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Volumn 87, Issue 2, 2008, Pages 57-68

Competition between targeting signals in hybrid proteins provides information on their relative in vivo affinities for subcellular compartments

Author keywords

Actin; Cytoskeleton; Dictyostelium; Endosome; Flotillin; Lysosome; Nucleus; Peroxisome; Reggie; Signal sequence

Indexed keywords

ACTIN BINDING PROTEIN; ACTIN BINDING PROTEIN 34; AIP1 PROTEIN; CELL PROTEIN; COFILIN; CYTOSKELETON PROTEIN; HYBRID PROTEIN; KHELLIN; TRIPEPTIDE; UNCLASSIFIED DRUG; VACUOLIN;

EID: 38149009618     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2007.10.003     Document Type: Article
Times cited : (4)

References (57)
  • 1
    • 84939297014 scopus 로고    scopus 로고
    • Abelson, J.N., Simon, M.I., Conn, P.M. (Eds.), 1999. Green fluorescent protein. Methods Enzymol. 302.
  • 2
    • 0001081894 scopus 로고    scopus 로고
    • Live dynamics of Dictyostelium cofilin suggests a role in remodelling actin latticework into bundles
    • Aizawa H., Fukui Y., and Yahara I. Live dynamics of Dictyostelium cofilin suggests a role in remodelling actin latticework into bundles. J. Cell Sci. 110 (1997) 2333-2344
    • (1997) J. Cell Sci. , vol.110 , pp. 2333-2344
    • Aizawa, H.1    Fukui, Y.2    Yahara, I.3
  • 3
    • 0032803529 scopus 로고    scopus 로고
    • Hyperosmotic stress-induced reorganization of actin bundles in Dictyostelium cells over-expressing cofilin
    • Aizawa H., Katadae M., Maruya M., Sameshima M., Murakami-Murofushi K., and Yahara I. Hyperosmotic stress-induced reorganization of actin bundles in Dictyostelium cells over-expressing cofilin. Genes Cells 4 (1999) 311-324
    • (1999) Genes Cells , vol.4 , pp. 311-324
    • Aizawa, H.1    Katadae, M.2    Maruya, M.3    Sameshima, M.4    Murakami-Murofushi, K.5    Yahara, I.6
  • 4
    • 0028928199 scopus 로고
    • Defining protein interactions with yeast actin in vivo
    • Amberg D.C., Basart E., and Botstein D. Defining protein interactions with yeast actin in vivo. Nat. Struct. Biol. 2 (1995) 28-35
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 28-35
    • Amberg, D.C.1    Basart, E.2    Botstein, D.3
  • 5
    • 0033570145 scopus 로고    scopus 로고
    • Dual targeting of cytochrome P4502B1 to endoplasmic reticulum and mitochondria involves a novel signal activation by cyclic AMP-dependent phosphorylation at ser128
    • Anandatheerthavarada H.K., Biswas G., Mullick J., Sepuri N.B., Otvos L., Pain D., and Avadhani N.G. Dual targeting of cytochrome P4502B1 to endoplasmic reticulum and mitochondria involves a novel signal activation by cyclic AMP-dependent phosphorylation at ser128. EMBO J. 18 (1999) 5494-5504
    • (1999) EMBO J. , vol.18 , pp. 5494-5504
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Mullick, J.3    Sepuri, N.B.4    Otvos, L.5    Pain, D.6    Avadhani, N.G.7
  • 6
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility
    • Carlier M.F., Laurent V., Santolini J., Melki R., Didry D., Xia G.X., Hong Y., Chua N.H., and Pantaloni D. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136 (1997) 1307-1322
    • (1997) J. Cell Biol. , vol.136 , pp. 1307-1322
    • Carlier, M.F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.X.6    Hong, Y.7    Chua, N.H.8    Pantaloni, D.9
  • 7
    • 0013410174 scopus 로고    scopus 로고
    • Dalbey R.E., and von Heijne G. (Eds), Academic Press, Elsevier, London
    • In: Dalbey R.E., and von Heijne G. (Eds). Protein Targeting, Transport, and Translocation (2002), Academic Press, Elsevier, London
    • (2002) Protein Targeting, Transport, and Translocation
  • 8
    • 0029015912 scopus 로고
    • How can the products of a single gene be localized to more than one intracellular compartment?
