메뉴 건너뛰기




Volumn 39, Issue 5, 2011, Pages 1185-1190

Function and regulation of Saccharomyces cerevisiae myosins-I in endocytic budding

Author keywords

Endocytic budding; Myosin I; Plasma membrane; Saccharomyces cerevisiae

Indexed keywords

ACTIN; CALMODULIN; FUNGAL PROTEIN; MYOSIN 3; MYOSIN 5; MYOSIN I; SERINE; UNCLASSIFIED DRUG;

EID: 80053351049     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0391185     Document Type: Review
Times cited : (9)

References (54)
  • 3
    • 0036856301 scopus 로고    scopus 로고
    • Cofilin, but not profilin, is required for myosin-I-induced actin polymerization and the endocytic uptake in yeast
    • DOI 10.1091/mbc.02-04-0052
    • Idrissi, F.Z., Wolf, B.L. and Geli, M.I. (2002) Cofilin, but not profilin, is required for myosin-I-induced actin polymerization and the endocytic uptake in yeast. Mol. Biol. Cell 13, 4074-4087 (Pubitemid 35398571)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.11 , pp. 4074-4087
    • Idrissi, F.-Z.1    Wolf, B.L.2    Geli, M.I.3
  • 5
    • 0034707580 scopus 로고    scopus 로고
    • Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization
    • DOI 10.1083/jcb.148.2.363
    • Lechler, T., Shevchenko, A. and Li, R. (2000) Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J. Cell Biol. 148, 363-373 (Pubitemid 30078248)
    • (2000) Journal of Cell Biology , vol.148 , Issue.2 , pp. 363-373
    • Lechler, T.1    Shevchenko, A.2    Shevchenko, A.3    Li, R.4
  • 6
    • 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, PII S1534580706002462
    • Sun, Y., Martin, A.C. and Drubin, D.G. (2006) Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity. Dev. Cell 11, 33-46 (Pubitemid 43977198)
    • (2006) Developmental Cell , vol.11 , Issue.1 , pp. 33-46
    • Sun, Y.1    Martin, A.C.2    Drubin, D.G.3
  • 7
    • 0034645065 scopus 로고    scopus 로고
    • Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASP
    • Lee, W.L., Bezanilla, M. and Pollard, T.D. (2000) Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASP. J. Cell Biol. 151, 789-800
    • (2000) J. Cell Biol. , vol.151 , pp. 789-800
    • Lee, W.L.1    Bezanilla, M.2    Pollard, T.D.3
  • 8
    • 0035889090 scopus 로고    scopus 로고
    • A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast
    • DOI 10.1083/jcb.200104094
    • Lechler, T., Jonsdottir, G.A., Klee, S.K., Pellman, D. and Li, R. (2001) A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast. J. Cell Biol. 155, 261-270 (Pubitemid 34289301)
    • (2001) Journal of Cell Biology , vol.155 , Issue.2 , pp. 261-270
    • Lechler, T.1    Jonsdottir, G.A.2    Klee, S.K.3    Pellman, D.4    Li, R.5
  • 9
    • 0035954433 scopus 로고    scopus 로고
    • The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains
    • DOI 10.1083/jcb.153.7.1479
    • Jung, G., Remmert, K., Wu, X., Volosky, J.M. and Hammer, III, J.A. (2001) The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains. J. Cell Biol. 153, 1479-1497 (Pubitemid 34286131)
    • (2001) Journal of Cell Biology , vol.153 , Issue.7 , pp. 1479-1497
    • Jung, G.1    Remmert, K.2    Wu, X.3    Volosky, J.M.4    Hammer III, J.A.5
  • 10
    • 0015834603 scopus 로고
    • Acanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin
    • Pollard, T.D. and Korn, E.D. (1973) Acanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin. J. Biol. Chem. 248, 4682-4690
