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Volumn 30, Issue 6, 2014, Pages 746-758

Crosstalk between PI(4,5)P2 and CK2 Modulates Actin Polymerization during Endocytic Uptake

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN RELATED PROTEIN 2-3 COMPLEX; CASEIN KINASE; CASEIN KINASE II; CASEIN KINASE IIALPHA; HOLOENZYME; MYOSIN I; MYOSIN V; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; SYNAPTOJANIN; UNCLASSIFIED DRUG; ACTIN; ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; ARP2 PROTEIN, S CEREVISIAE; ARP3 PROTEIN, S CEREVISIAE; CKA2 PROTEIN, S CEREVISIAE; INP51 PROTEIN, S CEREVISIAE; INP52 PROTEIN, S CEREVISIAE; MYO5 PROTEIN, S CEREVISIAE; PHOSPHATASE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84908154949     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2014.07.020     Document Type: Article
Times cited : (20)

References (60)
  • 1
    • 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
    • Anderson B.L., Boldogh I., Evangelista M., Boone C., Greene L.A., Pon L.A. 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. 1998, 141:1357-1370.
    • (1998) J.Cell Biol. , vol.141 , pp. 1357-1370
    • Anderson, B.L.1    Boldogh, I.2    Evangelista, M.3    Boone, C.4    Greene, L.A.5    Pon, L.A.6
  • 2
    • 0023001146 scopus 로고
    • Clathrin-coated vesicles contain two protein kinase activities. Phosphorylation of clathrin beta-light chain by casein kinase II
    • Bar-Zvi D., Branton D. Clathrin-coated vesicles contain two protein kinase activities. Phosphorylation of clathrin beta-light chain by casein kinase II. J.Biol. Chem. 1986, 261:9614-9621.
    • (1986) J.Biol. Chem. , vol.261 , pp. 9614-9621
    • Bar-Zvi, D.1    Branton, D.2
  • 3
    • 0034640476 scopus 로고    scopus 로고
    • Identification and characterization of CKIP-1, a novel pleckstrin homology domain-containing protein that interacts with protein kinase CK2
    • Bosc D.G., Graham K.C., Saulnier R.B., Zhang C., Prober D., Gietz R.D., Litchfield D.W. Identification and characterization of CKIP-1, a novel pleckstrin homology domain-containing protein that interacts with protein kinase CK2. J.Biol. Chem. 2000, 275:14295-14306.
    • (2000) J.Biol. Chem. , vol.275 , pp. 14295-14306
    • Bosc, D.G.1    Graham, K.C.2    Saulnier, R.B.3    Zhang, C.4    Prober, D.5    Gietz, R.D.6    Litchfield, D.W.7
  • 4
    • 30644470506 scopus 로고    scopus 로고
    • Sjl2p is specifically involved in early steps of endocytosis intimately linked to actin dynamics via the Ark1p/Prk1p kinases
    • Böttcher C., Wicky S., Schwarz H., Singer-Krüger B. Sjl2p is specifically involved in early steps of endocytosis intimately linked to actin dynamics via the Ark1p/Prk1p kinases. FEBS Lett. 2006, 580:633-641.
    • (2006) FEBS Lett. , vol.580 , pp. 633-641
    • Böttcher, C.1    Wicky, S.2    Schwarz, H.3    Singer-Krüger, B.4
  • 5
    • 79751494449 scopus 로고    scopus 로고
    • Synaptojanin 1-mediated PI(4,5)P2 hydrolysis is modulated by membrane curvature and facilitates membrane fission
    • Chang-Ileto B., Frere S.G., Chan R.B., Voronov S.V., Roux A., Di Paolo G. Synaptojanin 1-mediated PI(4,5)P2 hydrolysis is modulated by membrane curvature and facilitates membrane fission. Dev. Cell 2011, 20:206-218.