    • Danpure C.J. How can the products of a single gene be localized to more than one intracellular compartment?. Trends Cell Biol. 5 (1995) 230-238
    • (1995) Trends Cell Biol. , vol.5 , pp. 230-238
    • Danpure, C.J.1
  • 9
    • 0026041203 scopus 로고
    • Coronin, an actin binding protein of Dictyostelium discoideum localized to cell surface projections, has sequence similarities to G protein β subunits
    • de Hostos E.L., Bradtke B., Lottspeich F., Guggenheim R., and Gerisch G. Coronin, an actin binding protein of Dictyostelium discoideum localized to cell surface projections, has sequence similarities to G protein β subunits. EMBO J. 10 (1991) 4097-4104
    • (1991) EMBO J. , vol.10 , pp. 4097-4104
    • de Hostos, E.L.1    Bradtke, B.2    Lottspeich, F.3    Guggenheim, R.4    Gerisch, G.5
  • 10
    • 0019877153 scopus 로고
    • Secretion of lysosomal enzymes in the cellular slime mold, Dictyostelium discoideum
    • Dimond R.L., Burns R.A., and Jordan K.B. Secretion of lysosomal enzymes in the cellular slime mold, Dictyostelium discoideum. J. Biol. Chem. 256 (1981) 6565-6572
    • (1981) J. Biol. Chem. , vol.256 , pp. 6565-6572
    • Dimond, R.L.1    Burns, R.A.2    Jordan, K.B.3
  • 11
    • 0142104342 scopus 로고    scopus 로고
    • A coat of filamentous actin prevents clustering of late-endosomal vacuoles in vivo
    • Drengk A., Fritsch J., Schmauch C., Rühling H., and Maniak M. A coat of filamentous actin prevents clustering of late-endosomal vacuoles in vivo. Curr. Biol. 13 (2003) 1814-1819
    • (2003) Curr. Biol. , vol.13 , pp. 1814-1819
    • Drengk, A.1    Fritsch, J.2    Schmauch, C.3    Rühling, H.4    Maniak, M.5
  • 12
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan G.I., Lewis G.K., Ramsay G., and Bishop J.M. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell Biol. 5 (1985) 3610-3616
    • (1985) Mol. Cell Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 13
    • 0023188266 scopus 로고
    • The Dictyostelium discoideum 30,000-Da protein is an actin filament-bundling protein that is selectively present in filopodia
    • Fechheimer M. The Dictyostelium discoideum 30,000-Da protein is an actin filament-bundling protein that is selectively present in filopodia. J. Cell Biol. 104 (1987) 1539-1551
    • (1987) J. Cell Biol. , vol.104 , pp. 1539-1551
    • Fechheimer, M.1
  • 14
    • 38149052902 scopus 로고    scopus 로고
    • Small actin cross-linking proteins
    • Kreis T., and Vale R. (Eds), Oxford University Press, Oxford, UK
    • Fechheimer M. Small actin cross-linking proteins. In: Kreis T., and Vale R. (Eds). Cytoskeletal and Motor Proteins (1999), Oxford University Press, Oxford, UK 132-135
    • (1999) Cytoskeletal and Motor Proteins , pp. 132-135
    • Fechheimer, M.1
  • 15
    • 0043020649 scopus 로고    scopus 로고
    • Mitochondrial membrane dynamics are altered in cluA-mutants of Dictyostelium
    • Fields S.D., Arana Q., Heuser J., and Clarke M. Mitochondrial membrane dynamics are altered in cluA-mutants of Dictyostelium. J. Muscle Res. Cell Motil. 23 (2002) 829-838
    • (2002) J. Muscle Res. Cell Motil. , vol.23 , pp. 829-838
    • Fields, S.D.1    Arana, Q.2    Heuser, J.3    Clarke, M.4
  • 16
    • 7544220540 scopus 로고    scopus 로고
    • A brilliant monomeric red fluorescent protein to visualize cytoskeleton dynamics in Dictyostelium
