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Volumn 17, Issue 10, 2006, Pages 4343-4352

Novel function of clathrin light chain in promoting endocytic vesicle formation

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; CLATHRIN HEAVY CHAIN; CLATHRIN LIGHT CHAIN; PROTEIN SLA2P; UNCLASSIFIED DRUG;

EID: 33749469698     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-07-0606     Document Type: Article
Times cited : (40)

References (33)
  • 1
    • 0346731278 scopus 로고    scopus 로고
    • The Sla2p talin domain plays a role in endocytosis in Saccharomyces cerevisiae
    • Baggett, J. J., D'Aquino, K. E., and Wendland, B. (2003). The Sla2p talin domain plays a role in endocytosis in Saccharomyces cerevisiae. Genetics 165, 1661-1674.
    • (2003) Genetics , vol.165 , pp. 1661-1674
    • Baggett, J.J.1    D'Aquino, K.E.2    Wendland, B.3
  • 3
    • 14044275140 scopus 로고    scopus 로고
    • Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R) bind the conserved sequence of clathrin light chains and thereby influence clathrin assembly in vitro and actin distribution in vivo
    • Chen, C. Y., and Brodsky, F. M. (2005). Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R) bind the conserved sequence of clathrin light chains and thereby influence clathrin assembly in vitro and actin distribution in vivo. J. Biol. Chem. 280, 6109-6117.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6109-6117
    • Chen, C.Y.1    Brodsky, F.M.2
  • 4
    • 18744400775 scopus 로고    scopus 로고
    • Clathrin light and heavy chain interface: Alpha-helix binding super-helix loops via critical tryptophans
    • Chen, C. Y., Reese, M. L., Hwang, P. K., Ota, N., Agard, D., and Brodsky, F. M. (2002). Clathrin light and heavy chain interface: alpha-helix binding super-helix loops via critical tryptophans. EMBO J. 21, 6072-6082.
    • (2002) EMBO J. , vol.21 , pp. 6072-6082
    • Chen, C.Y.1    Reese, M.L.2    Hwang, P.K.3    Ota, N.4    Agard, D.5    Brodsky, F.M.6
  • 5
    • 12644297393 scopus 로고    scopus 로고
    • The light chain subunit is required for clathrin function in Saccharomyces cerevisiae
    • Chu, D. S., Pishvaee, B., and Payne, G. S. (1996). The light chain subunit is required for clathrin function in Saccharomyces cerevisiae. J. Biol. Chem. 271, 33123-33130.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33123-33130
    • Chu, D.S.1    Pishvaee, B.2    Payne, G.S.3
  • 7
    • 0033611051 scopus 로고    scopus 로고
    • An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles
    • Engqvist-Goldstein, A. E., Kessels, M. M., Chopra, V. S., Hayden, M. R., and Drubin, D. G. (1999). An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles. J. Cell Biol. 147, 1503-1518.
    • (1999) J. Cell Biol. , vol.147 , pp. 1503-1518
    • Engqvist-Goldstein, A.E.1    Kessels, M.M.2    Chopra, V.S.3    Hayden, M.R.4    Drubin, D.G.5
  • 8
    • 0035904239 scopus 로고    scopus 로고
    • The actin-binding protein Hip1R associates with clathrin during early stages of endocytosis and promotes clathrin assembly in vitro
    • Engqvist-Goldstein, A. E., Warren, R. A., Kessels, M. M., Keen, J. H., Heuser, J., and Drubin, D. G. (2001). The actin-binding protein Hip1R associates with clathrin during early stages of endocytosis and promotes clathrin assembly in vitro. J. Cell Biol. 154, 1209-1223.
    • (2001) J. Cell Biol. , vol.154 , pp. 1209-1223
    • Engqvist-Goldstein, A.E.1    Warren, R.A.2    Kessels, M.M.3    Keen, J.H.4    Heuser, J.5    Drubin, D.G.6
  • 10
    • 0036679002 scopus 로고    scopus 로고
    • Scd5p and clathrin function are important for cortical actin organization, endocytosis, and localization of Sla2p in yeast
    • Henry, K. R., D'Hondt, K., Chang, J., Newpher, T., Huang, K., Hudson, R. T., Riezman, H., and Lemmon, S. K. (2002). Scd5p and clathrin function are important for cortical actin organization, endocytosis, and localization of Sla2p in yeast. Mol. Biol. Cell 13, 2607-2625.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2607-2625
    • Henry, K.R.1    D'Hondt, K.2    Chang, J.3    Newpher, T.4    Huang, K.5    Hudson, R.T.6    Riezman, H.7    Lemmon, S.K.8
  • 11
    • 0030975677 scopus 로고    scopus 로고
    • Novel functions of clathrin light chains: Clathrin heavy chain trimerization is defective in light chain-deficient yeast
    • Huang, K. M., Gullberg, L., Nelson, K. K., Stefan, C. J., Blumer, K., and Lemmon, S. K. (1997). Novel functions of clathrin light chains: clathrin heavy chain trimerization is defective in light chain-deficient yeast. J. Cell Sci. 110 (Pt 7), 899-910.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 7 , pp. 899-910