    • (2011) Dev. Cell , vol.20 , pp. 206-218
    • Chang-Ileto, B.1    Frere, S.G.2    Chan, R.B.3    Voronov, S.V.4    Roux, A.5    Di Paolo, G.6
  • 7
    • 0038392873 scopus 로고    scopus 로고
    • Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP
    • Cory G.O., Cramer R., Blanchoin L., Ridley A.J. Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP. Mol. Cell 2003, 11:1229-1239.
    • (2003) Mol. Cell , vol.11 , pp. 1229-1239
    • Cory, G.O.1    Cramer, R.2    Blanchoin, L.3    Ridley, A.J.4
  • 8
    • 0032746494 scopus 로고    scopus 로고
    • Casein kinase II activity is required for transferrin receptor endocytosis
    • Cotlin L.F., Siddiqui M.A., Simpson F., Collawn J.F. Casein kinase II activity is required for transferrin receptor endocytosis. J.Biol. Chem. 1999, 274:30550-30556.
    • (1999) J.Biol. Chem. , vol.274 , pp. 30550-30556
    • Cotlin, L.F.1    Siddiqui, M.A.2    Simpson, F.3    Collawn, J.F.4
  • 10
    • 76549123909 scopus 로고    scopus 로고
    • Generation of branched actin networks: assembly and regulation of the N-WASP and WAVE molecular machines
    • Derivery E., Gautreau A. Generation of branched actin networks: assembly and regulation of the N-WASP and WAVE molecular machines. BioEssays 2010, 32:119-131.
    • (2010) BioEssays , vol.32 , pp. 119-131
    • Derivery, E.1    Gautreau, A.2
  • 12
    • 33748053027 scopus 로고    scopus 로고
    • Nerve growth factor-induced phosphorylation of amphiphysin-1 by casein kinase 2 regulates clathrin-amphiphysin interactions
    • Döring M., Loos A., Schrader N., Pfander B., Bauerfeind R. Nerve growth factor-induced phosphorylation of amphiphysin-1 by casein kinase 2 regulates clathrin-amphiphysin interactions. J.Neurochem. 2006, 98:2013-2022.
    • (2006) J.Neurochem. , vol.98 , pp. 2013-2022
    • Döring, M.1    Loos, A.2    Schrader, N.3    Pfander, B.4    Bauerfeind, R.5
  • 14
    • 38949214078 scopus 로고    scopus 로고
    • Distinct roles for Arp2/3 regulators in actin assembly and endocytosis
    • Galletta B.J., Chuang D.Y., Cooper J.A. Distinct roles for Arp2/3 regulators in actin assembly and endocytosis. PLoS Biol. 2008, 6:e1.
    • (2008) PLoS Biol. , vol.6 , pp. e1
    • Galletta, B.J.1    Chuang, D.Y.2    Cooper, J.A.3
  • 15
    • 79958139511 scopus 로고    scopus 로고
    • Interplay between N-WASP and CK2 optimizes clathrin-mediated endocytosis of EGFR
    • Galovic M., Xu D., Areces L.B., van der Kammen R., Innocenti M. Interplay between N-WASP and CK2 optimizes clathrin-mediated endocytosis of EGFR. J.Cell Sci. 2011, 124:2001-2012.
    • (2011) J.Cell Sci. , vol.124 , pp. 2001-2012
    • Galovic, M.1    Xu, D.2    Areces, L.B.3    van der Kammen, R.4    Innocenti, M.5
  • 16
    • 0034663930 scopus 로고    scopus 로고
    • An intact SH3 domain is required for myosin I-induced actin polymerization
    • Geli M.I., Lombardi R., Schmelzl B., Riezman H. An intact SH3 domain is required for myosin I-induced actin polymerization. EMBO J. 2000, 19:4281-4291.
    • (2000) EMBO J. , vol.19 , pp. 4281-4291
    • Geli, M.I.1    Lombardi, R.2    Schmelzl, B.3    Riezman, H.4
  • 17
    • 0023864673 scopus 로고
    • Brain coated vesicle destabilization and phosphorylation of coat proteins
    • Georgieva-Hanson V., Schook W.J., Puszkin S. Brain coated vesicle destabilization and phosphorylation of coat proteins. J.Neurochem. 1988, 50:307-315.