    • Fischer M., Haase I., Simmeth E., Gerisch G., and Müller-Taubenberger A. A brilliant monomeric red fluorescent protein to visualize cytoskeleton dynamics in Dictyostelium. FEBS Lett. 577 (2004) 227-232
    • (2004) FEBS Lett. , vol.577 , pp. 227-232
    • Fischer, M.1    Haase, I.2    Simmeth, E.3    Gerisch, G.4    Müller-Taubenberger, A.5
  • 17
    • 0031258948 scopus 로고    scopus 로고
    • Dynamics of GFP-coronin and eupodia in live Dictyostelium observed with real-time confocal optics
    • Fukui Y., de Hostos E.L., and Inoue S. Dynamics of GFP-coronin and eupodia in live Dictyostelium observed with real-time confocal optics. Biol. Bull. 193 (1997) 224-225
    • (1997) Biol. Bull. , vol.193 , pp. 224-225
    • Fukui, Y.1    de Hostos, E.L.2    Inoue, S.3
  • 19
    • 0037287050 scopus 로고    scopus 로고
    • GFP-fusion proteins as fluorescent reporters to study organelle and cytoskeleton dynamics in chemotaxis and phagocytosis
    • Gerisch G., and Müller-Taubenberger A. GFP-fusion proteins as fluorescent reporters to study organelle and cytoskeleton dynamics in chemotaxis and phagocytosis. Methods Enzymol. 361 (2003) 320-337
    • (2003) Methods Enzymol. , vol.361 , pp. 320-337
    • Gerisch, G.1    Müller-Taubenberger, A.2
  • 20
    • 0029411196 scopus 로고
    • Chemoattractant-controlled accumulation of coronin at the leading edge of Dictyostelium cells monitored using a green fluorescent protein-coronin fusion protein
    • Gerisch G., Albrecht R., Heizer C., Hodgkinson S., and Maniak M. Chemoattractant-controlled accumulation of coronin at the leading edge of Dictyostelium cells monitored using a green fluorescent protein-coronin fusion protein. Curr. Biol. 5 (1995) 1280-1285
    • (1995) Curr. Biol. , vol.5 , pp. 1280-1285
    • Gerisch, G.1    Albrecht, R.2    Heizer, C.3    Hodgkinson, S.4    Maniak, M.5
  • 21
    • 0028110118 scopus 로고
    • Saccharomyces cerevisiae peroxisomal thiolase is imported as a dimer
    • Glover J.R., Andrews D.W., and Rachubinski R.A. Saccharomyces cerevisiae peroxisomal thiolase is imported as a dimer. Proc. Natl. Acad. Sci. USA 91 (1994) 10541-10545
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10541-10545
    • Glover, J.R.1    Andrews, D.W.2    Rachubinski, R.A.3
  • 22
    • 0011888389 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Dalbey R.E., and von Heijne G. (Eds), Academic Press, Elsevier, London
    • Görlich D., and Jäkel S. Nucleocytoplasmic transport. In: Dalbey R.E., and von Heijne G. (Eds). Protein Targeting, Transport, and Translocation (2002), Academic Press, Elsevier, London 293-321
    • (2002) Protein Targeting, Transport, and Translocation , pp. 293-321
    • Görlich, D.1    Jäkel, S.2
  • 23
    • 0036799355 scopus 로고    scopus 로고
    • High-resolution dissection of phagosome maturation reveals distinct membrane trafficking phases
    • Gotthardt D., Warnatz H.J., Henschel O., Bruckert F., Schleicher M., and Soldati T. High-resolution dissection of phagosome maturation reveals distinct membrane trafficking phases. Mol. Biol. Cell 13 (2002) 3508-3520
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3508-3520
    • Gotthardt, D.1    Warnatz, H.J.2    Henschel, O.3    Bruckert, F.4    Schleicher, M.5    Soldati, T.6
  • 24
