메뉴 건너뛰기




Volumn 164, Issue 7, 2004, Pages 1065-1076

Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins

Author keywords

AP 3 adaptor protein; Clathrin; Endosomes; Immuno EM; TGN

Indexed keywords

ADAPTOR PROTEIN; ASIALOGLYCOPROTEIN RECEPTOR; CATION; CD63 ANTIGEN; CELL PROTEIN; CLATHRIN; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; LYSOSOME MEMBRANE PROTEIN; MEMBRANE PROTEIN; SOMATOMEDIN B RECEPTOR; TRANSFERRIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 1842509099     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200311064     Document Type: Article
Times cited : (283)

References (61)
  • 1
    • 0027433881 scopus 로고
    • Cycling of two endogenous lysosomal membrane proteins, lamp-2 and acid phosphatase, between the cell surface and lysosomes in cultured rat hepatocytes
    • Akasaki, K., M. Fukuzawa, H. Kinoshita, K. Furuno, and H. Tsuji. 1993. Cycling of two endogenous lysosomal membrane proteins, lamp-2 and acid phosphatase, between the cell surface and lysosomes in cultured rat hepatocytes. J. Biochem. (Tokyo). 114:598-604.
    • (1993) J. Biochem. (Tokyo) , vol.114 , pp. 598-604
    • Akasaki, K.1    Fukuzawa, M.2    Kinoshita, H.3    Furuno, K.4    Tsuji, H.5
  • 2
    • 0029084767 scopus 로고
    • Biosynthetic transport of a major lysosomal membrane glycoprotein, lamp-1: Convergence of biosynthetic and endocytic pathways occurs at three distinctive points
    • Akasaki, K., A. Michihara, K. Mibuka, Y. Fujiwara, and H. Tsuji. 1995. Biosynthetic transport of a major lysosomal membrane glycoprotein, lamp-1: convergence of biosynthetic and endocytic pathways occurs at three distinctive points. Exp. Cell Res. 220:464-473.
    • (1995) Exp. Cell Res. , vol.220 , pp. 464-473
    • Akasaki, K.1    Michihara, A.2    Mibuka, K.3    Fujiwara, Y.4    Tsuji, H.5
  • 3
    • 0030462963 scopus 로고    scopus 로고
    • Biosynthetic transport of a major lysosome-associated membrane glycoprotein 2, lamp-2: A significant fraction of newly synthesized lamp-2 is delivered to lysosomes by way of early endosomes
    • Akasaki, K., A. Michihara, Y. Fujiwara, K. Mibuka, and H. Tsuji. 1996. Biosynthetic transport of a major lysosome-associated membrane glycoprotein 2, lamp-2: a significant fraction of newly synthesized lamp-2 is delivered to lysosomes by way of early endosomes. J. Biochem. (Tokyo). 120:1088-1094.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 1088-1094
    • Akasaki, K.1    Michihara, A.2    Fujiwara, Y.3    Mibuka, K.4    Tsuji, H.5
  • 4
    • 0030797279 scopus 로고    scopus 로고
    • Syntaxin 6 functions in trans-Golgi network vesicle trafficking
    • Bock, J.B., J. Klumperman, S. Davanger, and R.H. Scheller. 1997. Syntaxin 6 functions in trans-Golgi network vesicle trafficking. Mol. Biol. Cell. 8:1261-1271.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1261-1271
    • Bock, J.B.1    Klumperman, J.2    Davanger, S.3    Scheller, R.H.4
  • 6
    • 0030886261 scopus 로고    scopus 로고
    • The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole
    • Cowles, C.R., G. Odorizzi, G.S. Payne, and S.D. Emr. 1997. 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
  • 7
    • 0000241799 scopus 로고
    • pH and the recycling of transferrin during receptor-mediated endocytosis
    • Dautry-Varsat, A., A. Ciechanover, and H.F. Lodish. 1983. pH and the recycling of transferrin during receptor-mediated endocytosis. Proc. Natl. Acad. Sci. USA. 80:2258-2262.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2258-2262
    • Dautry-Varsat, A.1    Ciechanover, A.2    Lodish, H.F.3
  • 10
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A-subunit of the AP-3 adaptor
    • Dell'Angelica, E.C., V. Shotelersuk, R.C. Aguilar, W.A. Gahl, and J.S. Bonifacino. 1999. Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A-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
  • 11
    • 0037031658 scopus 로고    scopus 로고
    • Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network
    • Doray, B., P. Ghosh, J. Griffith, H.J. Geuze, and S. Kornfeld. 2002. Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network. Science. 297:1700-1703.