    • (1988) J.Neurochem. , vol.50 , pp. 307-315
    • Georgieva-Hanson, V.1    Schook, W.J.2    Puszkin, S.3
  • 18
    • 68549085023 scopus 로고    scopus 로고
    • High-accuracy identification and bioinformatic analysis of invivo protein phosphorylation sites in yeast
    • Gnad F., de Godoy L.M., Cox J., Neuhauser N., Ren S., Olsen J.V., Mann M. High-accuracy identification and bioinformatic analysis of invivo protein phosphorylation sites in yeast. Proteomics 2009, 9:4642-4652.
    • (2009) Proteomics , vol.9 , pp. 4642-4652
    • Gnad, F.1    de Godoy, L.M.2    Cox, J.3    Neuhauser, N.4    Ren, S.5    Olsen, J.V.6    Mann, M.7
  • 20
    • 0027437850 scopus 로고
    • Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2
    • Gyuris J., Golemis E., Chertkov H., Brent R. Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell 1993, 75:791-803.
    • (1993) Cell , vol.75 , pp. 791-803
    • Gyuris, J.1    Golemis, E.2    Chertkov, H.3    Brent, R.4
  • 21
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification
    • Hanks S.K., Hunter T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 1995, 9:576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 22
    • 0028805890 scopus 로고
    • Casein kinase II is required for cell cycle progression during G1 and G2/M in Saccharomyces cerevisiae
    • Hanna D.E., Rethinaswamy A., Glover C.V. Casein kinase II is required for cell cycle progression during G1 and G2/M in Saccharomyces cerevisiae. J.Biol. Chem. 1995, 270:25905-25914.
    • (1995) J.Biol. Chem. , vol.270 , pp. 25905-25914
    • Hanna, D.E.1    Rethinaswamy, A.2    Glover, C.V.3
  • 23
    • 0033529507 scopus 로고    scopus 로고
    • AP180 and AP-2 interact directly in a complex that cooperatively assembles clathrin
    • Hao W., Luo Z., Zheng L., Prasad K., Lafer E.M. AP180 and AP-2 interact directly in a complex that cooperatively assembles clathrin. J.Biol. Chem. 1999, 274:22785-22794.
    • (1999) J.Biol. Chem. , vol.274 , pp. 22785-22794
    • Hao, W.1    Luo, Z.2    Zheng, L.3    Prasad, K.4    Lafer, E.M.5
  • 24
    • 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., Morgan D.O. Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 2009, 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
  • 25
    • 0036856301 scopus 로고    scopus 로고
    • Cofilin, but not profilin, is required for myosin-I-induced actin polymerization and the endocytic uptake in yeast
    • Idrissi F.Z., Wolf B.L., Geli M.I. Cofilin, but not profilin, is required for myosin-I-induced actin polymerization and the endocytic uptake in yeast. Mol. Biol. Cell 2002, 13:4074-4087.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4074-4087
    • Idrissi, F.Z.1    Wolf, B.L.2    Geli, M.I.3
  • 27
    • 84866840094 scopus 로고    scopus 로고
    • Ultrastructural dynamics of proteins involved in endocytic budding
    • Idrissi F.Z., Blasco A., Espinal A., Geli M.I. Ultrastructural dynamics of proteins involved in endocytic budding. Proc. Natl. Acad. Sci. USA 2012, 109:E2587-E2594.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. E2587-E2594
    • Idrissi, F.Z.1    Blasco, A.2    Espinal, A.3    Geli, M.I.4
  • 28
    • 33748288113 scopus 로고    scopus 로고
    • BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature
    • Itoh T., De Camilli P. BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. Biochim. Biophys. Acta 2006, 1761:897-912.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 897-912
    • Itoh, T.1    De Camilli, P.2
  • 29
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • Kaksonen M., Sun Y., Drubin D.G. A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 2003, 115:475-487.
