메뉴 건너뛰기




Volumn 10, Issue 11, 1999, Pages 3643-3659

Adaptor complex-independent clathrin function in yeast

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CLATHRIN;

EID: 0032744490     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.11.3643     Document Type: Article
Times cited : (124)

References (82)
  • 1
    • 0345012707 scopus 로고
    • Structural relationships between clathrin assembly proteins from the Golgi and the plasma membrane
    • Ahle, S., Mann, A., Eichelsbacher, U., and Ungewickell, E. (1988). Structural relationships between clathrin assembly proteins from the Golgi and the plasma membrane. EMBO J. 7, 919-929.
    • (1988) EMBO J. , vol.7 , pp. 919-929
    • Ahle, S.1    Mann, A.2    Eichelsbacher, U.3    Ungewickell, E.4
  • 3
    • 0029615380 scopus 로고
    • The tyrosine kinase substrate eps15 is constitutively associated with the plasma membrane adaptor AP-2
    • Benmerah, A., Gagnon, J., Begue, B., Megarbane, B., Dautry-Varsat, A., and Cerf-Bensussan, N. (1995). The tyrosine kinase substrate eps15 is constitutively associated with the plasma membrane adaptor AP-2. J. Cell Biol. 131, 1831-1838.
    • (1995) J. Cell Biol. , vol.131 , pp. 1831-1838
    • Benmerah, A.1    Gagnon, J.2    Begue, B.3    Megarbane, B.4    Dautry-Varsat, A.5    Cerf-Bensussan, N.6
  • 4
    • 0031911736 scopus 로고    scopus 로고
    • Vacuole biogenesis in saccharomyces cerevisiae: Protein transport pathways to the yeast vacuole
    • Bryant, N.J., and Stevens, T.H. (1998). Vacuole biogenesis in Saccharomyces cerevisiae: protein transport pathways to the yeast vacuole. Microbiol. Mol. Biol. Rev. 62, 230-247.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 230-247
    • Bryant, N.J.1    Stevens, T.H.2
  • 5
    • 0019551730 scopus 로고
    • "Western blotting": Electrophoretic transfer of proteins from SDS-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, W.N. (1981). "Western blotting": electrophoretic transfer of proteins from SDS-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112, 195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 6
    • 0025815340 scopus 로고
    • Purification and in vitro translocation of chemical amounts of prepro-α-factor
    • Bush, G.L., Friden, H., and Meyer, D.I. (1991). Purification and in vitro translocation of chemical amounts of prepro-α-factor. J. Biol. Chem. 266, 13811-13814.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13811-13814
    • Bush, G.L.1    Friden, H.2    Meyer, D.I.3
  • 8
    • 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
  • 9
    • 0032935411 scopus 로고    scopus 로고
    • A modulatory role for clathrin light chain phosphorylation in Golgi membrane protein localization during vegetative growth and during the mating response of Saccharomyces cerevisiae
    • Chu, D.S., Pishvaee, B., and Payne, G.S. (1999). A modulatory role for clathrin light chain phosphorylation in Golgi membrane protein localization during vegetative growth and during the mating response of Saccharomyces cerevisiae. Mol. Biol. Cell 10, 713-726.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 713-726
    • Chu, D.S.1    Pishvaee, B.2    Payne, G.S.3
  • 10
    • 0030886261 scopus 로고    scopus 로고
    • The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole
    • Cowles, C.R., Odorizzi, G., Payne, G.S., and Emr, S.D. (1997a). The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole. Cell 91, 109-118.
    • (1997) Cell , vol.91 , pp. 109-118
    • Cowles, C.R.1    Odorizzi, G.2    Payne, G.S.3    Emr, S.D.4
  • 11
    • 0030962901 scopus 로고    scopus 로고
    • Novel Golgi to vacuole delivery pathway in yeast: Identification of a sorting determinant and required transport component
    • Cowles, C.R., Snyder, W.B., Burd, C.G., and Emr, S.D. (1997b). Novel Golgi to vacuole delivery pathway in yeast: identification of a sorting determinant and required transport component. EMBO J. 16, 2769-2782.