    • 0038059592 scopus 로고    scopus 로고
    • Protein sorting at the membrane of the endoplasmic reticulum
    • Dalbey R.E., and von Heijne G. (Eds), Academic Press, Elsevier, London
    • Haigh N.G., and Johnson A.E. Protein sorting at the membrane of the endoplasmic reticulum. In: Dalbey R.E., and von Heijne G. (Eds). Protein Targeting, Transport, and Translocation (2002), Academic Press, Elsevier, London 180-213
    • (2002) Protein Targeting, Transport, and Translocation , pp. 180-213
    • Haigh, N.G.1    Johnson, A.E.2
  • 26
    • 0026918335 scopus 로고
    • A preparation protocol for postembedding immunoelectron microscopy of Dictyostelium discoideum cells with monoclonal antibodies
    • Humbel B.M., and Biegelmann E. A preparation protocol for postembedding immunoelectron microscopy of Dictyostelium discoideum cells with monoclonal antibodies. Scanning Microsc. 6 (1992) 817-825
    • (1992) Scanning Microsc. , vol.6 , pp. 817-825
    • Humbel, B.M.1    Biegelmann, E.2
  • 27
    • 0029087151 scopus 로고
    • Purification of an ATP-dependent actin-binding protein from a lower eukaryote, Physarum polycephalum
    • Ishikawa R., Sasaki Y., Nakamura A., Takagi T., and Kohama K. Purification of an ATP-dependent actin-binding protein from a lower eukaryote, Physarum polycephalum. Biochem. Biophys. Res. Commun. 212 (1995) 347-352
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 347-352
    • Ishikawa, R.1    Sasaki, Y.2    Nakamura, A.3    Takagi, T.4    Kohama, K.5
  • 28
    • 0031985593 scopus 로고    scopus 로고
    • Targeted gene disruption reveals a role for vacuolin B in the late endocytic pathway and exocytosis
    • Jenne N., Rauchenberger R., Hacker U., Kast T., and Maniak M. Targeted gene disruption reveals a role for vacuolin B in the late endocytic pathway and exocytosis. J. Cell Sci. 111 (1998) 61-70
    • (1998) J. Cell Sci. , vol.111 , pp. 61-70
    • Jenne, N.1    Rauchenberger, R.2    Hacker, U.3    Kast, T.4    Maniak, M.5
  • 29
    • 0030008154 scopus 로고    scopus 로고
    • The initiation of basal disc formation in Dictyostelium discoideum is an early event in culmination
    • Jermyn K., Traynor D., and Williams J. The initiation of basal disc formation in Dictyostelium discoideum is an early event in culmination. Development 122 (1996) 753-760
    • (1996) Development , vol.122 , pp. 753-760
    • Jermyn, K.1    Traynor, D.2    Williams, J.3
  • 30
    • 20044387943 scopus 로고    scopus 로고
    • Single translation - dual destination: mechanisms of dual protein targeting in eukaryotes
    • Karniely S., and Pines O. Single translation - dual destination: mechanisms of dual protein targeting in eukaryotes. EMBO Rep. 6 (2005) 420-425
    • (2005) EMBO Rep. , vol.6 , pp. 420-425
    • Karniely, S.1    Pines, O.2
  • 31
    • 0033606768 scopus 로고    scopus 로고
    • DAip1, a Dictyostelium homologue of the yeast actin-interacting protein 1, is involved in endocytosis, cytokinesis and motility
    • Konzok A., Weber I., Simmeth E., Hacker U., Maniak M., and Müller-Taubenberger A. DAip1, a Dictyostelium homologue of the yeast actin-interacting protein 1, is involved in endocytosis, cytokinesis and motility. J. Cell Biol. 146 (1999) 453-464
    • (1999) J. Cell Biol. , vol.146 , pp. 453-464
