메뉴 건너뛰기




Volumn 14, Issue 3, 2012, Pages 304-310

Flippase-mediated phospholipid asymmetry promotes fast Cdc42 recycling in dynamic maintenance of cell polarity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CELL CYCLE PROTEIN; DNF1 PROTEIN; DNF2 PROTEIN; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; LEM3 PROTEIN; LIPID FLIPPASE COMPLEX; MULTIPROTEIN COMPLEX; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLSERINE; PHOSPHOLIPID; PROTEIN CDC42; UNCLASSIFIED DRUG;

EID: 84863419997     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb2444     Document Type: Article
Times cited : (87)

References (40)
  • 1
    • 5644241027 scopus 로고    scopus 로고
    • Local exposure of phosphatidylethanolamine on the yeast plasma membrane is implicated in cell polarity
    • DOI 10.1111/j.1365-2443.2004.00782.x
    • Iwamoto, K. et al. Local exposure of phosphatidylethanolamine on the yeast plasma membrane is implicated in cell polarity. Genes Cells 9, 891-903 (2004). (Pubitemid 39369022)
    • (2004) Genes to Cells , vol.9 , Issue.10 , pp. 891-903
    • Iwamoto, K.1    Kobayashi, S.2    Fukuda, R.3    Umeda, M.4    Kobayashi, T.5    Ohta, A.6
  • 2
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates su-rface charge and protein localization
    • Yeung, T. et al. Membrane phosphatidylserine regulates su-rface charge and protein localization. Science 319, 210-213 (2008).
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1
  • 3
    • 0034640856 scopus 로고    scopus 로고
    • An essential role for a membrane lipid in cytokinesis: Regulation of contractile ring disassembly by redistribution of phosphatidylethanolamine
    • DOI 10.1083/jcb.149.6.1215
    • Emoto, K. & Umeda, M. An essential role for a membrane lipid in cytokinesis. Regulation of contractile ring disassembly by redistribution of phosphatidylethanolamine. J. Cell Biol. 149, 1215-1224 (2000). (Pubitemid 30399675)
    • (2000) Journal of Cell Biology , vol.149 , Issue.6 , pp. 1215-1224
    • Emoto, K.1    Umeda, M.2
  • 4
    • 33846097207 scopus 로고    scopus 로고
    • Lipid flippases and their biological functions
    • DOI 10.1007/s00018-006-6167-7
    • Pomorski, T. & Menon, A. K. Lipid flippases and their biological functions. Cell Mol. Life Sci. 63, 2908-2921 (2006). (Pubitemid 46072298)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.24 , pp. 2908-2921
    • Pomorski, T.1    Menon, A.K.2
  • 5
    • 2342432240 scopus 로고    scopus 로고
    • Cdc42-the centre of polarity
    • Etienne-Manneville, S. Cdc42-the centre of polarity. J. Cell Sci. 117, 1291-1300 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 1291-1300
    • Etienne-Manneville, S.1
  • 7
    • 4544295912 scopus 로고    scopus 로고
    • Robust cell polarity is a dynamic state established by coupling transport and GTPase signaling
    • DOI 10.1083/jcb.200405061
    • Wedlich-Soldner, R., Wai, S. C., Schmidt, T. & Li, R. Robust cell polarity is a dynamic state established by coupling transport and GTPase signaling. J. Cell Biol. 166, 889-900 (2004). (Pubitemid 39249839)
    • (2004) Journal of Cell Biology , vol.166 , Issue.6 , pp. 889-900
    • Wedlich-Soldner, R.1    Wai, S.C.2    Schmidt, T.3    Li, R.4
  • 8
    • 34147175165 scopus 로고    scopus 로고
    • Endocytosis Optimizes the Dynamic Localization of Membrane Proteins that Regulate Cortical Polarity
    • DOI 10.1016/j.cell.2007.02.043, PII S0092867407003522
    • Marco, E., Wedlich-Soldner, R., Li, R., Altschuler, S. J. & Wu, L. F. Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity. Cell 129, 411-422 (2007). (Pubitemid 46574971)
    • (2007) Cell , vol.129 , Issue.2 , pp. 411-422
    • Marco, E.1    Wedlich-Soldner, R.2    Li, R.3    Altschuler, S.J.4    Wu, L.F.5
  • 9
    • 71649099053 scopus 로고    scopus 로고
    • Dual modes of Cdc42 recyclingfine-tune polarized morphogenesis
    • Slaughter, B. D., Das, A., Schwartz, J. W., Rubinstein, B. & Li, R. Dual modes of Cdc42 recyclingfine-tune polarized morphogenesis. Dev. Cell 17, 823-835 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 823-835
    • Slaughter, B.D.1    Das, A.2    Schwartz, J.W.3    Rubinstein, B.4    Li, R.5
  • 11
    • 21744432683 scopus 로고    scopus 로고
    • GDIs: Central regulatory molecules in Rho GTPase activation
    • DOI 10.1016/j.tcb.2005.05.001, PII S0962892405001273