    • (1997) EMBO J. , vol.16 , pp. 2769-2782
    • Cowles, C.R.1    Snyder, W.B.2    Burd, C.G.3    Emr, S.D.4
  • 12
    • 0030060326 scopus 로고    scopus 로고
    • A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals
    • David, C., McPherson, P.S., Mundigl, O., and de Camilli, P. (1996). A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals. Proc. Natl. Acad. Sci. USA 93, 331-335.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 331-335
    • David, C.1    McPherson, P.S.2    Mundigl, O.3    De Camilli, P.4
  • 13
    • 0027175829 scopus 로고
    • Cis- and trans-acting functions required for endocytosis of the yeast pheromone receptors
    • Davis, N.G., Horecka, J.L., and Sprague, G.F., Jr. (1993). Cis- and trans-acting functions required for endocytosis of the yeast pheromone receptors. J. Cell Biol. 122, 53-65.
    • (1993) J. Cell Biol. , vol.122 , pp. 53-65
    • Davis, N.G.1    Horecka, J.L.2    Sprague G.F., Jr.3
  • 15
    • 0033548575 scopus 로고    scopus 로고
    • AP-4, a novel protein complex related to clathrin adaptors
    • Dell'Angelica, E.C., Mullins, C., and Bonifacino, J.S. (1999a). AP-4, a novel protein complex related to clathrin adaptors. J. Biol. Chem. 274, 7278-7285.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7278-7285
    • Dell'Angelica, E.C.1    Mullins, C.2    Bonifacino, J.S.3
  • 16
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor
    • Dell'Angelica, E.C., Shotelersuk, V., Aguilar, R.C., Gahl, W.A., and Bonifacino, J.S. (1999b). Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor. Mol. Cell 3, 11-21.
    • (1999) Mol. Cell , vol.3 , pp. 11-21
    • Dell'Angelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3    Gahl, W.A.4    Bonifacino, J.S.5
  • 17
    • 0023838558 scopus 로고
    • Enzymes required for yeast prohormone processing
    • Fuller, R.S., Sterne, R.E., and Thorner, J. (1988). Enzymes required for yeast prohormone processing. Annu. Rev. Physiol. 50, 345-362.
    • (1988) Annu. Rev. Physiol. , vol.50 , pp. 345-362
    • Fuller, R.S.1    Sterne, R.E.2    Thorner, J.3
  • 18
    • 0027330921 scopus 로고
    • The beta 1 and beta 2 subunits of the AP complexes are the clathrin coat assembly components
    • Gallusser, A., and Kirchhausen, T. (1993). The beta 1 and beta 2 subunits of the AP complexes are the clathrin coat assembly components. EMBO J. 12, 5237-5244.
    • (1993) EMBO J. , vol.12 , pp. 5237-5244
    • Gallusser, A.1    Kirchhausen, T.2
  • 19
    • 0343632367 scopus 로고    scopus 로고
    • Role of Drosophila alpha-adaptin in presynaptic vesicle recycling
    • González-Gaitán, M., and Jäckle, H. (1997). Role of Drosophila alpha-adaptin in presynaptic vesicle recycling. Cell 88, 767-776.
    • (1997) Cell , vol.88 , pp. 767-776
    • González-Gaitán, M.1    Jäckle, H.2
  • 20
    • 12644259509 scopus 로고    scopus 로고
    • Arrestin/Clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain
    • Goodman, O.B., Jr., Krupnick, J.G., Gurevich, V., Benovic, J.L., and Keen, J.H. (1997). Arrestin/Clathrin Interaction. Localization of the arrestin binding locus to the clathrin terminal domain. J. Biol. Chem. 272, 15017-15022.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15017-15022
    • Goodman O.B., Jr.1    Krupnick, J.G.2    Gurevich, V.3    Benovic, J.L.4    Keen, J.H.5
  • 22
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan, K.L., and Dixon, J.E. (1991). Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem 192, 262-267.
    • (1991) Anal. Biochem , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 23
    • 0003448569 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (1988). Antibodies: A Laboratory Manual, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 24
    • 0022781503 scopus 로고
    • Yeast/E. Coli shuttle vectors with multiple unique restriction sites
    • Hill, J.E., Myers, A.M., Koerner, T.J., and Tzagoloff, A. (1986). Yeast/E. coli shuttle vectors with multiple unique restriction sites. Yeast 2, 163-167.