    • Konzok, A.1    Weber, I.2    Simmeth, E.3    Hacker, U.4    Maniak, M.5    Müller-Taubenberger, A.6
  • 32
    • 0035928730 scopus 로고    scopus 로고
    • Peroxisomes: the extended shuttle to the peroxisome matrix
    • Kunau W. Peroxisomes: the extended shuttle to the peroxisome matrix. Curr. Biol. 11 (2001) R659-R662
    • (2001) Curr. Biol. , vol.11
    • Kunau, W.1
  • 33
    • 0039613963 scopus 로고    scopus 로고
    • Three distinct F-actin binding sites in the Dictyostelium discoideum 34,000 Da actin bundling protein
    • Lim R.W., Furukawa R., Eagle S., Cartwright R.C., and Fechheimer M. Three distinct F-actin binding sites in the Dictyostelium discoideum 34,000 Da actin bundling protein. Biochemistry 38 (1999) 800-812
    • (1999) Biochemistry , vol.38 , pp. 800-812
    • Lim, R.W.1    Furukawa, R.2    Eagle, S.3    Cartwright, R.C.4    Fechheimer, M.5
  • 34
    • 0029583095 scopus 로고
    • Coronin involved in phagocytosis: dynamics of particle-induced relocalization visualized by a green fluorescent protein tag
    • Maniak M., Rauchenberger R., Albrecht R., Murphy J., and Gerisch G. Coronin involved in phagocytosis: dynamics of particle-induced relocalization visualized by a green fluorescent protein tag. Cell 83 (1995) 915-924
    • (1995) Cell , vol.83 , pp. 915-924
    • Maniak, M.1    Rauchenberger, R.2    Albrecht, R.3    Murphy, J.4    Gerisch, G.5
  • 35
    • 0029146150 scopus 로고
    • Cloning vectors for the production of proteins in Dictyostelium discoideum
    • Manstein D.J., Schuster H.P., Morandini P., and Hunt D.M. Cloning vectors for the production of proteins in Dictyostelium discoideum. Gene 162 (1995) 129-134
    • (1995) Gene , vol.162 , pp. 129-134
    • Manstein, D.J.1    Schuster, H.P.2    Morandini, P.3    Hunt, D.M.4
  • 36
    • 0036573221 scopus 로고    scopus 로고
    • Formation of Hirano bodies in Dictyostelium and mammalian cells induced by expression of a modified form of an actin-crosslinking protein
    • Maselli A.G., Davis R., Furukawa R., and Fechheimer M. Formation of Hirano bodies in Dictyostelium and mammalian cells induced by expression of a modified form of an actin-crosslinking protein. J. Cell Sci. 115 (2002) 1939-1949
    • (2002) J. Cell Sci. , vol.115 , pp. 1939-1949
    • Maselli, A.G.1    Davis, R.2    Furukawa, R.3    Fechheimer, M.4
  • 37
    • 0028033934 scopus 로고
    • An oligomeric protein is imported into peroxisomes in vivo
    • McNew J.A., and Goodman J.M. An oligomeric protein is imported into peroxisomes in vivo. J. Cell Biol. 127 (1994) 1245-1257
    • (1994) J. Cell Biol. , vol.127 , pp. 1245-1257
    • McNew, J.A.1    Goodman, J.M.2
  • 38
    • 0033050852 scopus 로고    scopus 로고
    • XAIP1: a Xenopus homologue of yeast actin interacting protein 1 (AIP1), which induces disassembly of actin filaments cooperatively with ADF/cofilin family proteins
    • Okada K., Obinata T., and Abe H. XAIP1: a Xenopus homologue of yeast actin interacting protein 1 (AIP1), which induces disassembly of actin filaments cooperatively with ADF/cofilin family proteins. J. Cell Sci. 112 (1999) 1553-1565
    • (1999) J. Cell Sci. , vol.112 , pp. 1553-1565
    • Okada, K.1    Obinata, T.2    Abe, H.3
  • 39
    • 0037044771 scopus 로고    scopus 로고
    • Xenopus actin interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping filament ends