    • DerMardirossian, C. & Bokoch, G. M. GDIs: central regulatory molecules in Rho GTPase activation. Trends Cell Biol. 15, 356-363 (2005). (Pubitemid 40943524)
    • (2005) Trends in Cell Biology , vol.15 , Issue.7 , pp. 356-363
    • DerMardirossian, C.1    Bokoch, G.M.2
  • 12
    • 69949132404 scopus 로고    scopus 로고
    • New insights into how the Rho guanine nucleotide dissociation inhibitor regulates the interaction of Cdc42 with membranes
    • Johnson, J. L., Erickson, J. W. & Cerione, R. A. New insights into how the Rho guanine nucleotide dissociation inhibitor regulates the interaction of Cdc42 with membranes. J. Biol. Chem. 284, 23860-23871 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 23860-23871
    • Johnson, J.L.1    Erickson, J.W.2    Cerione, R.A.3
  • 13
    • 3042812985 scopus 로고    scopus 로고
    • Analysis of cell-cycle specific localization of the Rdi1p RhoGDI and the structural determinants required for Cdc42p membrane localization and clustering at sites of polarized growth
    • DOI 10.1007/s00294-004-0505-9
    • Richman, T. J. et al. Analysis of cell-cycle specific localization of the Rdi1p RhoGDI and the structural determinants required for Cdc42p membrane localization and clustering at sites of polarized growth. Curr. Genet. 45, 339-349 (2004). (Pubitemid 38878480)
    • (2004) Current Genetics , vol.45 , Issue.6 , pp. 339-349
    • Richman, T.J.1    Toenjes, K.A.2    Morales, S.E.3    Cole, K.C.4    Wasserman, B.T.5    Taylor, C.M.6    Koster, J.A.7    Whelihan, M.F.8    Johnson, D.I.9
  • 15
    • 0037345029 scopus 로고    scopus 로고
    • Drs2p-related P-type ATPases Dnflp and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis
    • DOI 10.1091/mbc.E02-08-0501
    • Pomorski, T. et al. Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis. Mol. Biol. Cell. 14, 1240-1254 (2003). (Pubitemid 36337466)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.3 , pp. 1240-1254
    • Pomorski, T.1    Lombardi, R.2    Riezman, H.3    Devaux, P.F.4    Van Meer, G.5    Holthuis, J.C.M.6
  • 16
    • 0037020182 scopus 로고    scopus 로고
    • A novel membrane protein, Ros3p, is required for phospholipid translocation across the plasma membrane in Saccharomyces cerevisiae
    • Kato, U. et al. A novel membrane protein, Ros3p, is required for phospholipid translocation across the plasma membrane in Saccharomyces cerevisiae. J. Biol. Chem. 277, 37855-37862 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 37855-37862
    • Kato, U.1
  • 17
    • 35548947966 scopus 로고    scopus 로고
    • Transbilayer Phospholipid Flipping Regulates Cdc42p Signaling during Polarized Cell Growth via Rga GTPase-Activating Proteins
    • DOI 10.1016/j.devcel.2007.09.014, PII S1534580707003553
    • Saito, K. et al. Transbilayer phospholipidfiipping regulates Cdc42p signaling during polarized cell growth via Rga GTPase-activating proteins. Dev. Cell 13, 743-751 (2007). (Pubitemid 350011986)
    • (2007) Developmental Cell , vol.13 , Issue.5 , pp. 743-751
    • Saito, K.1    Fujimura-Kamada, K.2    Hanamatsu, H.3    Kato, U.4    Umeda, M.5    Kozminski, K.G.6    Tanaka, K.7
  • 18
    • 78650481678 scopus 로고    scopus 로고
    • Toward quantitative ̀in vivo biochemistry' withfluorescence fluctuation spectroscopy
    • Slaughter, B. D. & Li, R. Toward quantitative ̀in vivo biochemistry' withfluorescence fluctuation spectroscopy. Mol. Biol. Cell 21, 4306-4311 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4306-4311
    • Slaughter, B.D.1    Li, R.2
  • 19
    • 0035887166 scopus 로고    scopus 로고
    • RhoGDI-binding-defective mutant of Cdc42Hs targets to membranes and activates filopodia formation but does not cycle with the cytosol of mammalian cells
    • DOI 10.1042/0264-6021:3590285
    • Gibson, R. M. & Wilson-Delfosse, A. L. RhoGDI-binding-defective mutant of Cdc42Hs targets to membranes and activates fllopodia formation but does not cycle with the cytosol of mammalian cells. Biochem. J. 359, 285-294 (2001). (Pubitemid 32999772)
    • (2001) Biochemical Journal , vol.359 , Issue.2 , pp. 285-294
    • Gibson, R.M.1    Wilson-Delfosse, A.L.2
  • 20
    • 58249087906 scopus 로고    scopus 로고
    • Plasma membrane microdomains regulate turnover of transport proteins in yeast
    • Grossmann, G. et al. Plasma membrane microdomains regulate turnover of transport proteins in yeast. J. Cell Biol. 183, 1075-1088 (2008).