    • (2002) Science , vol.297 , pp. 1700-1703
    • Doray, B.1    Ghosh, P.2    Griffith, J.3    Geuze, H.J.4    Kornfeld, S.5
  • 12
    • 0033739794 scopus 로고    scopus 로고
    • The assembly of AP-3 adaptor complex-containing clathrin-coated vesicles on synthetic liposomes
    • Drake, M.T., Y. Zhu, and S. Kornfeld. 2000. The assembly of AP-3 adaptor complex-containing clathrin-coated vesicles on synthetic liposomes. Mol. Biol. Cell. 11:3723-3736.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3723-3736
    • Drake, M.T.1    Zhu, Y.2    Kornfeld, S.3
  • 13
    • 0024842857 scopus 로고
    • Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome
    • Dunn, K.W., T.E. McGraw, and F.R. Maxfield. 1989. Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome. J. Cell Biol. 109:3303-3314.
    • (1989) J. Cell Biol , vol.109 , pp. 3303-3314
    • Dunn, K.W.1    McGraw, T.E.2    Maxfield, F.R.3
  • 14
    • 0032076102 scopus 로고    scopus 로고
    • A function for the AP3 coat complex in synaptic vesicle formation from endosomes
    • Faundez, V., J.T. Horng, and R.B. Kelly. 1998. A function for the AP3 coat complex in synaptic vesicle formation from endosomes. Cell. 93:423-432.
    • (1998) Cell. , vol.93 , pp. 423-432
    • Faundez, V.1    Horng, J.T.2    Kelly, R.B.3
  • 15
    • 0032102108 scopus 로고    scopus 로고
    • The role of endosomes and lysosomes in MHC class II functioning
    • Geuze, H.J. 1998. The role of endosomes and lysosomes in MHC class II functioning. Immunol. Today. 19:282-287.
    • (1998) Immunol. Today , vol.19 , pp. 282-287
    • Geuze, H.J.1
  • 16
    • 0020685762 scopus 로고
    • Intracellular site of asialoglycoprotein receptor-ligand uncoupling: Double-label immunoelectron microscopy during receptor-mediated endocytosis
    • Geuze, H.J., J.W. Slot, G.J. Strous, H.F. Lodish, and A.L. Schwartz. 1983. Intracellular site of asialoglycoprotein receptor-ligand uncoupling: double-label immunoelectron microscopy during receptor-mediated endocytosis. Cell. 32:277-287.
    • (1983) Cell , vol.32 , pp. 277-287
    • Geuze, H.J.1    Slot, J.W.2    Strous, G.J.3    Lodish, H.F.4    Schwartz, A.L.5
  • 18
    • 0024787848 scopus 로고
    • A quantitative analysis of the endocytic pathway in baby hamster kidney cells
    • Griffiths, G., R. Back, and M. Marsh. 1989. A quantitative analysis of the endocytic pathway in baby hamster kidney cells. J. Cell Biol. 109:2703-2720.
    • (1989) J. Cell Biol. , vol.109 , pp. 2703-2720
    • Griffiths, G.1    Back, R.2    Marsh, M.3
  • 19
    • 0026545549 scopus 로고
    • Transport of the lysosomal membrane glycoprotein lgp120 (lgpA) to lysosomes does not require appearance on the plasma membrane
    • Harter, C., and I. Mellman. 1992. Transport of the lysosomal membrane glycoprotein lgp120 (lgpA) to lysosomes does not require appearance on the plasma membrane. J. Cell Biol. 117:311-325.
    • (1992) J. Cell Biol. , vol.117 , pp. 311-325
    • Harter, C.1    Mellman, I.2
  • 20
    • 0024075871 scopus 로고
    • Deep-etch visualization of proteins involved in clathrin assembly
    • Heuser, J.E., and J. Keen. 1988. Deep-etch visualization of proteins involved in clathrin assembly. J. Cell Biol. 107:877-886.
    • (1988) J. Cell Biol. , vol.107 , pp. 877-886
    • Heuser, J.E.1    Keen, J.2
  • 21
    • 0028339264 scopus 로고
    • In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella
    • Hopkins, C.R., A. Gibson, M. Shipman, D.K. Strickland, and I.S. Trowbridge. 1994. In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella. J. Cell Biol. 125:1265-1274.