    • Okada K., Blanchoin L., Abe H., Chen H., Pollard T.D., and Bamburg J.R. Xenopus actin interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping filament ends. J. Biol. Chem. 277 (2002) 43011-43016
    • (2002) J. Biol. Chem. , vol.277 , pp. 43011-43016
    • Okada, K.1    Blanchoin, L.2    Abe, H.3    Chen, H.4    Pollard, T.D.5    Bamburg, J.R.6
  • 40
    • 33745613278 scopus 로고    scopus 로고
    • Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments
    • Okada K., Ravi H., Smith E.M., and Goode B.L. Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments. Mol. Biol. Cell 17 (2006) 2855-2868
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2855-2868
    • Okada, K.1    Ravi, H.2    Smith, E.M.3    Goode, B.L.4
  • 41
    • 0344391975 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments
    • Ono S. Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments. Biochemistry 42 (2003) 13363-13370
    • (2003) Biochemistry , vol.42 , pp. 13363-13370
    • Ono, S.1
  • 42
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton L.F., and Paschal B.M. Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 6 (2005) 187-198
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 43
    • 28744459273 scopus 로고    scopus 로고
    • Role of calcium-dependent actin-bundling proteins: characterization of Dictyostelium mutants lacking fimbrin and the 34-kDa protein
    • Pikzack C., Prassler J., Furukawa R., Fechheimer M., and Rivero F. Role of calcium-dependent actin-bundling proteins: characterization of Dictyostelium mutants lacking fimbrin and the 34-kDa protein. Cell Motil. Cytoskeleton 62 (2005) 210-231
    • (2005) Cell Motil. Cytoskeleton , vol.62 , pp. 210-231
    • Pikzack, C.1    Prassler, J.2    Furukawa, R.3    Fechheimer, M.4    Rivero, F.5
  • 44
    • 2542442517 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Dalbey R.E., and von Heijne G. (Eds), Academic Press, Elsevier, London
    • Prinz T., Pfanner N., and Truscott K.N. Translocation of proteins into mitochondria. In: Dalbey R.E., and von Heijne G. (Eds). Protein Targeting, Transport, and Translocation (2002), Academic Press, Elsevier, London 214-239
    • (2002) Protein Targeting, Transport, and Translocation , pp. 214-239
    • Prinz, T.1    Pfanner, N.2    Truscott, K.N.3
  • 45
    • 0031105025 scopus 로고    scopus 로고
    • Coronin and vacuolin identify consecutive stages of a late, actin-coated endocytic compartment in Dictyostelium
    • Rauchenberger R., Hacker U., Murphy J., Niewöhner J., and Maniak M. Coronin and vacuolin identify consecutive stages of a late, actin-coated endocytic compartment in Dictyostelium. Curr. Biol. 7 (1997) 215-218
    • (1997) Curr. Biol. , vol.7 , pp. 215-218
    • Rauchenberger, R.1    Hacker, U.2    Murphy, J.3    Niewöhner, J.4    Maniak, M.5
  • 46
    • 32044464800 scopus 로고    scopus 로고
    • Ancient origin of reggie (flotillin), reggie-like, and other lipid-raft proteins: convergent evolution of the SPFH domain
    • Rivera-Milla E., Stuermer C.A., and Malaga-Trillo E. Ancient origin of reggie (flotillin), reggie-like, and other lipid-raft proteins: convergent evolution of the SPFH domain. Cell Mol. Life Sci. 63 (2006) 343-357
    • (2006) Cell Mol. Life Sci. , vol.63 , pp. 343-357
    • Rivera-Milla, E.1    Stuermer, C.A.2    Malaga-Trillo, E.3