    • (2008) J. Cell Biol. , vol.183 , pp. 1075-1088
    • Grossmann, G.1
  • 21
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • DOI 10.1083/jcb.137.2.399
    • Ayscough, K. R. et al. High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J. Cell Biol. 137, 399-416 (1997). (Pubitemid 27181293)
    • (1997) Journal of Cell Biology , vol.137 , Issue.2 , pp. 399-416
    • Ayscough, K.R.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.G.6
  • 22
    • 0028101276 scopus 로고
    • A novel peptide probe for studying the transbilayer movement of phosphatidylethanolamine
    • Aoki, Y., Uenaka, T., Aoki, J., Umeda, M. & Inoue, K. A novel peptide probe for studying the transbilayer movement of phosphatidylethanolamine. J. Biochem. 116, 291-297 (1994). (Pubitemid 24265600)
    • (1994) Journal of Biochemistry , vol.116 , Issue.2 , pp. 291-297
    • Aoki, Y.1    Uenaka, T.2    Aoki, J.3    Umeda, M.4    Inoue, K.5
  • 23
    • 58049203860 scopus 로고    scopus 로고
    • The putative aminophospholipid translocases, DNF1 and DNF2, are not required for 7-nitrobenz-2-oxa-1,3-diazol-4-yl-phosphatidylserine flip across the plasma membrane of Saccharomyces cerevisiae
    • Stevens, H. C., Malone, L. & Nichols, J. W. The putative aminophospholipid translocases, DNF1 and DNF2, are not required for 7-nitrobenz-2-oxa-1,3-diazol-4-yl-phosphatidylserine flip across the plasma membrane of Saccharomyces cerevisiae. J. Biol. Chem. 283, 35060-35069 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 35060-35069
    • Stevens, H.C.1    Malone, L.2    Nichols, J.W.3
  • 24
    • 0036181710 scopus 로고    scopus 로고
    • The yeast synaptojanin-like proteins control the cellular distribution of phosphatidylinositol (4,5)-bisphosphate
    • DOI 10.1091/mbc.01-10-0476
    • Stefan, C. J., Audhya, A. & Emr, S. D. The yeast synaptojanin-like proteins control the cellular distribution of phosphatidylinositol (4,5)-bisphosphate. Mol. Biol. Cell 13, 542-557 (2002). (Pubitemid 34165082)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.2 , pp. 542-557
    • Stefan, C.J.1    Audhya, A.2    Emr, S.D.3
  • 25
    • 0037081858 scopus 로고    scopus 로고
    • Phosphorylation states of Cdc42 and RhoA regulate their interactions with Rho GDP dissociation inhibitor and their extraction from biological membranes
    • DOI 10.1042/0264-6021:3610243
    • Forget, M. A., Desrosiers, R. R., Gingras, D. & Beliveau, R. Phosphorylation states of Cdc42 and RhoA regulate their interactions with Rho GDP dissociation inhibitor and their extraction from biological membranes. Biochem. J. 361, 243-254 (2002). (Pubitemid 34174491)
    • (2002) Biochemical Journal , vol.361 , Issue.2 , pp. 243-254
    • Forget, M.-A.1    Desrosiers, R.R.2    Gingras, D.3    Beliveau, R.4
  • 26
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • DOI 10.1126/science.281.5374.269
    • Griffin, B. A., Adams, S. R. & Tsien, R. Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281, 269-272 (1998). (Pubitemid 28334512)
    • (1998) Science , vol.281 , Issue.5374 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 27
    • 84856137855 scopus 로고    scopus 로고
    • Phosphatidylserine is polarized and required for proper Cdc42 localization and for development of cell polarity
    • Fairn, G. D., Hermansson, M., Somerharju, P. & Grinstein, S. Phosphatidylserine is polarized and required for proper Cdc42 localization and for development of cell polarity. Nat. Cell Biol. 13, 1424-1430 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1424-1430