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 30
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin- and actin-mediated endocytosis machinery
    • Kaksonen M., Toret C.P., Drubin D.G. A modular design for the clathrin- and actin-mediated endocytosis machinery. Cell 2005, 123:305-320.
    • (2005) Cell , vol.123 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 33
    • 0036300863 scopus 로고    scopus 로고
    • CK2 and GAK/auxilin2 are major protein kinases in clathrin-coated vesicles
    • Korolchuk V.I., Banting G. CK2 and GAK/auxilin2 are major protein kinases in clathrin-coated vesicles. Traffic 2002, 3:428-439.
    • (2002) Traffic , vol.3 , pp. 428-439
    • Korolchuk, V.I.1    Banting, G.2
  • 34
    • 28844483671 scopus 로고    scopus 로고
    • Regulation of CK2 activity by phosphatidylinositol phosphates
    • Korolchuk V.I., Cozier G., Banting G. Regulation of CK2 activity by phosphatidylinositol phosphates. J.Biol. Chem. 2005, 280:40796-40801.
    • (2005) J.Biol. Chem. , vol.280 , pp. 40796-40801
    • Korolchuk, V.I.1    Cozier, G.2    Banting, G.3
  • 35
    • 34248209063 scopus 로고    scopus 로고
    • Phosphoinositides: regulators of membrane traffic and protein function
    • Krauss M., Haucke V. Phosphoinositides: regulators of membrane traffic and protein function. FEBS Lett. 2007, 581:2105-2111.
    • (2007) FEBS Lett. , vol.581 , pp. 2105-2111
    • Krauss, M.1    Haucke, V.2
  • 36
    • 78651270028 scopus 로고    scopus 로고
    • Correlated fluorescence and 3D electron microscopy with high sensitivity and spatial precision
    • Kukulski W., Schorb M., Welsch S., Picco A., Kaksonen M., Briggs J.A. Correlated fluorescence and 3D electron microscopy with high sensitivity and spatial precision. J.Cell Biol. 2011, 192:111-119.
    • (2011) J.Cell Biol. , vol.192 , pp. 111-119
    • Kukulski, W.1    Schorb, M.2    Welsch, S.3    Picco, A.4    Kaksonen, M.5    Briggs, J.A.6
  • 37
    • 84864592255 scopus 로고    scopus 로고
    • Plasma membrane reshaping during endocytosis is revealed by time-resolved electron tomography
    • Kukulski W., Schorb M., Kaksonen M., Briggs J.A. Plasma membrane reshaping during endocytosis is revealed by time-resolved electron tomography. Cell 2012, 150:508-520.
    • (2012) Cell , vol.150 , pp. 508-520
    • Kukulski, W.1    Schorb, M.2    Kaksonen, M.3    Briggs, J.A.4
  • 38
    • 0034707580 scopus 로고    scopus 로고
    • Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization
    • Lechler T., Shevchenko A., Li R. Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J.Cell Biol. 2000, 148:363-373.
    • (2000) J.Cell Biol. , vol.148 , pp. 363-373
    • Lechler, T.1    Shevchenko, A.2    Li, R.3
  • 39
    • 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
    • Lechler T., Jonsdottir G.A., Klee S.K., Pellman D., Li R. A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast. J.Cell Biol. 2001, 155:261-270.
    • (2001) J.Cell Biol. , vol.155 , pp. 261-270
    • Lechler, T.1    Jonsdottir, G.A.2    Klee, S.K.3    Pellman, D.4    Li, R.5
  • 41
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: structure, regulation and role in cellular decisions of life and death
    • Litchfield D.W. Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem. J. 2003, 369:1-15.
    • (2003) Biochem. J. , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 43
    • 69249208824 scopus 로고    scopus 로고
    • Verprolin: a cool set of actin-binding sites and some very HOT prolines
    • Munn A.L., Thanabalu T. Verprolin: a cool set of actin-binding sites and some very HOT prolines. IUBMB Life 2009, 61:707-712.