    • Huang, K.M.1    Gullberg, L.2    Nelson, K.K.3    Stefan, C.J.4    Blumer, K.5    Lemmon, S.K.6
  • 13
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • 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.
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 14
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin- and actin-mediated endocytosis machinery
    • 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.
    • (2005) Cell , vol.123 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 15
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • Kaksonen, M., Toret, C. P., and Drubin, D. G. (2006). Harnessing actin dynamics for clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 7, 404-414.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 16
    • 0037205440 scopus 로고    scopus 로고
    • HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. Identification of a novel interaction with clathrin light chain
    • Legendre-Guillemin, V., Metzler, M., Charbonneau, M., Gan, L., Chopra, V., Philie, J., Hayden, M. R., and McPherson, P. S. (2002). HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. Identification of a novel interaction with clathrin light chain. J. Biol. Chem. 277, 19897-19904.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19897-19904
    • Legendre-Guillemin, V.1    Metzler, M.2    Charbonneau, M.3    Gan, L.4    Chopra, V.5    Philie, J.6    Hayden, M.R.7    McPherson, P.S.8
  • 17
    • 14044265129 scopus 로고    scopus 로고
    • Huntingtin interacting protein 1 (HIP1) regulates clathrin assembly through direct binding to the regulatory region of the clathrin light chain
    • Legendre-Guillemin, V., Metzler, M., Lemaire, J. F., Philie, J., Gan, L., Hayden, M. R., and McPherson, P. S. (2005). Huntingtin interacting protein 1 (HIP1) regulates clathrin assembly through direct binding to the regulatory region of the clathrin light chain. J. Biol. Chem. 280, 6101-6108.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6101-6108
    • Legendre-Guillemin, V.1    Metzler, M.2    Lemaire, J.F.3    Philie, J.4    Gan, L.5    Hayden, M.R.6    McPherson, P.S.7
  • 18
    • 0023986504 scopus 로고
    • Characterization of yeast clathrin and anticlathrin heavy-chain monoclonal antibodies
    • Lemmon, S., Lemmon, V. P., and Jones, E. W. (1988). Characterization of yeast clathrin and anticlathrin heavy-chain monoclonal antibodies. J. Cell. Biochem. 36, 329-340.
    • (1988) J. Cell. Biochem. , vol.36 , pp. 329-340
    • Lemmon, S.1    Lemmon, V.P.2    Jones, E.W.3
  • 19
    • 0023663065 scopus 로고
    • Clathrin requirement for normal growth of yeast
    • Lemmon, S. K., and Jones, E. W. (1987). Clathrin requirement for normal growth of yeast. Science 238, 504-509.
    • (1987) Science , vol.238 , pp. 504-509
    • Lemmon, S.K.1    Jones, E.W.2
  • 20
    • 0028858382 scopus 로고
    • Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs
    • Liu, S. H., Wong, M. L., Craik, C. S., and Brodsky, F. M. (1995). Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs. Cell 83, 257-267.
    • (1995) Cell , vol.83 , pp. 257-267
    • Liu, S.H.1    Wong, M.L.2    Craik, C.S.3    Brodsky, F.M.4
  • 21
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., McKenzie, A., 3rd, Demarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippsen, P., and Pringle, J. R. (1998). Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 22
    • 0030908297 scopus 로고    scopus 로고
    • The I/LWEQ module: A conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals
    • McCann, R. O., and Craig, S. W. (1997). The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc. Natl. Acad. Sci. USA 94, 5679-5684.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5679-5684
    • McCann, R.O.1    Craig, S.W.2
  • 23
    • 0027390598 scopus 로고
    • Suppressors of clathrin deficiency: Overexpression of ubiquitin rescues lethal strains of clathrin-deficient Saccharomyces cerevisiae
    • Nelson, K. K., and Lemmon, S. K. (1993). Suppressors of clathrin deficiency: overexpression of ubiquitin rescues lethal strains of clathrin-deficient Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 521-532.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 521-532
    • Nelson, K.K.1    Lemmon, S.K.2
  • 24
    • 33745757008 scopus 로고    scopus 로고
