메뉴 건너뛰기




Volumn 17, Issue 3, 1998, Pages 635-647

Distinct functions of calmodulin are required for the uptake step of receptor-mediated endocytosis in yeast: The type I myosin Myo5p is one of the calmodulin targets

Author keywords

Calmodulin; Endocytosis; Saccharomyces cerevisiae; Type I myosin

Indexed keywords

CALMODULIN; MYOSIN;

EID: 0032472908     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.3.635     Document Type: Article
Times cited : (54)

References (63)
  • 1
    • 0027050472 scopus 로고
    • Structural analysis of wild-type and mutant yeast calmodulins by limited proteolysis and electrospray ionization mass spectrometry
    • Brockerhoff, S.E., Edmonds, C.G. and Davis, T.N. (1992) Structural analysis of wild-type and mutant yeast calmodulins by limited proteolysis and electrospray ionization mass spectrometry. Protein Sci., 1, 504-516.
    • (1992) Protein Sci. , vol.1 , pp. 504-516
    • Brockerhoff, S.E.1    Edmonds, C.G.2    Davis, T.N.3
  • 2
    • 0027954167 scopus 로고
    • The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae
    • Brockerhoff, S.E., Stevens, R.C. and Davis, T.N. (1994) The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae. J. Cell Biol., 124, 315-323.
    • (1994) J. Cell Biol. , vol.124 , pp. 315-323
    • Brockerhoff, S.E.1    Stevens, R.C.2    Davis, T.N.3
  • 3
    • 0028024386 scopus 로고
    • The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast
    • Bénédetti, H., Raths, S., Crausaz, F. and Riezman, H. (1994) The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast. Mol. Biol. Cell, 5, 1023-1037.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1023-1037
    • Bénédetti, H.1    Raths, S.2    Crausaz, F.3    Riezman, H.4
  • 5
    • 0025264994 scopus 로고
    • Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro
    • Collins, K., Sellers, J.R. and Matsudaira, P. (1990) Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro. J. Cell Biol., 110, 1137-1147.
    • (1990) J. Cell Biol. , vol.110 , pp. 1137-1147
    • Collins, K.1    Sellers, J.R.2    Matsudaira, P.3
  • 6
    • 0023006881 scopus 로고
    • Isolation of the yeast calmodulin gene: Calmodulin is an essential protein
    • Davis, T.N., Urdea, M.S., Masiarz, F.R. and Thorner, J. (1986) Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell, 47, 423-431.
    • (1986) Cell , vol.47 , pp. 423-431
    • Davis, T.N.1    Urdea, M.S.2    Masiarz, F.R.3    Thorner, J.4
  • 8
    • 0023948010 scopus 로고
    • High efficiency transformation of E.coli by high voltage electroporation
    • Dower, W.J., Miller, J.F. and Ragsdale, C.W. (1988) High efficiency transformation of E.coli by high voltage electroporation. Nucleic Acids Res., 16, 6127-6145.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 9
    • 0022182550 scopus 로고
    • Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light-chain kinase
    • Edelman, A.M., Takio, K., Blumenthal D.K., Hansen, R.S., Walsh, K.A., Titani, K. and Krebs, E.G. (1985) Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light-chain kinase. J. Biol. Chem., 260, 11275-11285.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11275-11285
    • Edelman, A.M.1    Takio, K.2    Blumenthal, D.K.3    Hansen, R.S.4    Walsh, K.A.5    Titani, K.6    Krebs, E.G.7
  • 10
    • 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. (1985) Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol., 5, 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
  • 12
    • 0029923034 scopus 로고    scopus 로고
    • Role of type I myosins in receptor-mediated endocytosis in yeast
    • Geli, M.I. and Riezman, H. (1996) Role of type I myosins in receptor-mediated endocytosis in yeast. Science, 272, 533-535.
    • (1996) Science , vol.272 , pp. 533-535
    • Geli, M.I.1    Riezman, H.2
  • 13
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R.D. and Sugino, A. (1988) New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene, 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 14
    • 0028929478 scopus 로고
    • Identification and molecular characterization of a yeast myosin I
    • Goodson, H.V. and Spudich, J.A. (1995) Identification and molecular characterization of a yeast myosin I. Cell. Motility Cytoskeleton, 30, 73-84.