    • (1986) Yeast , vol.2 , pp. 163-167
    • Hill, J.E.1    Myers, A.M.2    Koerner, T.J.3    Tzagoloff, A.4
  • 26
    • 0033565639 scopus 로고    scopus 로고
    • Clathrin functions in the absence of heterotetrameric adaptors and AP180-related proteins in yeast
    • Huang, K.M., D'Hondt, K., Riezman, H., and Lemmon, S.K. (1999). Clathrin functions in the absence of heterotetrameric adaptors and AP180-related proteins in yeast. EMBO J. 18, 3897-3908.
    • (1999) EMBO J. , vol.18 , pp. 3897-3908
    • Huang, K.M.1    D'Hondt, K.2    Riezman, H.3    Lemmon, S.K.4
  • 27
    • 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, 899-910.
    • (1997) J. Cell Sci. , vol.110 , 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
  • 28
    • 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
  • 29
    • 0023550870 scopus 로고
    • Clathrin assembly proteins: Affinity purification and a model for coat assembly
    • Keen, J.H. (1987). Clathrin assembly proteins: affinity purification and a model for coat assembly. J. Cell Biol. 105, 1989-1998.
    • (1987) J. Cell Biol. , vol.105 , pp. 1989-1998
    • Keen, J.H.1
  • 30
    • 0028979656 scopus 로고
    • A gene encoding gamma-adaptin is required for apical extension growth in ustilago maydis
    • Keon, J.P., Jewitt, S., and Hargreaves, J.A. (1995). A gene encoding gamma-adaptin is required for apical extension growth in Ustilago maydis. Gene 162, 141-145.
    • (1995) Gene , vol.162 , pp. 141-145
    • Keon, J.P.1    Jewitt, S.2    Hargreaves, J.A.3
  • 31
    • 0032514158 scopus 로고    scopus 로고
    • The LDL receptor clustering motif interacts with the clathrin terminal domain in a reverse turn conformation
    • Kibbey, R.G., Rizo, J., Gierasch, L.M., and Anderson, R.G.W. (1998). The LDL receptor clustering motif interacts with the clathrin terminal domain in a reverse turn conformation. J. Cell Biol. 142, 59-67.
    • (1998) J. Cell Biol. , vol.142 , pp. 59-67
    • Kibbey, R.G.1    Rizo, J.2    Gierasch, L.M.3    Anderson, R.G.W.4
  • 32
    • 0025059483 scopus 로고
    • Identification of a putative yeast homolog of the mammalian β chains of the clathrin associated protein complexes
    • Kirchhausen, T. (1990). Identification of a putative yeast homolog of the mammalian β chains of the clathrin associated protein complexes. Mol. Cell. Biol. 10, 6089-6090.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6089-6090
    • Kirchhausen, T.1
  • 33
    • 0019435922 scopus 로고
    • Protein organization in clathrin trimers
    • Kirchhausen, T., and Harrison, S.C. (1981). Protein organization in clathrin trimers. Cell 23, 755-761.
    • (1981) Cell , vol.23 , pp. 755-761
    • Kirchhausen, T.1    Harrison, S.C.2
  • 34
    • 0024514979 scopus 로고
    • Structural and functional division into two domains of the large (100-to 115-kDa) chains of the clathrin-associated protein complex AP-2
    • Kirchhausen, T., Nathanson, K.L., Matsui, W., Vaisberg, A., Chow, E.P., Burne, C., Keen, J.H., and Davis, A.E. (1989). Structural and functional division into two domains of the large (100-to 115-kDa) chains of the clathrin-associated protein complex AP-2. Proc. Natl. Acad. Sci. USA 86, 2612-2616.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2612-2616
    • Kirchhausen, T.1    Nathanson, K.L.2    Matsui, W.3    Vaisberg, A.4    Chow, E.P.5    Burne, C.6    Keen, J.H.7    Davis, A.E.8
  • 35
    • 0032079372 scopus 로고    scopus 로고
    • Nonclassical protein sorting to the yeast vacuole
    • Klionsky, D.J. (1998). Nonclassical protein sorting to the yeast vacuole. J. Biol. Chem. 273, 10807-10810.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10807-10810
    • Klionsky, D.J.1
  • 36
    • 0032145879 scopus 로고    scopus 로고
    • Mechanisms of protein sorting and coat assembly: Insights from the clathrin-coated vesicle pathway
    • Le Borgne, R., and Hoflack, B. (1998). Mechanisms of protein sorting and coat assembly: insights from the clathrin-coated vesicle pathway. Curr. Opin. Cell Biol. 10, 499-503.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 499-503
    • Le Borgne, R.1    Hoflack, B.2
  • 37
    • 0028179670 scopus 로고
    • unc-101, a gene required for many aspects of C. elegans development and behavior, encodes a clathrin-associated protein
    • Lee, J., Jongeward, G.D., and Sternberg, P.W. (1994). unc-101, a gene required for many aspects of C. elegans development and behavior, encodes a clathrin-associated protein. Genes & Dev. 8, 60-73.