    • Clathrin is important for normal actin dynamics and progression of Sla2p-containing patches during endocytosis in yeast
    • Newpher, T. M., and Lemmon, S. K. (2006). Clathrin is important for normal actin dynamics and progression of Sla2p-containing patches during endocytosis in yeast. Traffic 7, 574-588.
    • (2006) Traffic , vol.7 , pp. 574-588
    • Newpher, T.M.1    Lemmon, S.K.2
  • 25
    • 21344469702 scopus 로고    scopus 로고
    • In vivo dynamics of clathrin and its adaptor-dependent recruitment to the actin-based endocytic machinery in yeast
    • Newpher, T. M., Smith, R. P., Lemmon, V., and Lemmon, S. K. (2005). In vivo dynamics of clathrin and its adaptor-dependent recruitment to the actin-based endocytic machinery in yeast. Dev. Cell 9, 87-98.
    • (2005) Dev. Cell , vol.9 , pp. 87-98
    • Newpher, T.M.1    Smith, R.P.2    Lemmon, V.3    Lemmon, S.K.4
  • 26
    • 0024454653 scopus 로고
    • Clathrin: A role in the intracellular retention of a Golgi membrane protein
    • Payne, G. S., and Schekman, R. (1989). Clathrin: a role in the intracellular retention of a Golgi membrane protein. Science 245, 1358-1365.
    • (1989) Science , vol.245 , pp. 1358-1365
    • Payne, G.S.1    Schekman, R.2
  • 27
    • 0025254061 scopus 로고
    • Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3
    • Scarmato, P., and Kirchhausen, T. (1990). Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3. J. Biol. Chem. 265, 3661-3668.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3661-3668
    • Scarmato, P.1    Kirchhausen, T.2
  • 28
    • 10644221869 scopus 로고    scopus 로고
    • Intrasteric inhibition mediates the interaction of the I/LWEQ module proteins Talin1, Talin2, Hip1, and Hip12 with actin
    • Senetar, M. A., Foster, S. J., and McCann, R. O. (2004). Intrasteric inhibition mediates the interaction of the I/LWEQ module proteins Talin1, Talin2, Hip1, and Hip12 with actin. Biochemistry 43, 15418-15428.
    • (2004) Biochemistry , vol.43 , pp. 15418-15428
    • Senetar, M.A.1    Foster, S.J.2    McCann, R.O.3
  • 29
    • 12844261584 scopus 로고    scopus 로고
    • Interaction of Sla2p's ANTH domain with PtdIns(4,5)P2 is important for actin-dependent endocytic internalization
    • Sun, Y., Kaksonen, M., Madden, D. T., Schekman, R., and Drubin, D. G. (2005). Interaction of Sla2p's ANTH domain with PtdIns(4,5)P2 is important for actin-dependent endocytic internalization. Mol. Biol. Cell 16, 717-730.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 717-730
    • Sun, Y.1    Kaksonen, M.2    Madden, D.T.3    Schekman, R.4    Drubin, D.G.5
  • 30
    • 33645801592 scopus 로고    scopus 로고
    • Spatial dynamics of receptor-mediated endocytic trafficking in budding yeast revealed by using fluorescent alpha-factor derivatives
    • Toshima, J. Y., Toshima, J., Kaksonen, M., Martin, A. C., King, D. S., and Drubin, D. G. (2006). Spatial dynamics of receptor-mediated endocytic trafficking in budding yeast revealed by using fluorescent alpha-factor derivatives. Proc. Natl. Acad. Sci. USA 103, 5793-5798.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5793-5798
    • Toshima, J.Y.1    Toshima, J.2    Kaksonen, M.3    Martin, A.C.4    King, D.S.5    Drubin, D.G.6
  • 31
    • 0025900858 scopus 로고
    • Bovine brain clathrin light chains impede heavy chain assembly in vitro
    • Ungewickell, E., and Ungewickell, H. (1991). Bovine brain clathrin light chains impede heavy chain assembly in vitro. J. Biol. Chem. 266, 12710-12714.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12710-12714
    • Ungewickell, E.1    Ungewickell, H.2
  • 32
    • 0032589216 scopus 로고    scopus 로고
    • Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals
    • Yang, S., Cope, M. J., and Drubin, D. G. (1999). Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals. Mol. Biol. Cell 10, 2265-2283.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2265-2283
    • Yang, S.1    Cope, M.J.2    Drubin, D.G.3
  • 33
    • 0032473362 scopus 로고    scopus 로고
    • Clathrin self-assembly is regulated by three light-chain residues controlling the formation of critical salt bridges
    • Ybe, J. A., Greene, B., Liu, S. H., Pley, U., Parham, P., and Brodsky, F. M. (1998). Clathrin self-assembly is regulated by three light-chain residues controlling the formation of critical salt bridges. EMBO J. 17, 1297-1303.
    • (1998) EMBO J. , vol.17 , pp. 1297-1303
    • Ybe, J.A.1    Greene, B.2    Liu, S.H.3    Pley, U.4    Parham, P.5    Brodsky, F.M.6


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