    • (1995) Cell. Motility Cytoskeleton , vol.30 , pp. 73-84
    • Goodson, H.V.1    Spudich, J.A.2
  • 15
    • 0029984773 scopus 로고    scopus 로고
    • Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): Myosin I proteins are required for polarization of the actin cytoskeleton
    • Goodson, H.V., Anderson, B.L., Warrick, H.M., Pon, L.A. and Spudich, J.A. (1996) Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton. J. Cell Biol., 133, 1277-1291.
    • (1996) J. Cell Biol. , vol.133 , pp. 1277-1291
    • Goodson, H.V.1    Anderson, B.L.2    Warrick, H.M.3    Pon, L.A.4    Spudich, J.A.5
  • 16
    • 0019842601 scopus 로고
    • Role of sulA and sulB in filamentation by lon mutants of Escherichia coli K-12
    • Gottesman, S., Halpern, E. and Trisler, P. (1981) Role of sulA and sulB in filamentation by lon mutants of Escherichia coli K-12. J. Bacteriol., 148, 265-273.
    • (1981) J. Bacteriol. , vol.148 , pp. 265-273
    • Gottesman, S.1    Halpern, E.2    Trisler, P.3
  • 17
  • 18
    • 0030803426 scopus 로고    scopus 로고
    • Transport through the yeast endocytic pathway occurs through morphologically distinct compartments and requires an active secretory pathway and Sec18p/N-ethylmaleimide-sensitive fusion protein
    • Hicke, L., Zanolari, B., Pypaert, M., Rohrer, J. and Riezman, H. (1997) Transport through the yeast endocytic pathway occurs through morphologically distinct compartments and requires an active secretory pathway and Sec18p/N-ethylmaleimide-sensitive fusion protein. Mol. Biol. Cell, 8, 13-31.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 13-31
    • Hicke, L.1    Zanolari, B.2    Pypaert, M.3    Rohrer, J.4    Riezman, H.5
  • 19
    • 0028019430 scopus 로고
    • Rapid protein extraction from yeast
    • Horvath, A. and H. Riezman (1994) Rapid protein extraction from yeast. Yeast 10, 1305-1310.
    • (1994) Yeast , vol.10 , pp. 1305-1310
    • Horvath, A.1    Riezman, H.2
  • 20
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K. and Kimura, A. (1983) Transformation of intact yeast cells treated with alkali cations. J. Bacteriol., 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 22
    • 0028921581 scopus 로고
    • Calmodulin-binding domains: Just two faced or multi-faceted?
    • James, P.H., Vorherr, T. and Carafoli, E. (1995) Calmodulin-binding domains: just two faced or multi-faceted?. Trends Biochem. Sci., 20, 38-42.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 38-42
    • James, P.H.1    Vorherr, T.2    Carafoli, E.3
  • 23
    • 0028274104 scopus 로고
    • Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
    • Janmey, P.A. (1994) Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol., 56, 169-191.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 169-191
    • Janmey, P.A.1
  • 24
    • 0029925627 scopus 로고    scopus 로고
    • Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions
    • Jung, G., Wu, X. and Hammer, J.A., III (1996) Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions. J. Cell Biol., 133, 305-323.
    • (1996) J. Cell Biol. , vol.133 , pp. 305-323
    • Jung, G.1    Wu, X.2    Hammer III, J.A.3
  • 25
    • 0025899139 scopus 로고
    • The regulatory light-chain of nonmuscle myosin is encoded by spaghetti-squash, a gene required for cytokinesis in Drosophila
    • Karess, R.E., Chang, X.-J., Edwards, K.A., Kulkarni, S., Aguilera, I. and Kiehart, D.P. (1991) The regulatory light-chain of nonmuscle myosin is encoded by spaghetti-squash, a gene required for cytokinesis in Drosophila. Cell, 65, 1177-1189.
    • (1991) Cell , vol.65 , pp. 1177-1189
    • Karess, R.E.1    Chang, X.-J.2    Edwards, K.A.3    Kulkarni, S.4    Aguilera, I.5    Kiehart, D.P.6
  • 28
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kübler, E. and Riezman, H. (1993) Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J., 12, 2855-2862.