    • (1994) Genes & Dev. , vol.8 , pp. 60-73
    • Lee, J.1    Jongeward, G.D.2    Sternberg, P.W.3
  • 38
    • 0033529056 scopus 로고    scopus 로고
    • An assembly protein for clathrin cages
    • McMahon, H.T. (1999). An assembly protein for clathrin cages. Curr. Biol. 9, R332-R335.
    • (1999) Curr. Biol. , vol.9
    • McMahon, H.T.1
  • 39
    • 0027182508 scopus 로고
    • Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast
    • Mitchell, D.A., Marshall, T.K., and Deschenes, R.J. (1993). Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast. Yeast 9, 715-722.
    • (1993) Yeast , vol.9 , pp. 715-722
    • Mitchell, D.A.1    Marshall, T.K.2    Deschenes, R.J.3
  • 40
    • 0033153279 scopus 로고    scopus 로고
    • Functional organization of clathrin in coats: Combining electron cryomicroscopy and X-ray crystallography
    • Musacchio, A., Smith, C.J., Roseman, A.M., Harrison, S.C., Kirchhausen, T., and Pearse, B.M. (1999). Functional organization of clathrin in coats: combining electron cryomicroscopy and x-ray crystallography. Mol. Cell 3, 761-770.
    • (1999) Mol. Cell , vol.3 , pp. 761-770
    • Musacchio, A.1    Smith, C.J.2    Roseman, A.M.3    Harrison, S.C.4    Kirchhausen, T.5    Pearse, B.M.6
  • 41
    • 0032404443 scopus 로고    scopus 로고
    • The AP-3 complex: A coat of many colors
    • Odorizzi, G., Cowles, C.R., and Emr, S.D. (1998). The AP-3 complex: a coat of many colors. Trends Cell Biol. 8, 282-288.
    • (1998) Trends Cell Biol. , vol.8 , pp. 282-288
    • Odorizzi, G.1    Cowles, C.R.2    Emr, S.D.3
  • 43
    • 0033000498 scopus 로고    scopus 로고
    • A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain
    • Owen, D.J., Vallis, Y., Noble, M.E., Hunter, J.B., Dafforn, T.R., Evans, P.R., and McMahon, H.T. (1999). A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain. Cell 97, 805-815.
    • (1999) Cell , vol.97 , pp. 805-815
    • Owen, D.J.1    Vallis, Y.2    Noble, M.E.3    Hunter, J.B.4    Dafforn, T.R.5    Evans, P.R.6    McMahon, H.T.7
  • 44
    • 0030743354 scopus 로고    scopus 로고
    • Suppressors of YCK-encoded yeast casien kinase 1 deficiency define the four subunits of a novel clathrin AP-like complex
    • Panek, H.R., Stepp, J.D., Engle, H.M., Marks, K.M., Tan, P.K., Lemmon, S.K., and Robinson, L.C. (1997). Suppressors of YCK-encoded yeast casien kinase 1 deficiency define the four subunits of a novel clathrin AP-like complex. EMBO J. 16, 4194-4204.
    • (1997) Embo J. , vol.16 , pp. 4194-4204
    • Panek, H.R.1    Stepp, J.D.2    Engle, H.M.3    Marks, K.M.4    Tan, P.K.5    Lemmon, S.K.6    Robinson, L.C.7
  • 45
    • 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
  • 46
    • 0021487739 scopus 로고
    • Purification and properties of 100-kDa proteins from coated vesicles and their reconstitution with clathrin
    • Pearse, B.M., and Robinson, M.S. (1984). Purification and properties of 100-kDa proteins from coated vesicles and their reconstitution with clathrin. EMBO J. 3, 1951-1957.