    • (1973) J. Biol. Chem. , vol.248 , pp. 4682-4690
    • Pollard, T.D.1    Korn, E.D.2
  • 12
    • 44449133509 scopus 로고    scopus 로고
    • Actin in the endocytic pathway: From yeast to mammals
    • Girao, H., Geli, M.I. and Idrissi, F.Z. (2008) Actin in the endocytic pathway: from yeast to mammals. FEBS Lett. 582, 2112-2119
    • (2008) FEBS Lett. , vol.582 , pp. 2112-2119
    • Girao, H.1    Geli, M.I.2    Idrissi, F.Z.3
  • 13
    • 47749143279 scopus 로고    scopus 로고
    • Myosin I: From yeast to human
    • Kim, S.V. and Flavell, R.A. (2008) Myosin I: from yeast to human. Cell. Mol. Life Sci. 65, 2128-2137
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2128-2137
    • Kim, S.V.1    Flavell, R.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 Motil. Cytoskeleton 30, 73-84
    • (1995) Cell Motil. Cytoskeleton , vol.30 , pp. 73-84
    • Goodson, H.V.1    Spudich, J.A.2
  • 15
    • 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 (Pubitemid 26138193)
    • (1996) Science , vol.272 , Issue.5261 , pp. 533-535
    • Geli, M.I.1    Riezman, H.2
  • 16
    • 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
    • DOI 10.1083/jcb.133.6.1277
    • 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 (Pubitemid 26192329)
    • (1996) Journal of Cell Biology , vol.133 , Issue.6 , pp. 1277-1291
    • Goodson, H.V.1    Andersen, B.L.2    Warrick, H.M.3    Pon, L.A.4    Spudich, J.A.5
  • 17
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kubler, E. and Riezman, H. (1993) Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J. 12, 2855-2862 (Pubitemid 23218335)
    • (1993) EMBO Journal , vol.12 , Issue.7 , pp. 2855-2862
    • Kubler, E.1    Riezman, H.2
  • 18
    • 0028027789 scopus 로고
    • Calcium-independent calmodulin requirement for endocytosis in yeast
    • Kubler, E., Schimmoller, F. and Riezman, H. (1994) Calcium-independent calmodulin requirement for endocytosis in yeast. EMBO J. 13, 5539-5546 (Pubitemid 24363021)
    • (1994) EMBO Journal , vol.13 , Issue.23 , pp. 5539-5546
    • Kubler, E.1    Schimmoller, F.2    Riezman, H.3
  • 19
    • 0141727533 scopus 로고    scopus 로고
    • Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling
    • DOI 10.1016/j.cub.2003.09.001
    • Valdez-Taubas, J. and Pelham, H.R. (2003) Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling. Curr. Biol. 13, 1636-1640 (Pubitemid 37215889)
    • (2003) Current Biology , vol.13 , Issue.18 , pp. 1636-1640
    • Valdez-Taubas, J.1    Pelham, H.R.B.2
  • 20
    • 0032526679 scopus 로고    scopus 로고
    • The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization
    • DOI 10.1083/jcb.141.6.1357
    • Anderson, B.L., Boldogh, I., Evangelista, M., Boone, C., Greene, L.A. and Pon, L.A. (1998) The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J. Cell Biol. 141, 1357-1370 (Pubitemid 28289911)
    • (1998) Journal of Cell Biology , vol.141 , Issue.6 , pp. 1357-1370
    • Anderson, B.L.1    Boldogh, I.2    Evangelista, M.3    Boone, C.4    Greene, L.A.5    Pon, L.A.6
  • 21
    • 0034002965 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast. 1. Establishment and maintenance of polarity states
    • Pruyne, D. and Bretscher, A. (2000) Polarization of cell growth in yeast. I. Establishment and maintenance of polarity states. J. Cell Sci. 113, 365-375 (Pubitemid 30116643)
    • (2000) Journal of Cell Science , vol.113 , Issue.3 , pp. 365-375