    • (1994) J. Cell Biol. , vol.125 , pp. 1265-1274
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Strickland, D.K.4    Trowbridge, I.S.5
  • 22
    • 0019519884 scopus 로고
    • Characterization of plasma membrane proteins identified by monoclonal antibodies
    • Hughes, E.N., and J.T. August. 1981. Characterization of plasma membrane proteins identified by monoclonal antibodies. J. Biol. Chem. 256:664-671.
    • (1981) J. Biol. Chem. , vol.256 , pp. 664-671
    • Hughes, E.N.1    August, J.T.2
  • 23
    • 0030137994 scopus 로고    scopus 로고
    • Intracellular trafficking of lysosomal membrane proteins
    • Hunziker, W., and H.J. Geuze. 1996. Intracellular trafficking of lysosomal membrane proteins. Bioessays. 18:379-389.
    • (1996) Bioessays , vol.18 , pp. 379-389
    • Hunziker, W.1    Geuze, H.J.2
  • 24
    • 0025014580 scopus 로고
    • Role of the human transferrin receptor cytoplasmic domain in endocytosis: Localization of a specific signal sequence for internalization
    • Jing, S.Q., T. Spencer, K. Miller, C. Hopkins, and I.S. Trowbridge. 1990. Role of the human transferrin receptor cytoplasmic domain in endocytosis: localization of a specific signal sequence for internalization. J. Cell Biol. 110:283-294.
    • (1990) J. Cell Biol. , vol.110 , pp. 283-294
    • Jing, S.Q.1    Spencer, T.2    Miller, K.3    Hopkins, C.4    Trowbridge, I.S.5
  • 28
    • 0032491411 scopus 로고    scopus 로고
    • The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins
    • Le Borgne, R., A. Alconada, U. Bauer, and B. Hoflack. 1998. The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins. J. Biol. Chem. 273:29451-29461.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29451-29461
    • Le Borgne, R.1    Alconada, A.2    Bauer, U.3    Hoflack, B.4
  • 29
    • 0021342268 scopus 로고
    • Expression of transferrin receptor on murine hematopoietic progenitors
    • Lesley, J., R. Hyman, R. Schulte, and J. Trotter. 1984. Expression of transferrin receptor on murine hematopoietic progenitors. Cell. Immunol. 83:14-25.
    • (1984) Cell. Immunol. , vol.83 , pp. 14-25
    • Lesley, J.1    Hyman, R.2    Schulte, R.3    Trotter, J.4
  • 30
    • 0029762913 scopus 로고    scopus 로고
    • Improving structural integrity of cryosections for immunogold labeling
    • Liou, W., H.J. Geuze, and J.W. Slot. 1996. Improving structural integrity of cryosections for immunogold labeling. Histochem. Cell Biol. 106:41-58.
    • (1996) Histochem. Cell Biol. , vol.106 , pp. 41-58
    • Liou, W.1    Geuze, H.J.2    Slot, J.W.3
  • 31
    • 0023644927 scopus 로고
    • Cycling of the integral membrane glycoprotein, LEP100, between plasma membrane and lysosomes: Kinetic and morphological analysis
    • Lippincott-Schwartz, J., and D.M. Fambrough. 1987. Cycling of the integral membrane glycoprotein, LEP100, between plasma membrane and lysosomes: kinetic and morphological analysis. Cell. 49:669-677.
    • (1987) Cell , vol.49 , pp. 669-677
    • Lippincott-Schwartz, J.1    Fambrough, D.M.2
  • 32
    • 0032538927 scopus 로고    scopus 로고
    • Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of shiga toxin B-fragment transport
    • Mallard, F., C. Antony, D. Tenza, J. Salamero, B. Goud, and L. Johannes. 1998. Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of shiga toxin B-fragment transport. J. Cell Biol. 143:973-990.
    • (1998) J. Cell Biol. , vol.143 , pp. 973-990
    • Mallard, F.1    Antony, C.2    Tenza, D.3    Salamero, J.4    Goud, B.5    Johannes, L.6
  • 34
    • 0027243406 scopus 로고
    • Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process
    • Mayor, S., J.F. Presley, and F.R. Maxfield. 1993. Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process. J. Cell Biol. 121:1257-1269.
