. Polishchuk, P. Marra, S. Alberti, R. Buccione, A. Luini, and A.A. Mironov. 2000. Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane. J. Cell Biol. 148:45-58. doi:10.1083/jcb.148.1.45
    • (2000) J. Cell Biol , vol.148 , pp. 45-58
    • Polishchuk, R.S.1    Polishchuk, E.V.2    Marra, P.3    Alberti, S.4    Buccione, R.5    Luini, A.6    Mironov, A.A.7
  • 38
    • 3042808106 scopus 로고    scopus 로고
    • LIMK1 regulates Golgi dynamics, traffic of Golgi-derived vesicles, and process extension in primary cultured neurons
    • doi:10.1091/mbc.E03-05- 0328
    • Rosso, S., F. Bollati, M. Bisbal, D. Peretti, T. Sumi, T. Nakamura, S. Quiroga, A. Ferreira, and A. Cáceres. 2004. LIMK1 regulates Golgi dynamics, traffic of Golgi-derived vesicles, and process extension in primary cultured neurons. Mol. Biol. Cell. 15:3433-3449. doi:10.1091/mbc.E03-05- 0328
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3433-3449
    • Rosso, S.1    Bollati, F.2    Bisbal, M.3    Peretti, D.4    Sumi, T.5    Nakamura, T.6    Quiroga, S.7    Ferreira, A.8    Cáceres, A.9
  • 39
    • 61449242669 scopus 로고    scopus 로고
    • TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites
    • doi:10.1016/j.cell. 2008.12.025
    • Saito, K., M. Chen, F. Bard, S. Chen, H. Zhou, D. Woodley, R. Polischuk, R. Schekman, and V. Malhotra. 2009. TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites. Cell. 136:891-902. doi:10.1016/j.cell. 2008.12.025
    • (2009) Cell , vol.136 , pp. 891-902
    • Saito, K.1    Chen, M.2    Bard, F.3    Chen, S.4    Zhou, H.5    Woodley, D.6    Polischuk, R.7    Schekman, R.8    Malhotra, V.9
  • 40
    • 63049103127 scopus 로고    scopus 로고
    • LIM kinase 1 and cofilin regulate actin filament population required for dynamindependent apical carrier fission from the trans-Golgi network
    • doi:10.1091/mbc.E08-08-0891
    • Salvarezza, S.B., S. Deborde, R. Schreiner, F. Campagne, M.M. Kessels, B. Qualmann, A. Caceres, G. Kreitzer, and E. Rodriguez-Boulan. 2009. LIM kinase 1 and cofilin regulate actin filament population required for dynamindependent apical carrier fission from the trans-Golgi network. Mol. Biol. Cell. 20:438-451. doi:10.1091/mbc.E08-08-0891
    • (2009) Mol. Biol. Cell , vol.20 , pp. 438-451
    • Salvarezza, S.B.1    Deborde, S.2    Schreiner, R.3    Campagne, F.4    Kessels, M.M.5    Qualmann, B.6    Caceres, A.7    Kreitzer, G.8    Rodriguez-Boulan, E.9
  • 41
  • 42
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • doi:10.1038/nprot.2006.468
    • Shevchenko, A., H. Tomas, J. Havlis, J.V. Olsen, and M. Mann. 2006. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1:2856-2860. doi:10.1038/nprot.2006.468
    • (2006) Nat. Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 43
    • 0036702196 scopus 로고    scopus 로고
    • Regulating the actin cytoskeleton during vesicular transport
    • doi:10.1016/S0955-0674(02) 00349-6
    • Stamnes, M. 2002. Regulating the actin cytoskeleton during vesicular transport. Curr. Opin. Cell Biol. 14:428-433. doi:10.1016/S0955-0674(02) 00349-6
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 428-433
    • Stamnes, M.1
  • 44
    • 0033611107 scopus 로고    scopus 로고
    • Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho- and Cdc42-activated LIM-kinase 2
    • doi:10.1083/jcb.147.7.1519
    • Sumi, T., K. Matsumoto, Y. Takai, and T. Nakamura. 1999. Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho- and Cdc42-activated LIM-kinase 2. J. Cell Biol. 147:1519-1532. doi:10.1083/jcb.147.7.1519
    • (1999) J. Cell Biol , vol.147 , pp. 1519-1532
    • Sumi, T.1    Matsumoto, K.2    Takai, Y.3    Nakamura, T.4
  • 45
    • 33745535568 scopus 로고    scopus 로고
    • Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity
    • doi:10.1016/j.devcel.2006.05.008
    • Sun, Y., A.C. Martin, and D.G. Drubin. 2006. Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity. Dev. Cell. 11:33-46. doi:10.1016/j.devcel.2006.05.008
    • (2006) Dev. Cell , vol.11 , pp. 33-46
    • Sun, Y.1    Martin, A.C.2    Drubin, D.G.3
  • 46
    • 33749011468 scopus 로고    scopus 로고
    • Exomer: A coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast
    • doi:10.1083/jcb.200605106
    • Wang, C.W., S. Hamamoto, L. Orci, and R. Schekman. 2006. Exomer: a coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast. J. Cell Biol. 174:973-983. doi:10.1083/jcb.200605106
    • (2006) J. Cell Biol , vol.174 , pp. 973-983
    • Wang, C.W.1    Hamamoto, S.2    Orci, L.3    Schekman, R.4


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