  • 49
    • 0344962439 scopus 로고    scopus 로고
    • One ticket for multiple destinations: dual targeting of proteins to distinct subcellular locations
    • Silva-Filho M.C. One ticket for multiple destinations: dual targeting of proteins to distinct subcellular locations. Curr. Opin. Plant Biol. 6 (2003) 589-595
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 589-595
    • Silva-Filho, M.C.1
  • 50
    • 38149010408 scopus 로고    scopus 로고
    • The import and sorting of proteins into chloroplasts
    • Dalbey R.E., and von Heijne G. (Eds), Academic Press, Elsevier, London
    • Soll J., Robinson C., and Heins L. The import and sorting of proteins into chloroplasts. In: Dalbey R.E., and von Heijne G. (Eds). Protein Targeting, Transport, and Translocation (2002), Academic Press, Elsevier, London 240-267
    • (2002) Protein Targeting, Transport, and Translocation , pp. 240-267
    • Soll, J.1    Robinson, C.2    Heins, L.3
  • 53
    • 33746375657 scopus 로고    scopus 로고
    • Coronins: the return of the crown
    • Uetrecht A.C., and Bear J.E. Coronins: the return of the crown. Trends Cell Biol. 16 (2006) 421-426
    • (2006) Trends Cell Biol. , vol.16 , pp. 421-426
    • Uetrecht, A.C.1    Bear, J.E.2
  • 54
    • 0141557547 scopus 로고    scopus 로고
    • The structure of Aip1p, A WD repeat protein that regulates cofilin-mediated actin depolymerization
    • Voegtli W.C., Madrona A.Y., and Wilson D.K. The structure of Aip1p, A WD repeat protein that regulates cofilin-mediated actin depolymerization. J. Biol. Chem. 278 (2003) 34373-34379
    • (2003) J. Biol. Chem. , vol.278 , pp. 34373-34379
    • Voegtli, W.C.1    Madrona, A.Y.2    Wilson, D.K.3
  • 55
    • 0242574928 scopus 로고    scopus 로고
    • A Dictyostelium long chain fatty acyl coenzyme A synthetase mediates fatty acid retrieval from endosomes
    • von Löhneysen K., Pawolleck N., Rühling H., and Maniak M. A Dictyostelium long chain fatty acyl coenzyme A synthetase mediates fatty acid retrieval from endosomes. Eur. J. Cell Biol. 82 (2003) 505-514
    • (2003) Eur. J. Cell Biol. , vol.82 , pp. 505-514
    • von Löhneysen, K.1    Pawolleck, N.2    Rühling, H.3    Maniak, M.4
  • 56
    • 33748272686 scopus 로고    scopus 로고
    • Vacuolin, a flotillin/reggie-related protein from Dictyostelium oligomerizes for endosome association
    • Wienke D., Drengk A., Schmauch C., Jenne N., and Maniak M. Vacuolin, a flotillin/reggie-related protein from Dictyostelium oligomerizes for endosome association. Eur. J. Cell Biol. 85 (2006) 991-1000
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 991-1000
    • Wienke, D.1    Drengk, A.2    Schmauch, C.3    Jenne, N.4    Maniak, M.5
  • 57
    • 0030690360 scopus 로고    scopus 로고
    • On the role of myosin-II in cytokinesis: division of Dictyostelium cells under adhesive and nonadhesive conditions
    • Zang J.H., Cavet G., Sabry J.H., Wagner P., Moores S.L., and Spudich J.A. On the role of myosin-II in cytokinesis: division of Dictyostelium cells under adhesive and nonadhesive conditions. Mol. Biol. Cell 8 (1997) 2617-2629
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2617-2629
    • Zang, J.H.1    Cavet, G.2    Sabry, J.H.3    Wagner, P.4    Moores, S.L.5    Spudich, J.A.6


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