    • (1984) EMBO J. , vol.3 , pp. 1951-1957
    • Pearse, B.M.1    Robinson, M.S.2
  • 47
    • 0028354374 scopus 로고
    • The Saccharomyces cerevisiae APS1 gene encodes a homolog of the small subunit of the mammalian clathrin AP-1 complex: Evidence for functional interaction with clathrin at the Golgi complex
    • Phan, H.L., Finlay, J.A., Chu, D.S., Tan, P.K., Kirchhausen, T., and Payne, G.S. (1994). The Saccharomyces cerevisiae APS1 gene encodes a homolog of the small subunit of the mammalian clathrin AP-1 complex: evidence for functional interaction with clathrin at the Golgi complex. EMBO J. 13, 1706-1717.
    • (1994) EMBO J. , vol.13 , pp. 1706-1717
    • Phan, H.L.1    Finlay, J.A.2    Chu, D.S.3    Tan, P.K.4    Kirchhausen, T.5    Payne, G.S.6
  • 48
    • 0030852699 scopus 로고    scopus 로고
    • The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway
    • Piper, R.C., Bryant, N.J., and Stevens, T.H. (1997). The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway. J. Cell Biol. 138, 531-545.
    • (1997) J. Cell Biol. , vol.138 , pp. 531-545
    • Piper, R.C.1    Bryant, N.J.2    Stevens, T.H.3
  • 49
    • 0032515135 scopus 로고    scopus 로고
    • Clathrin coats - Threads laid bare
    • Pishvaee, B., and Payne, G.S. (1998). Clathrin coats - threads laid bare. Cell 95, 443-446.
    • (1998) Cell , vol.95 , pp. 443-446
    • Pishvaee, B.1    Payne, G.S.2
  • 50
    • 0028904692 scopus 로고
    • Saccharomyces cerevisiae Ap12p, a homologue of the mammalian AP β subunit, plays a role in clathrin-dependent Golgi functions
    • Rad, M.R., Phan, H.L., Kirchrath, L., Tan, P.K., Kirchhausen, T., Hollenberg, C.P., and Payne, G.S. (1995). Saccharomyces cerevisiae Ap12p, a homologue of the mammalian AP β subunit, plays a role in clathrin-dependent Golgi functions. J. Cell Sci. 108, 1605-1615.
    • (1995) J. Cell Sci. , vol.108 , pp. 1605-1615
    • Rad, M.R.1    Phan, H.L.2    Kirchrath, L.3    Tan, P.K.4    Kirchhausen, T.5    Hollenberg, C.P.6    Payne, G.S.7
  • 51
    • 0032522517 scopus 로고    scopus 로고
    • Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site
    • Rapaport, I., Chen, Y.C., Cupers, P., Shoelson, S.E., and Kirchhausen, T. (1998). Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site. EMBO J. 17, 2148-2155.
    • (1998) EMBO J. , vol.17 , pp. 2148-2155
    • Rapaport, I.1    Chen, Y.C.2    Cupers, P.3    Shoelson, S.E.4    Kirchhausen, T.5
  • 52
    • 0023739386 scopus 로고
    • Protein sorting in Saccharomyces cerevisiae: Isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
    • Robinson, J.S., Klionsky, D.J., Banta, L.M., and Emr, S.D. (1988). Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol. Cell. Biol. 8, 4936-4948.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4936-4948
    • Robinson, J.S.1    Klionsky, D.J.2    Banta, L.M.3    Emr, S.D.4
  • 53
    • 0023228992 scopus 로고
    • 100-kDa coated vesicle proteins: Molecular heterogeneity and intracellular distribution studied with monoclonal antibodies
    • Robinson, M.S. (1987). 100-kDa coated vesicle proteins: molecular heterogeneity and intracellular distribution studied with monoclonal antibodies. J. Cell Biol. 104, 887-895.
    • (1987) J. Cell Biol. , vol.104 , pp. 887-895
    • Robinson, M.S.1
  • 54
    • 0021209385 scopus 로고
    • Structure and function of the yeast URA3 gene: Expression in Escherichia coli
    • Rose, M.D., Grisafi, P., and Botstein, D. (1984). Structure and function of the yeast URA3 gene: Expression in Escherichia coli. Gene 29, 113-124.
    • (1984) Gene , vol.29 , pp. 113-124
    • Rose, M.D.1    Grisafi, P.2    Botstein, D.3
  • 55
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • Rothstein, R. (1991). Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194, 281-301.
    • (1991) Methods Enzymol. , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 57
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and Orci, L. (1996). Coat proteins and vesicle budding. Science 271, 1526-1532.