    • (1993) EMBO J. , vol.12 , pp. 2855-2862
    • Kübler, E.1    Riezman, H.2
  • 29
    • 0028027789 scopus 로고
    • Calcium-independent calmodulin requirement for endocytosis in yeast
    • Kübler, E., Schimmöller, F. and Riezman, H. (1994) Calcium-independent calmodulin requirement for endocytosis in yeast. EMBO J., 13, 5539-5546.
    • (1994) EMBO J. , vol.13 , pp. 5539-5546
    • Kübler, E.1    Schimmöller, F.2    Riezman, H.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.), 227, 680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0030860515 scopus 로고    scopus 로고
    • The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells
    • Lamaze, C., Fujimoto, L.M., Yin, H.L. and Schmid, S.L. (1997) The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells. J. Biol. Chem., 272, 20332-20335.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20332-20335
    • Lamaze, C.1    Fujimoto, L.M.2    Yin, H.L.3    Schmid, S.L.4
  • 32
    • 0018177274 scopus 로고
    • The isolated heavy chain of an Acanthamoeba myosin contains full enzymatic activity
    • Maruta, H., Gadasi, H., Collins, J.H. and Korn, E.D. (1978) The isolated heavy chain of an Acanthamoeba myosin contains full enzymatic activity. J. Biol. Chem., 253, 6297-6300.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6297-6300
    • Maruta, H.1    Gadasi, H.2    Collins, J.H.3    Korn, E.D.4
  • 34
    • 0028856410 scopus 로고
    • End5, end6, and end7: Mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae
    • Munn, A.L., Stevenson, B.J., Geli, M.I. and Riezman, H. (1995). end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell, 6, 1721-1742.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1721-1742
    • Munn, A.L.1    Stevenson, B.J.2    Geli, M.I.3    Riezman, H.4
  • 35
    • 0028838302 scopus 로고
    • Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis
    • Novak, K.D., Peterson, M.D., Reedy, M.C. and Titus, M.A. (1995) Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis. J. Cell Biol., 131, 1205-1221.
    • (1995) J. Cell Biol. , vol.131 , pp. 1205-1221
    • Novak, K.D.1    Peterson, M.D.2    Reedy, M.C.3    Titus, M.A.4
  • 36
    • 0028266837 scopus 로고
    • Diverse essential functions revealed by complementing yeast calmodulin mutants
    • Ohya, Y. and Botstein, D. (1994a) Diverse essential functions revealed by complementing yeast calmodulin mutants. Science, 263, 963-966.
    • (1994) Science , vol.263 , pp. 963-966
    • Ohya, Y.1    Botstein, D.2
  • 37
    • 0027960082 scopus 로고
    • Structure-based systematic isolation of conditional-lethal mutations in the single yeast calmodulin gene
    • Ohya, Y. and Botstein, D. (1994b) Structure-based systematic isolation of conditional-lethal mutations in the single yeast calmodulin gene. Genetics, 138, 1041-1054.
    • (1994) Genetics , vol.138 , pp. 1041-1054
    • Ohya, Y.1    Botstein, D.2
  • 38
    • 0028906643 scopus 로고
    • The interaction of calmodulin with clathrin-coated vesicles, triskelions, and light-chains. Localization of a binding site
    • Pley, U.M., Alibert, C., Brodsky, F.M. and Parham, P. (1995) The interaction of calmodulin with clathrin-coated vesicles, triskelions, and light-chains. Localization of a binding site. J. Biol. Chem., 270, 2395-2402.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2395-2402
    • Pley, U.M.1    Alibert, C.2    Brodsky, F.M.3    Parham, P.4
  • 40
    • 0027455339 scopus 로고
    • End3 and end4: Two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • Raths, S., Rohrer, J., Crausaz, F. and Riezman, H. (1993) end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol., 120, 55-65.
    • (1993) J. Cell Biol. , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 41
    • 0000848663 scopus 로고    scopus 로고
    • Yeast vectors and assays for expression of cloned genes
    • John Wiley and Sons Inc., USA
    • Reynolds, A., Lundblad, V., Dorris, D. and Keaveney, M. (1997) Yeast vectors and assays for expression of cloned genes. In Current Protocols in Molecular Biology, Volume II. John Wiley and Sons Inc., USA, 13.6.1-13.6.6.