    • (2009) IUBMB Life , vol.61 , pp. 707-712
    • Munn, A.L.1    Thanabalu, T.2
  • 44
    • 78049288556 scopus 로고    scopus 로고
    • Structural basis of the constitutive activity of protein kinase CK2
    • Olsen B.B., Guerra B., Niefind K., Issinger O.G. Structural basis of the constitutive activity of protein kinase CK2. Methods Enzymol. 2010, 484:515-529.
    • (2010) Methods Enzymol. , vol.484 , pp. 515-529
    • Olsen, B.B.1    Guerra, B.2    Niefind, K.3    Issinger, O.G.4
  • 45
    • 4744338740 scopus 로고    scopus 로고
    • The Pleckstrin homology domain of CK2 interacting protein-1 is required for interactions and recruitment of protein kinase CK2 to the plasma membrane
    • Olsten M.E., Canton D.A., Zhang C., Walton P.A., Litchfield D.W. The Pleckstrin homology domain of CK2 interacting protein-1 is required for interactions and recruitment of protein kinase CK2 to the plasma membrane. J.Biol. Chem. 2004, 279:42114-42127.
    • (2004) J.Biol. Chem. , vol.279 , pp. 42114-42127
    • Olsten, M.E.1    Canton, D.A.2    Zhang, C.3    Walton, P.A.4    Litchfield, D.W.5
  • 46
    • 0025281150 scopus 로고
    • Isolation, sequencing, and disruption of the yeast CKA2 gene: casein kinase II is essential for viability in Saccharomyces cerevisiae
    • Padmanabha R., Chen-Wu J.L., Hanna D.E., Glover C.V. Isolation, sequencing, and disruption of the yeast CKA2 gene: casein kinase II is essential for viability in Saccharomyces cerevisiae. Mol. Cell. Biol. 1990, 10:4089-4099.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4089-4099
    • Padmanabha, R.1    Chen-Wu, J.L.2    Hanna, D.E.3    Glover, C.V.4
  • 47
    • 58149333848 scopus 로고    scopus 로고
    • WAVE2 is regulated by multiple phosphorylation events within its VCA domain
    • Pocha S.M., Cory G.O. WAVE2 is regulated by multiple phosphorylation events within its VCA domain. Cell Motil. Cytoskeleton 2009, 66:36-47.
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 36-47
    • Pocha, S.M.1    Cory, G.O.2
  • 48
    • 0032489364 scopus 로고    scopus 로고
    • Temperature-sensitive mutations of the CKA1 gene reveal a role for casein kinase II in maintenance of cell polarity in Saccharomyces cerevisiae
    • Rethinaswamy A., Birnbaum M.J., Glover C.V. Temperature-sensitive mutations of the CKA1 gene reveal a role for casein kinase II in maintenance of cell polarity in Saccharomyces cerevisiae. J.Biol. Chem. 1998, 273:5869-5877.
    • (1998) J.Biol. Chem. , vol.273 , pp. 5869-5877
    • Rethinaswamy, A.1    Birnbaum, M.J.2    Glover, C.V.3
  • 50
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate
    • Rohatgi R., Ho H.Y., Kirschner M.W. Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate. J.Cell Biol. 2000, 150:1299-1310.
    • (2000) J.Cell Biol. , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 51
    • 0032557824 scopus 로고    scopus 로고
    • The tight association of protein kinase CK2 with plasma membranes is mediated by a specific domain of its regulatory beta-subunit
    • Sarrouilhe D., Filhol O., Leroy D., Bonello G., Baudry M., Chambaz E.M., Cochet C. The tight association of protein kinase CK2 with plasma membranes is mediated by a specific domain of its regulatory beta-subunit. Biochim. Biophys. Acta 1998, 1403:199-210.