    • (1996) Science , vol.271 , pp. 1526-1532
    • Schekman, R.1    Orci, L.2
  • 58
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid, S.L. (1997). Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu. Rev. Biochem. 66, 511-548.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 59
    • 0026652588 scopus 로고
    • A role for clathrin in the sorting of vacuolar proteins in the Golgi complex of yeast
    • Seeger, M., and Payne, G.S. (1992a). A role for clathrin in the sorting of vacuolar proteins in the Golgi complex of yeast. EMBO J. 11, 2811-2818.
    • (1992) EMBO J. , vol.11 , pp. 2811-2818
    • Seeger, M.1    Payne, G.S.2
  • 60
    • 0026742306 scopus 로고
    • Selective and immediate effects of clathrin heavy chain mutations on Golgi membrane protein retention in Saccharomyces cerevisiae
    • Seeger, M., and Payne, G.S. (1992b). Selective and immediate effects of clathrin heavy chain mutations on Golgi membrane protein retention in Saccharomyces cerevisiae. J. Cell Biol. 118, 531-540.
    • (1992) J. Cell Biol. , vol.118 , pp. 531-540
    • Seeger, M.1    Payne, G.S.2
  • 62
    • 0029584896 scopus 로고
    • A clathrin-binding site in the hinge of the beta 2 chain of mammalian AP-2 complexes
    • Shih, W., Gallusser, A., and Kirchhausen, T. (1995). A clathrin-binding site in the hinge of the beta 2 chain of mammalian AP-2 complexes. J. Biol. Chem. 270, 31083-31090.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31083-31090
    • Shih, W.1    Gallusser, A.2    Kirchhausen, T.3
  • 63
    • 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
  • 65
    • 0030926547 scopus 로고    scopus 로고
    • Characterization of the adaptor-related protein complex, AP-3
    • Simpson, F., Peden, A.A., Christopoulou, L., and Robinson, M.S. (1997). Characterization of the adaptor-related protein complex, AP-3. J. Cell Biol. 137, 835-845.
    • (1997) J. Cell Biol. , vol.137 , pp. 835-845
    • Simpson, F.1    Peden, A.A.2    Christopoulou, L.3    Robinson, M.S.4
  • 66
    • 0032167614 scopus 로고    scopus 로고
    • Clathrin coats at 21Å resolution: A cellular assembly designed to recycle multiple membrane receptors
    • Smith, C.J., Grigorieff, N., and Pearse, B.M.F. (1998). Clathrin coats at 21Å resolution: a cellular assembly designed to recycle multiple membrane receptors. EMBO J. 17, 4943-4953.
    • (1998) EMBO J. , vol.17 , pp. 4943-4953
    • Smith, C.J.1    Grigorieff, N.2    Pearse, B.M.F.3
  • 67
    • 0029010492 scopus 로고
    • A late golgi sorting function for Saccharomyces cerevisiae Apm1p, but not for Apm2p, a second yeast clathrin AP medium chain-related protein
    • Stepp, D.J., Pellicena-Palle, A., Hamilton, S., Kirchhausen, T., and Lemmon, S.K. (1995). A late Golgi sorting function for Saccharomyces cerevisiae Apm1p, but not for Apm2p, a second yeast clathrin AP medium chain-related protein. Mol. Biol. Cell 6, 41-58.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 41-58
    • Stepp, D.J.1    Pellicena-Palle, A.2    Hamilton, S.3    Kirchhausen, T.4    Lemmon, S.K.5
  • 68
    • 0031408332 scopus 로고    scopus 로고
    • The yeast adaptor protein complex, AP-3, is essential for the efficient delivery of alkaline phosphatase by the alternate pathway to the vacuole
    • Stepp, J.D., Huang, K., and Lemmon, S.K. (1997). The yeast adaptor protein complex, AP-3, is essential for the efficient delivery of alkaline phosphatase by the alternate pathway to the vacuole. J. Cell Biol. 139, 1761-1774.
    • (1997) J. Cell Biol. , vol.139 , pp. 1761-1774
    • Stepp, J.D.1    Huang, K.2    Lemmon, S.K.3
  • 70
    • 0027752442 scopus 로고
    • Clathrin facilitates the internalization of seven transmembrane segment receptors for mating pheromones in yeast
    • Tan, P.K., Davis, N.G., Sprague, G.F., and Payne, G.S. (1993). Clathrin facilitates the internalization of seven transmembrane segment receptors for mating pheromones in yeast. J. Cell Biol. 123, 1707-1716.