    • Pruyne, D.1    Bretscher, A.2
  • 22
    • 0034056057 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast
    • Pruyne, D. and Bretscher, A. (2000) Polarization of cell growth in yeast. J. Cell Sci. 113, 571-585
    • (2000) J. Cell Sci. , vol.113 , pp. 571-585
    • Pruyne, D.1    Bretscher, A.2
  • 23
    • 69249208824 scopus 로고    scopus 로고
    • Verprolin: A cool set of actin-binding sites and some very HOT prolines
    • Munn, A.L. and Thanabalu, T. (2009) Verprolin: a cool set of actin-binding sites and some very HOT prolines. IUBMB Life 61, 707-712
    • (2009) IUBMB Life , vol.61 , pp. 707-712
    • Munn, A.L.1    Thanabalu, T.2
  • 24
    • 0344827286 scopus 로고    scopus 로고
    • A Pathway for Association of Receptors, Adaptors, and Actin during Endocytic Internalization
    • DOI 10.1016/S0092-8674(03)00883-3
    • Kaksonen, M., Sun, Y. and Drubin, D.G. (2003) A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 115, 475-487 (Pubitemid 37456809)
    • (2003) Cell , vol.115 , Issue.4 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 25
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin- and actin-mediated endocytosis machinery
    • DOI 10.1016/j.cell.2005.09.024, PII S0092867405009785
    • Kaksonen, M., Toret, C.P. and Drubin, D.G. (2005) A modular design for the clathrin- and actin-mediated endocytosis machinery. Cell 123, 305-320 (Pubitemid 41457219)
    • (2005) Cell , vol.123 , Issue.2 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 27
    • 4644250535 scopus 로고    scopus 로고
    • Dynamics of yeast myosin I: Evidence for a possible role in scission of endocytic vesicles
    • DOI 10.1016/j.cub.2004.08.055, PII S0960982204006542
    • Jonsdottir, G.A. and Li, R. (2004) Dynamics of yeast myosin I: evidence for a possible role in scission of endocytic vesicles. Curr. Biol. 14, 1604-1609 (Pubitemid 39290061)
    • (2004) Current Biology , vol.14 , Issue.17 , pp. 1604-1609
    • Jonsdottir, G.A.1    Li, R.2
  • 28
    • 0034663930 scopus 로고    scopus 로고
    • An intact SH3 domain is required for myosin I-induced actin polymerization
    • Geli, M.I., Lombardi, R., Schmelzl, B. and Riezman, H. (2000) An intact SH3 domain is required for myosin I-induced actin polymerization. EMBO J. 19, 4281-4291 (Pubitemid 30623739)
    • (2000) EMBO Journal , vol.19 , Issue.16 , pp. 4281-4291
    • Geli, M.I.1    Lombardi, R.2    Schmelzl, B.3    Riezman, H.4
  • 29
    • 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
  • 30
    • 38949214078 scopus 로고    scopus 로고
    • Distinct roles for Arp2/3 regulators in actin assembly and endocytosis
    • Galletta, B.J., Chuang, D.Y. and Cooper, J.A. (2008) Distinct roles for Arp2/3 regulators in actin assembly and endocytosis. PLoS Biol. 6, e1
    • (2008) PLoS Biol. , vol.6
    • Galletta, B.J.1    Chuang, D.Y.2    Cooper, J.A.3
  • 31
    • 33846821794 scopus 로고    scopus 로고
    • Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis
    • DOI 10.1016/j.febslet.2007.01.021, PII S0014579307000543
    • Krendel, M., Osterweil, E.K. and Mooseker, M.S. (2007) Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis. FEBS Lett. 581, 644-650 (Pubitemid 46216290)
    • (2007) FEBS Letters , vol.581 , Issue.4 , pp. 644-650
    • Krendel, M.1    Osterweil, E.K.2    Mooseker, M.S.3
  • 32
    • 79953718772 scopus 로고    scopus 로고