    • (1993) J. Cell Biol. , vol.121 , pp. 1257-1269
    • Mayor, S.1    Presley, J.F.2    Maxfield, F.R.3
  • 35
    • 0034657033 scopus 로고    scopus 로고
    • μ1A adaptin-deficient mice: Lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors
    • Meyer, C., D. Zizioli, S. Lausmann, E.L. Eskelinen, J. Hamann, P. Saftig, K. von Figura, and P. Schu. 2000. μ1A adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors. EMBO J. 19:2193-2203.
    • (2000) EMBO J. , vol.19 , pp. 2193-2203
    • Meyer, C.1    Zizioli, D.2    Lausmann, S.3    Eskelinen, E.L.4    Hamann, J.5    Saftig, P.6    Von Figura, K.7    Schu, P.8
  • 36
    • 0037076273 scopus 로고    scopus 로고
    • The 8 subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface
    • Nishimura, N., H. Plutner, K. Hahn, and W.E. Balch. 2002. The 8 subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface. Proc. Natl. Acad. Sci. USA. 99:6755-6760.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6755-6760
    • Nishimura, N.1    Plutner, H.2    Hahn, K.3    Balch, W.E.4
  • 37
  • 38
    • 0037148533 scopus 로고    scopus 로고
    • Assembly and function of AP-3 complexes in cells expressing mutant-subunits
    • Peden, A.A., R.E. Rudge, W.W. Lui, and M.S. Robinson. 2002. Assembly and function of AP-3 complexes in cells expressing mutant-subunits. J. Cell Biol. 156:327-336.
    • (2002) J. Cell Biol. , vol.156 , pp. 327-336
    • Peden, A.A.1    Rudge, R.E.2    Lui, W.W.3    Robinson, M.S.4
  • 39
    • 0028232681 scopus 로고
    • Biogenesis of lysosomal membranes
    • Peters, C., and K. von Figura. 1994. Biogenesis of lysosomal membranes. FEBS Lett. 346:108-114.
    • (1994) FEBS Lett. , vol.346 , pp. 108-114
    • Peters, C.1    Von Figura, K.2
  • 41
  • 45
    • 0036231098 scopus 로고    scopus 로고
    • Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes
    • Sachse, M., S. Urbe, V. Oorschot, G.J. Strous, and J. Klumpetman. 2002. Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes. Mol. Biol. Cell. 13:1313-1328.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1313-1328
    • Sachse, M.1    Urbe, S.2    Oorschot, V.3    Strous, G.J.4    Klumpetman, J.5
  • 46
    • 0027371110 scopus 로고
    • Targeting and mistargeting of plasma membrane adaptors in vitro
    • Seaman, M.N., C.L. Ball, and M.S. Robinson. 1993. Targeting and mistargeting of plasma membrane adaptors in vitro. J. Cell Biol. 123:1093-1105.
    • (1993) J. Cell Biol. , vol.123 , pp. 1093-1105
    • Seaman, M.N.1    Ball, C.L.2    Robinson, M.S.3
  • 48
  • 49
    • 0025761381 scopus 로고
    • Immuno-localization of the insulin regulatable glucose transporter in brown adipose tissue of the rat
    • Slot, J.W., H.J. Geuze, S. Gigengack, G.E. Lienhatd, and D.E. James. 1991. Immuno-localization of the insulin regulatable glucose transporter in brown adipose tissue of the rat. J. Cell Biol. 113:123-135.
    • (1991) J. Cell Biol. , vol.113 , pp. 123-135
    • Slot, J.W.1    Geuze, H.J.2    Gigengack, S.3    Lienhatd, G.E.4    James, D.E.5
  • 50
    • 0036428014 scopus 로고    scopus 로고
    • The molecular machinery for the biogenesis of lysosome-related organelles: Lessons from Hermansky-Pudlak syndrome
    • Starcevic, M., R. Nazarian, and E.C. Dell'Angelica. 2002. The molecular machinery for the biogenesis of lysosome-related organelles: lessons from Hermansky-Pudlak syndrome. Semin. Cell Dev. Biol. 13:271-278.