    • (1997) Current Protocols in Molecular Biology , vol.2 , pp. 1361-1366
    • Reynolds, A.1    Lundblad, V.2    Dorris, D.3    Keaveney, M.4
  • 42
    • 0030476867 scopus 로고    scopus 로고
    • Actin-, myosin- and ubiquitin-dependent endocytosis
    • Riezman, H., Munn, A., Geli, M.I. and Hicke, L. (1996) Actin-, myosin-and ubiquitin-dependent endocytosis. Experientia, 52, 1033-1041.
    • (1996) Experientia , vol.52 , pp. 1033-1041
    • Riezman, H.1    Munn, A.2    Geli, M.I.3    Hicke, L.4
  • 43
    • 0026429185 scopus 로고
    • Generating yeast transcriptional activators containing no yeast protein sequences
    • Ruden, D.M., Ma, J., Li, Y., Wood, K. and Ptashne, M. (1991) Generating yeast transcriptional activators containing no yeast protein sequences. Nature, 350, 250-252.
    • (1991) Nature , vol.350 , pp. 250-252
    • Ruden, D.M.1    Ma, J.2    Li, Y.3    Wood, K.4    Ptashne, M.5
  • 44
    • 0019068962 scopus 로고
    • Role of coated vesicles, microfilaments, and calmodulin in receptor-mediated endocytosis by cultured B lymphoblastoid cells
    • Salisbury, J.L., Condeelis, J.S. and Satir, P. (1980) Role of coated vesicles, microfilaments, and calmodulin in receptor-mediated endocytosis by cultured B lymphoblastoid cells. J. Cell Biol., 87, 132-141.
    • (1980) J. Cell Biol. , vol.87 , pp. 132-141
    • Salisbury, J.L.1    Condeelis, J.S.2    Satir, P.3
  • 47
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 48
    • 0028930161 scopus 로고
    • A novel mammalian myosin I from rat with an SH3 domain localizes to con A-inducible. F-actin-rich structures at cell-cell contacts
    • Stöffler, H.-E., Ruppert, C., Reinhard, J. and Bähler, M. (1995) A novel mammalian myosin I from rat with an SH3 domain localizes to con A-inducible. F-actin-rich structures at cell-cell contacts. J. Cell Biol., 129, 819-830.
    • (1995) J. Cell Biol. , vol.129 , pp. 819-830
    • Stöffler, H.-E.1    Ruppert, C.2    Reinhard, J.3    Bähler, M.4
  • 49
    • 0025201631 scopus 로고
    • The ADE2 gene from Saccharomyces cerevisiae: Sequence and new vectors
    • Stotz, A. and Linder, P. (1990) The ADE2 gene from Saccharomyces cerevisiae: sequence and new vectors. Gene, 95, 91-98.
    • (1990) Gene , vol.95 , pp. 91-98
    • Stotz, A.1    Linder, P.2
  • 50
    • 0025782956 scopus 로고
    • Rapid, high-yield purification of intestinal Brush Border Myosin I
    • Swanljung-Collins, H. and Collins, J.H. (1991) Rapid, high-yield purification of intestinal Brush Border Myosin I. Methods Enzymol., 196, 3-11.
    • (1991) Methods Enzymol. , vol.196 , pp. 3-11
    • Swanljung-Collins, H.1    Collins, J.H.2
  • 51
    • 0026709998 scopus 로고
    • Control of nonmuscle myosins by phosphorylation
    • Tan, J.L., Ravid, S. and Spudich, J.A. (1992) Control of nonmuscle myosins by phosphorylation. Annu. Rev. Biochem., 61, 721-759.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 721-759
    • Tan, J.L.1    Ravid, S.2    Spudich, J.A.3
  • 52
    • 0344279906 scopus 로고    scopus 로고
    • EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae
    • Tang, H.-Y., Munn, A. and Cai, M. (1997) EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae. Mol. Cell. Biol., 17, 4294-4304.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4294-4304
    • Tang, H.-Y.1    Munn, A.2    Cai, M.3
  • 53
    • 0031106858 scopus 로고    scopus 로고
    • Unconventional myosins: New frontiers in actin-based motors
    • Titus, M.A. (1997) Unconventional myosins: new frontiers in actin-based motors. Trends Cell Biol., 7, 119-123.