    • A high precision survey of the molecular dynamics of Mammalian clathrin-mediated endocytosis
    • Taylor, M.J., Perrais, D. and Merrifield, C.J. (2011) A high precision survey of the molecular dynamics of Mammalian clathrin-mediated endocytosis. PLoS Biol. 9, e1000604
    • (2011) PLoS Biol. , vol.9
    • Taylor, M.J.1    Perrais, D.2    Merrifield, C.J.3
  • 33
    • 0034908071 scopus 로고    scopus 로고
    • Regulation of nonmuscle myosins by heavy chain phosphorylation
    • Redowicz, M.J. (2001) Regulation of nonmuscle myosins by heavy chain phosphorylation. J. Muscle Res. Cell Motil. 22, 163-173
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 163-173
    • Redowicz, M.J.1
  • 34
    • 0029006373 scopus 로고
    • TEDS rule: A molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head
    • Bement, W.M. and Mooseker, M.S. (1995) TEDS rule: a molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head. Cell Motil. Cytoskeleton 31, 87-92
    • (1995) Cell Motil. Cytoskeleton , vol.31 , pp. 87-92
    • Bement, W.M.1    Mooseker, M.S.2
  • 36
    • 0029910216 scopus 로고    scopus 로고
    • Cloning and characterization of a Dictyostelium myosin I heavy chain kinase activated by Cdc42 and Rac
    • DOI 10.1074/jbc.271.43.27044
    • Lee, S.F., Egelhoff, T.T., Mahasneh, A. and Cote, G.P. (1996) Cloning and characterization of a Dictyostelium myosin I heavy chain kinase activated by Cdc42 and Rac. J. Biol. Chem. 271, 27044-27048 (Pubitemid 26359123)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.43 , pp. 27044-27048
    • Lee, S.-F.1    Egelhoff, T.T.2    Mahasneh, A.3    Cote, G.P.4
  • 37
    • 0038554077 scopus 로고    scopus 로고
    • Biology of the p21-activated kinases
    • Bokoch, G.M. (2003) Biology of the p21-activated kinases. Annu. Rev. Biochem. 72, 743-781
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 743-781
    • Bokoch, G.M.1
  • 38
    • 33744959045 scopus 로고    scopus 로고
    • TEDS site phosphorylation of the yeast myosins I is required for ligand-induced but not for constitutive endocytosis of the G protein-coupled receptor Ste2p
    • DOI 10.1074/jbc.M508933200
    • Grosshans, B.L., Grotsch, H., Mukhopadhyay, D., Fernandez, I.M., Pfannstiel, J., Idrissi, F.Z., Lechner, J., Riezman, H. and Geli, M.I. (2006) TEDS site phosphorylation of the yeast myosins I is required for ligand-induced but not for constitutive endocytosis of the G protein-coupled receptor Ste2p. J. Biol. Chem. 281, 11104-11114 (Pubitemid 43855535)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.16 , pp. 11104-11114
    • Grosshans, B.L.1    Grotsch, H.2    Mukhopadhyay, D.3    Ferna, I.M.4    Pfannstiel, J.5    Idrissi, F.-Z.6    Lechner, J.7    Riezman, H.8    Geli, M.I.9
  • 39
    • 50049119791 scopus 로고    scopus 로고
    • Sphingolipids: New insights into sphingolipid metabolism and function in budding yeast
    • Dickson, R.C. (2008) Sphingolipids: new insights into sphingolipid metabolism and function in budding yeast. J. Lipid Res. 49, 909-921
    • (2008) J. Lipid Res. , vol.49 , pp. 909-921
    • Dickson, R.C.1
  • 41
    • 34250844333 scopus 로고    scopus 로고
    • SNX9 Couples Actin Assembly to Phosphoinositide Signals and Is Required for Membrane Remodeling during Endocytosis
    • DOI 10.1016/j.devcel.2007.04.014, PII S153458070700161X
    • Yarar, D., Waterman-Storer, C.M. and Schmid, S.L. (2007) SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Dev. Cell 13, 43-56 (Pubitemid 46972030)