    • (1998) Biochim. Biophys. Acta , vol.1403 , pp. 199-210
    • Sarrouilhe, D.1    Filhol, O.2    Leroy, D.3    Bonello, G.4    Baudry, M.5    Chambaz, E.M.6    Cochet, C.7
  • 52
    • 0024227621 scopus 로고
    • H+-ATPase from plasma membranes of Saccharomyces cerevisiae and Avena sativa roots: purification and reconstitution
    • Serrano R. H+-ATPase from plasma membranes of Saccharomyces cerevisiae and Avena sativa roots: purification and reconstitution. Methods Enzymol. 1988, 157:533-544.
    • (1988) Methods Enzymol. , vol.157 , pp. 533-544
    • Serrano, R.1
  • 53
  • 54
    • 0032493929 scopus 로고    scopus 로고
    • Role of phosphorylation in regulation of the assembly of endocytic coat complexes
    • Slepnev V.I., Ochoa G.C., Butler M.H., Grabs D., De Camilli P. Role of phosphorylation in regulation of the assembly of endocytic coat complexes. Science 1998, 281:821-824.
    • (1998) Science , vol.281 , pp. 821-824
    • Slepnev, V.I.1    Ochoa, G.C.2    Butler, M.H.3    Grabs, D.4    De Camilli, P.5
  • 55
    • 0036181710 scopus 로고    scopus 로고
    • The yeast synaptojanin-like proteins control the cellular distribution of phosphatidylinositol (4,5)-bisphosphate
    • 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 2002, 13:542-557.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 542-557
    • Stefan, C.J.1    Audhya, A.2    Emr, S.D.3
  • 56
    • 16244404272 scopus 로고    scopus 로고
    • The phosphoinositide phosphatase Sjl2 is recruited to cortical actin patches in the control of vesicle formation and fission during endocytosis
    • Stefan C.J., Padilla S.M., Audhya A., Emr S.D. The phosphoinositide phosphatase Sjl2 is recruited to cortical actin patches in the control of vesicle formation and fission during endocytosis. Mol. Cell. Biol. 2005, 25:2910-2923.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2910-2923
    • Stefan, C.J.1    Padilla, S.M.2    Audhya, A.3    Emr, S.D.4
  • 57
    • 33745535568 scopus 로고    scopus 로고
    • Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity
    • Sun Y., Martin A.C., Drubin D.G. Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity. Dev. Cell 2006, 11:33-46.
    • (2006) Dev. Cell , vol.11 , pp. 33-46
    • Sun, Y.1    Martin, A.C.2    Drubin, D.G.3
  • 58
    • 34247526437 scopus 로고    scopus 로고
    • PtdIns(4,5)P2 turnover is required for multiple stages during clathrin- and actin-dependent endocytic internalization
    • Sun Y., Carroll S., Kaksonen M., Toshima J.Y., Drubin D.G. PtdIns(4,5)P2 turnover is required for multiple stages during clathrin- and actin-dependent endocytic internalization. J.Cell Biol. 2007, 177:355-367.
    • (2007) J.Cell Biol. , vol.177 , pp. 355-367
    • Sun, Y.1    Carroll, S.2    Kaksonen, M.3    Toshima, J.Y.4    Drubin, D.G.5
  • 59
    • 41849145402 scopus 로고    scopus 로고
    • Multiple pathways regulate endocytic coat disassembly in Saccharomyces cerevisiae for optimal downstream trafficking
    • Toret C.P., Lee L., Sekiya-Kawasaki M., Drubin D.G. Multiple pathways regulate endocytic coat disassembly in Saccharomyces cerevisiae for optimal downstream trafficking. Traffic 2008, 9:848-859.
    • (2008) Traffic , vol.9 , pp. 848-859
    • Toret, C.P.1    Lee, L.2    Sekiya-Kawasaki, M.3    Drubin, D.G.4
  • 60
    • 0029825766 scopus 로고    scopus 로고
    • Invivo phosphorylation of adaptors regulates their interaction with clathrin
    • Wilde A., Brodsky F.M. Invivo phosphorylation of adaptors regulates their interaction with clathrin. J.Cell Biol. 1996, 135:635-645.
    • (1996) J.Cell Biol. , vol.135 , pp. 635-645
    • Wilde, A.1    Brodsky, F.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.