    • (1997) Trends Cell Biol. , vol.7 , pp. 119-123
    • Titus, M.A.1
  • 54
    • 0027767689 scopus 로고
    • A functional recombinant myosin II lacking a regulatory light-chain-binding site
    • Uyeda, T.Q.P. and Spudich, J.A. (1993) A functional recombinant myosin II lacking a regulatory light-chain-binding site. Science. 262, 1867-1869.
    • (1993) Science , vol.262 , pp. 1867-1869
    • Uyeda, T.Q.P.1    Spudich, J.A.2
  • 55
    • 0343286277 scopus 로고
    • Movement of scallop myosin on Nitella actin filaments: Regulation by calcium
    • Vale, R.D., Szent-Gyorgyi, A.G. and Sheetz, M.P. (1984) Movement of scallop myosin on Nitella actin filaments: regulation by calcium. Proc. Natl Acad. Sci. USA, 81, 6775-6778.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 6775-6778
    • Vale, R.D.1    Szent-Gyorgyi, A.G.2    Sheetz, M.P.3
  • 56
    • 0016167677 scopus 로고
    • Beta-galactosidase from termination and deletion mutant strains
    • Villarejo, M.R. and Zabin, I. (1974) Beta-galactosidase from termination and deletion mutant strains. J. Bacteriol., 120, 466-474.
    • (1974) J. Bacteriol. , vol.120 , pp. 466-474
    • Villarejo, M.R.1    Zabin, I.2
  • 58
    • 0027062885 scopus 로고
    • Myosin light-chain-2 mutation affects flight, wing beat frequency, and indirect flight muscle contraction kinetics in Drosophila
    • Warmke, J., Yamakawa, M., Molloy, J., Fankenthal, S. and Maughan, D. (1992) Myosin light-chain-2 mutation affects flight, wing beat frequency, and indirect flight muscle contraction kinetics in Drosophila. J. Cell Biol., 119, 1523-1189.
    • (1992) J. Cell Biol. , vol.119 , pp. 1523-11189
    • Warmke, J.1    Yamakawa, M.2    Molloy, J.3    Fankenthal, S.4    Maughan, D.5
  • 59
    • 12644263389 scopus 로고    scopus 로고
    • A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15
    • Wendland, B., McCaffery, J.M., Xiao, Q. and Emr, S.D. (1996) A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15. J. Cell Biol., 135, 1485-1500.
    • (1996) J. Cell Biol. , vol.135 , pp. 1485-1500
    • Wendland, B.1    McCaffery, J.M.2    Xiao, Q.3    Emr, S.D.4
  • 60
    • 0030785341 scopus 로고    scopus 로고
    • End4/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae
    • Wesp, A., Hicke, L., Palecek, J., Lombardi, R., Aust, J., Munn, L.A. and Riezman, H. (1997) End4/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell, 8, 2291-2306.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2291-2306
    • Wesp, A.1    Hicke, L.2    Palecek, J.3    Lombardi, R.4    Aust, J.5    Munn, L.A.6    Riezman, H.7
  • 61
    • 0027219972 scopus 로고
    • Calcium-calmodulin and regulation of brush border myosin-I Mg-ATPase and mechanochemistry
    • Wolenski, J.S., Hayden, S.M., Forscher, P. and Mooseker, M.S. (1993) Calcium-calmodulin and regulation of brush border myosin-I Mg-ATPase and mechanochemistry. J. Cell Biol., 122, 613-621.
    • (1993) J. Cell Biol. , vol.122 , pp. 613-621
    • Wolenski, J.S.1    Hayden, S.M.2    Forscher, P.3    Mooseker, M.S.4
  • 62
    • 0029025172 scopus 로고
    • Regulation of calmodulin binding myosins
    • Wolenski, J.S. (1995) Regulation of calmodulin binding myosins. Trends Cell Biol., 5, 310-316.
    • (1995) Trends Cell Biol. , vol.5 , pp. 310-316
    • Wolenski, J.S.1
  • 63
    • 0021338945 scopus 로고
    • 2+-ATPase of the erythrocyte membrane. A correlation between the structure and the function of the enzyme
    • 2+-ATPase of the erythrocyte membrane. A correlation between the structure and the function of the enzyme. J. Biol. Chem. 259, 618-624.
    • (1984) J. Biol. Chem. , vol.259 , pp. 618-624
    • Zurini, M.1    Krebs, J.2    Penniston, J.T.3    Carafoli, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.