    • (2007) Developmental Cell , vol.13 , Issue.1 , pp. 43-56
    • Yarar, D.1    Waterman-Storer, C.M.2    Schmid, S.L.3
  • 42
    • 55549134613 scopus 로고    scopus 로고
    • EFC/F-BAR proteins and the N-WASP-WIP complex induce membrane curvature-dependent actin polymerization
    • Takano, K., Toyooka, K. and Suetsugu, S. (2008) EFC/F-BAR proteins and the N-WASP-WIP complex induce membrane curvature-dependent actin polymerization. EMBO J. 27, 2817-2828
    • (2008) EMBO J. , vol.27 , pp. 2817-2828
    • Takano, K.1    Toyooka, K.2    Suetsugu, S.3
  • 44
    • 33750515229 scopus 로고    scopus 로고
    • Myo1c binds phosphoinositides through a putative pleckstrin homology domain
    • DOI 10.1091/mbc.E06-05-0449
    • Hokanson, D.E., Laakso, J.M., Lin, T., Sept, D. and Ostap, E.M. (2006) Myo1c binds phosphoinositides through a putative pleckstrin homology domain. Mol. Biol. Cell 17, 4856-4865 (Pubitemid 44665754)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.11 , pp. 4856-4865
    • Hokanson, D.E.1    Laakso, J.M.2    Lin, T.3    Sept, D.4    Ostap, E.M.5
  • 45
    • 57649133951 scopus 로고    scopus 로고
    • Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative charge
    • Brzeska, H., Hwang, K.J. and Korn, E.D. (2008) Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative charge. J. Biol. Chem. 283, 32014-32023
    • (2008) J. Biol. Chem. , vol.283 , pp. 32014-32023
    • Brzeska, H.1    Hwang, K.J.2    Korn, E.D.3
  • 46
    • 77956257788 scopus 로고    scopus 로고
    • Localization of myosin 1b to actin protrusions requires phosphoinositide binding
    • Komaba, S. and Coluccio, L.M. (2010) Localization of myosin 1b to actin protrusions requires phosphoinositide binding. J. Biol. Chem. 285, 27686-27693
    • (2010) J. Biol. Chem. , vol.285 , pp. 27686-27693
    • Komaba, S.1    Coluccio, L.M.2
  • 47
    • 77950573946 scopus 로고    scopus 로고
    • Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH)
    • Patino-Lopez, G., Aravind, L., Dong, X., Kruhlak, M.J., Ostap, E.M. and Shaw, S. (2010) Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH). J. Biol. Chem. 285, 8675-8686
    • (2010) J. Biol. Chem. , vol.285 , pp. 8675-8686
    • Patino-Lopez, G.1    Aravind, L.2    Dong, X.3    Kruhlak, M.J.4    Ostap, E.M.5    Shaw, S.6
  • 52
    • 70349546862 scopus 로고    scopus 로고
    • Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution
    • Holt, L.J., Tuch, B.B., Villén, J., Johnson, A.D., Gygi, S.P. and Morgan, D.O. (2009) Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325, 1682-1686
    • (2009) Science , vol.325 , pp. 1682-1686
    • Holt, L.J.1    Tuch, B.B.2    Villén, J.3    Johnson, A.D.4    Gygi, S.P.5    Morgan, D.O.6
  • 54
    • 47849125967 scopus 로고    scopus 로고
    • A multidimensional chromatography technology for in-depth phosphoproteome analysis
    • DOI 10.1074/mcp.M700468-MCP200
    • Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J. and Zhou, H. (2008) A multidimensional chromatography technology for in-depth phosphoproteome analysis. Mol. Cell. Proteomics. 7, 1389-1396 (Pubitemid 352038280)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.7 , pp. 1389-1396
    • Albuquerque, C.P.1    Smolka, M.B.2    Payne, S.H.3    Bafna, V.4    Eng, J.5    Zhou, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.