    • (1993) J. Cell Biol. , vol.123 , pp. 1707-1716
    • Tan, P.K.1    Davis, N.G.2    Sprague, G.F.3    Payne, G.S.4
  • 71
    • 0018930599 scopus 로고
    • Sequence of a yeast DNA fragment containing a chromosomal replicator and the TRP1 gene
    • Tschumper, G., and Carbon, J. (1980). Sequence of a yeast DNA fragment containing a chromosomal replicator and the TRP1 gene. Gene 10, 157-166.
    • (1980) Gene , vol.10 , pp. 157-166
    • Tschumper, G.1    Carbon, J.2
  • 72
    • 0019890534 scopus 로고
    • Assembly units of clathrin coats
    • Ungewickell, E., and Branton, D. (1981). Assembly units of clathrin coats. Nature 289, 420-422.
    • (1981) Nature , vol.289 , pp. 420-422
    • Ungewickell, E.1    Branton, D.2
  • 73
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida, T.A., and Emr, S.D. (1995). A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J. Cell Biol. 128, 779-792.
    • (1995) J. Cell Biol. , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 74
    • 0022684837 scopus 로고
    • Three-dimensional structure of clathrin cages in ice
    • Vigers, G.P., Crowther, R.A., and Pearse, B.M. (1986a). Three-dimensional structure of clathrin cages in ice. EMBO J. 5, 529-534.
    • (1986) EMBO J. , vol.5 , pp. 529-534
    • Vigers, G.P.1    Crowther, R.A.2    Pearse, B.M.3
  • 75
    • 0022780984 scopus 로고
    • Location of the 100 kDa-50 kda accessory proteins in clathrin coats
    • Vigers, G.P., Crowther, R.A., and Pearse, B.M. (1986b). Location of the 100 kDa-50 kDa accessory proteins in clathrin coats. EMBO J. 5, 2079-2085.
    • (1986) EMBO J. , vol.5 , pp. 2079-2085
    • Vigers, G.P.1    Crowther, R.A.2    Pearse, B.M.3
  • 76
    • 0032079666 scopus 로고    scopus 로고
    • A dileucine-like sorting signal directs transport into an AP-3-dependent, clathrin-independent pathway to the yeast vacuole
    • Vowels, J.J., and Payne, G.S. (1998a). A dileucine-like sorting signal directs transport into an AP-3-dependent, clathrin-independent pathway to the yeast vacuole. EMBO J. 17, 2482-2493.
    • (1998) EMBO J. , vol.17 , pp. 2482-2493
    • Vowels, J.J.1    Payne, G.S.2
  • 77
    • 0028986797 scopus 로고
    • The appendage domain of alpha-adaptin is a high affinity binding site for dynamin
    • Wang, L.H., Sudhof, T.C., and Anderson, R.G. (1995). The appendage domain of alpha-adaptin is a high affinity binding site for dynamin. J. Biol. Chem. 270, 10079-10083.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10079-10083
    • Wang, L.H.1    Sudhof, T.C.2    Anderson, R.G.3
  • 78
    • 0032489873 scopus 로고    scopus 로고
    • Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions for endocytosis
    • Wendland, B., and Emr, S.D. (1998). Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions for endocytosis. J. Cell Biol. 141, 71-84.
    • (1998) J. Cell Biol. , vol.141 , pp. 71-84
    • Wendland, B.1    Emr, S.D.2
  • 79
    • 0033575748 scopus 로고    scopus 로고
    • Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin, and are required for endocytosis
    • Wendland, B., Steece, K.E., and Emr, S.D. (1999). Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin, and are required for endocytosis. EMBO J. 8, 4383-4393.
    • (1999) EMBO J. , vol.8 , pp. 4383-4393
    • Wendland, B.1    Steece, K.E.2    Emr, S.D.3
  • 81
    • 0031214092 scopus 로고    scopus 로고
    • Inhibition of receptor-mediated endocytosis by the amphiphysin SH3 domain
    • Wigge, P., Vallis, Y., and McMahon, H.T. (1997b). Inhibition of receptor-mediated endocytosis by the amphiphysin SH3 domain. Curr. Biol. 7, 554-560.
    • (1997) Curr. Biol. , vol.7 , pp. 554-560
    • Wigge, P.1    Vallis, Y.2    McMahon, H.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.