    • (2002) Semin. Cell Dev. Biol. , vol.13 , pp. 271-278
    • Starcevic, M.1    Nazarian R.Dell'Angelica, E.C.2
  • 51
    • 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., K. Huang, and S.K. Lemmon. 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
  • 52
    • 0023256389 scopus 로고
    • Sorting of endocytosed transferrin and asialoglycoprotein occurs immediately after internalization in HepG2 cells
    • Stoorvogel, W., H.J. Geuze, and G.J. Strous. 1987. Sorting of endocytosed transferrin and asialoglycoprotein occurs immediately after internalization in HepG2 cells. J. Cell Biol. 104:1261-1268.
    • (1987) J. Cell Biol. , vol.104 , pp. 1261-1268
    • Stoorvogel, W.1    Geuze, H.J.2    Strous, G.J.3
  • 53
    • 0036285648 scopus 로고    scopus 로고
    • Failure of trafficking and antigen presentation by CD1 in AP-3-deficient cells
    • Sugita, M., X. Cao, G.F. Watts, R.A. Rogers, J.S. Bonifacino, and M.B. Brenner. 2002. Failure of trafficking and antigen presentation by CD1 in AP-3-deficient cells. Immunity. 16:697-706.
    • (2002) Immunity , vol.16 , pp. 697-706
    • Sugita, M.1    Cao, X.2    Watts, G.F.3    Rogers, R.A.4    Bonifacino, J.S.5    Brenner, M.B.6
  • 54
    • 0003059314 scopus 로고    scopus 로고
    • Rapid production of retroviruses for efficient gene delivery to mammalian cells using 293T cell-based systems
    • J.E. Coligan, A.M. Kruisbeek, D.H. Margulies, E.M. Shevach, and W. Strober, editors. John Wiley & Sons Inc., New York
    • Swift, S., J.B. Lorens, P. Achacoso, and G.P. Nolan. 1999. Rapid production of retroviruses for efficient gene delivery to mammalian cells using 293T cell-based systems. In Current Protocols in Immunology. J.E. Coligan, A.M. Kruisbeek, D.H. Margulies, E.M. Shevach, and W. Strober, editors. John Wiley & Sons Inc., New York. Suppl. 31.
    • (1999) Current Protocols in Immunology , Issue.SUPPL. 31
    • Swift, S.1    Lorens, J.B.2    Achacoso, P.3    Nolan, G.P.4
  • 55
    • 0033967923 scopus 로고    scopus 로고
    • Peptide-in-groove interactions link target proteins to the β-propeller of clathrin
    • ter Haar, E., S.C. Harrison, and T. Kirchhausen. 2000. Peptide-in-groove interactions link target proteins to the β-propeller of clathrin. Proc. Natl. Acad. Sci. USA. 97:1096-1100.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1096-1100
    • Ter Haar, E.1    Harrison, S.C.2    Kirchhausen, T.3
  • 56
    • 0036153898 scopus 로고    scopus 로고
    • Dynamin-dependent transferrin receptor recycling by endosome-derived clathrin-coated vesicles
    • van Dam, E.M., and W. Stoorvogel. 2002. Dynamin-dependent transferrin receptor recycling by endosome-derived clathrin-coated vesicles. Mol. Biol. Cell. 13:169-182.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 169-182
    • Van Dam, E.M.1    Stoorvogel, W.2
  • 57
    • 0033621149 scopus 로고    scopus 로고
    • A tubular endosomal fraction from rat liver: Biochemical evidence of receptor sorting by default
    • Verges, M., R.J. Havel, and K.E. Mostov. 1999. A tubular endosomal fraction from rat liver: biochemical evidence of receptor sorting by default. Proc. Natl. Acad. Sci. USA. 96:10146-10151.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10146-10151
    • Verges, M.1    Havel, R.J.2    Mostov, K.E.3
  • 58
    • 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 G.S. Payne. 1998. 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
  • 61
    • 0037200068 scopus 로고    scopus 로고
    • Controlled elimination of clathrin heavy-chain expression in DT40 lymphocytes
    • Wettey, F.R., S.F. Hawkins, A. Stewart, J.P. Luzio, J.C. Howard, and A.P. Jackson. 2002. Controlled elimination of clathrin heavy-chain expression in DT40 lymphocytes. Science. 297:1521-1525.
    • (2002) Science , vol.297 , pp. 1521-1525
    • Wettey, F.R.1    Hawkins, S.F.2    Stewart, A.3    Luzio, J.P.4    Howard, J.C.5    Jackson, A.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.