    • Fairn, G.D.1    Hermansson, M.2    Somerharju, P.3    Grinstein, S.4
  • 28
    • 0141541745 scopus 로고    scopus 로고
    • The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast
    • DOI 10.1091/mbc.E03-04-0247
    • Caviston, J. P., Longtine, M., Pringle, J. R. & Bi, E. The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast. Mol. Biol. Cell 14, 4051-4066 (2003). (Pubitemid 37186308)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.10 , pp. 4051-4066
    • Caviston, J.P.1    Longtine, M.2    Pringle, J.R.3    Bi, E.4
  • 29
    • 38049181017 scopus 로고    scopus 로고
    • Mapping dynamic protein interactions in MAP kinase signaling using live-cellfluorescence fluctuation spectroscopy and imaging
    • Slaughter, B. D., Schwartz, J. W. & Li, R. Mapping dynamic protein interactions in MAP kinase signaling using live-cellfluorescence fluctuation spectroscopy and imaging. Proc. Natl Acad. Sci. USA 104, 20320-20325 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 20320-20325
    • Slaughter, B.D.1    Schwartz, J.W.2    Li, R.3
  • 30
    • 35748946937 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in living cells
    • DOI 10.1038/nmeth1104, PII NMETH1104
    • Kim, S. A., Heinze, K. G. & Schwille, P. Fluorescence correlation spectroscopy in living cells. Nat. Methods 4, 963-973 (2007). (Pubitemid 350042387)
    • (2007) Nature Methods , vol.4 , Issue.11 , pp. 963-973
    • Kim, S.A.1    Heinze, K.G.2    Schwille, P.3
  • 35
    • 0012081578 scopus 로고
    • Mercury-plated rotating ring-disk electrode
    • Daly, P. J., Page, D. J. & Compton, R. G. Mercury-plated rotating ring-disk electrode. Anal. Chem. 55, 1191-1192 (1983).
    • (1983) Anal. Chem. , vol.55 , pp. 1191-1192
    • Daly, P.J.1    Page, D.J.2    Compton, R.G.3
  • 36
    • 0036789423 scopus 로고    scopus 로고
    • Focal volume optics and experimental artifacts in confocalfluorescence correlation spectroscopy
    • Hess, S. T. & Webb, W. W. Focal volume optics and experimental artifacts in confocalfluorescence correlation spectroscopy. Biophys. J. 83, 2300-2317 (2002).
    • (2002) Biophys. J. , vol.83 , pp. 2300-2317
    • Hess, S.T.1    Webb, W.W.2
  • 37
    • 27144448780 scopus 로고    scopus 로고
    • Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity
    • DOI 10.1038/nbt1136, PII N1136
    • Martin, B. R., Giepmans, B. N., Adams, S. R. & Tsien, R. Y. Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improvedfluorescence and affinity. Nat. Biotechnol. 23, 1308-1314 (2005). (Pubitemid 41486860)
    • (2005) Nature Biotechnology , vol.23 , Issue.10 , pp. 1308-1314
    • Martin, B.R.1    Giepmans, B.N.G.2    Adams, S.R.3    Tsien, R.Y.4
  • 38
    • 0024276923 scopus 로고
    • A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast
    • Goud, B., Salminen, A., Walworth, N. C. & Novick, P. J. A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast. Cell 53, 753-768 (1988).
    • (1988) Cell , vol.53 , pp. 753-768
    • Goud, B.1    Salminen, A.2    Walworth, N.C.3    Novick, P.J.4
  • 39
    • 77956537388 scopus 로고    scopus 로고
    • Self-assembly of fllopodia-like structures on supported lipid bilayers
    • Lee, K., Gallop, J. L., Rambani, K. & Kirschner, M. W. Self-assembly of fllopodia-like structures on supported lipid bilayers. Science 329, 1341-1345 (2010).
    • (2010) Science , vol.329 , pp. 1341-1345
    • Lee, K.1    Gallop, J.L.2    Rambani, K.3    Kirschner, M.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.