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Volumn 3, Issue 8, 2002, Pages 537-546

Cargo selection in vesicular transport: The making and breaking of a coat

Author keywords

Accessory protein; Adaptor compelex; AP 2; Cargo selection; Clathrin; COPII; Endoplasmic reticulum; GTPase; Phospholipid membrane; Phosphorylation; Vasicle budding; Vesicular transport

Indexed keywords

ADAPTOR PROTEIN; CLATHRIN; COAT PROTEIN; SNARE PROTEIN; UBIQUITIN;

EID: 0036704516     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-0854.2002.30804.x     Document Type: Review
Times cited : (61)

References (105)
  • 1
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: Towards an understanding at the molecular level
    • Ellgaard L, Helenius A. ER quality control: Towards an understanding at the molecular level. Curr Opin Cell Biol 2001;13:431-437.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 431-437
    • Ellgaard, L.1    Helenius, A.2
  • 3
    • 0027500969 scopus 로고
    • SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER
    • Barlowe C, Schekman R. SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature 1993:365:347-349.
    • (1993) Nature , vol.365 , pp. 347-349
    • Barlowe, C.1    Schekman, R.2
  • 4
    • 0034680777 scopus 로고    scopus 로고
    • Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum
    • Aridor M, Balch WE. Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum. J Biol Chem 2000;275:35673-35676.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35673-35676
    • Aridor, M.1    Balch, W.E.2
  • 6
    • 0032215324 scopus 로고    scopus 로고
    • Coat assembly directs v-SNARE concentration into synthetic COPII vesicles
    • Matsuoka K, Morimitsu Y, Uchida K, Schekman R. Coat assembly directs v-SNARE concentration into synthetic COPII vesicles. Mol Cell 1998;2:703-708.
    • (1998) Mol. Cell , vol.2 , pp. 703-708
    • Matsuoka, K.1    Morimitsu, Y.2    Uchida, K.3    Schekman, R.4
  • 7
    • 18344405156 scopus 로고    scopus 로고
    • COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes
    • Matsuoka K, Orci L, Amherdt M, Bednarek SY, Hamamoto S, Schekman R, Yeung T. COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 1998;93:263-275.
    • (1998) Cell , vol.93 , pp. 263-275
    • Matsuoka, K.1    Orci, L.2    Amherdt, M.3    Bednarek, S.Y.4    Hamamoto, S.5    Schekman, R.6    Yeung, T.7
  • 10
    • 0032489878 scopus 로고    scopus 로고
    • Cargo selection by the COPII budding machinery during export from the ER
    • Aridor M, Weissman J, Bannykh S, Nuoffer C, Balch WE. Cargo selection by the COPII budding machinery during export from the ER. J Cell Biol 1998;141:61-70.
    • (1998) J. Cell Biol. , vol.141 , pp. 61-70
    • Aridor, M.1    Weissman, J.2    Bannykh, S.3    Nuoffer, C.4    Balch, W.E.5
  • 11
    • 0032495477 scopus 로고    scopus 로고
    • COPII-cargo interactions direct protein sorting into ER-derived transport vesicles
    • Kuehn MJ, Herrmann JM, Schekman R. COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature 1998;391:187-190.
    • (1998) Nature , vol.391 , pp. 187-190
    • Kuehn, M.J.1    Herrmann, J.M.2    Schekman, R.3
  • 14
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman JE, Wieland FT. Protein sorting by transport vesicles. Science 1996;272:227-234.
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 15
    • 0025764613 scopus 로고
    • Recycling of proteins between the endoplasmic reticulum and Golgi complex
    • Pelham HR. Recycling of proteins between the endoplasmic reticulum and Golgi complex. Curr Opin Cell Biol 1991;3:585-591.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 585-591
    • Pelham, H.R.1
  • 16
    • 0031464540 scopus 로고    scopus 로고
    • The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1
    • Aoe T, Cukierman E, Lee A, Cassel D, Peters PJ, Hsu VW. The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1. EMBO J 1997:16:7305-7316.
    • (1997) EMBO J. , vol.16 , pp. 7305-7316
    • Aoe, T.1    Cukierman, E.2    Lee, A.3    Cassel, D.4    Peters, P.J.5    Hsu, V.W.6
  • 17
    • 0033582917 scopus 로고    scopus 로고
    • Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis
    • Goldberg J. Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell 1999:96:893-902.
    • (1999) Cell , vol.96 , pp. 893-902
    • Goldberg, J.1
  • 18
    • 0034677633 scopus 로고    scopus 로고
    • Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex
    • Goldberg J. Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex. Cell 2000:100:671-679.
    • (2000) Cell , vol.100 , pp. 671-679
    • Goldberg, J.1
  • 21
    • 0035800751 scopus 로고    scopus 로고
    • The carboxyl-terminal valine is required for transport of glycoprotein CD8 alpha from the endoplasmic reticulum to the intermediate compartment
    • Iodice L, Sarnataro S, Bonatti S. The carboxyl-terminal valine is required for transport of glycoprotein CD8 alpha from the endoplasmic reticulum to the intermediate compartment. J Biol Chem 2001;276:28920-28926.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28920-28926
    • Iodice, L.1    Sarnataro, S.2    Bonatti, S.3
  • 22
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum
    • Nishimura N, Balch WE. A di-acidic signal required for selective export from the endoplasmic reticulum. Science 1997;277:556-558.
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 23
    • 0037186091 scopus 로고    scopus 로고
    • Diverse trafficking patterns due to multiple traffic motifs in G protein-activated inwardly rectifying potassium channels from brain and heart
    • Ma D, Zerangue N, Raab-Graham K, Fried SR, Jan YN, Jan LY. Diverse trafficking patterns due to multiple traffic motifs in G protein-activated inwardly rectifying potassium channels from brain and heart. Neuron 2002;33:715-729.
    • (2002) Neuron , vol.33 , pp. 715-729
    • Ma, D.1    Zerangue, N.2    Raab-Graham, K.3    Fried, S.R.4    Jan, Y.N.5    Jan, L.Y.6
  • 24
    • 0035846990 scopus 로고    scopus 로고
    • Role of ER export signals in controlling surface potassium channel numbers
    • Ma D, Zerangue N, Lin YF, Collins A, Yu M, Jan YN, Jan LY. Role of ER export signals in controlling surface potassium channel numbers. Science 2001;291:316-319.
    • (2001) Science , vol.291 , pp. 316-319
    • Ma, D.1    Zerangue, N.2    Lin, Y.F.3    Collins, A.4    Yu, M.5    Jan, Y.N.6    Jan, L.Y.7
  • 25
    • 0035900761 scopus 로고    scopus 로고
    • Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex
    • Belden WJ, Barlowe C. Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex. J Biol Chem 2001:276:43040-43048.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43040-43048
    • Belden, W.J.1    Barlowe, C.2
  • 26
    • 0035803582 scopus 로고    scopus 로고
    • An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export
    • Votsmeier C, Gallwitz D. An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export. EMBO J 2001;20:6742-6750.
    • (2001) EMBO J. , vol.20 , pp. 6742-6750
    • Votsmeier, C.1    Gallwitz, D.2
  • 27
    • 0031662589 scopus 로고    scopus 로고
    • Receptor-associated protein (RAP): A specialized chaperone for endocytic receptors
    • Willnow TE. Receptor-associated protein (RAP): A specialized chaperone for endocytic receptors. Biol Chem 1998;379:1025-1031.
    • (1998) Biol. Chem. , vol.379 , pp. 1025-1031
    • Willnow, T.E.1
  • 28
    • 0028143610 scopus 로고
    • The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin
    • Baker EK, Colley NJ, Zuker CS. The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J 1994;13:4886-4895.
    • (1994) EMBO J. , vol.13 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 29
    • 0037007201 scopus 로고    scopus 로고
    • Ligands act as pharmacological chaperones and increase the efficiency of delta opioid receptor maturation
    • Petaja-Repo UE, Hogue M, Bhalla S, Laperriere A, Morello JP, Bouvier M. Ligands act as pharmacological chaperones and increase the efficiency of delta opioid receptor maturation. EMBO J 2002;21:1628-1637.
    • (2002) EMBO J. , vol.21 , pp. 1628-1637
    • Petaja-Repo, U.E.1    Hogue, M.2    Bhalla, S.3    Laperriere, A.4    Morello, J.P.5    Bouvier, M.6
  • 30
    • 0035011489 scopus 로고    scopus 로고
    • Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein
    • Bermak JC, Li M, Bullock C, Zhou QY. Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein. Nat Cell Biol 2001;3:492-498.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 492-498
    • Bermak, J.C.1    Li, M.2    Bullock, C.3    Zhou, Q.Y.4
  • 31
    • 0035341508 scopus 로고    scopus 로고
    • An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing
    • Scott DB, Blanpied TA, Swanson GT, Zhang C, Ehlers MD. An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing. J Neurosci 2001;21:3063-3072.
    • (2001) J. Neurosci. , vol.21 , pp. 3063-3072
    • Scott, D.B.1    Blanpied, T.A.2    Swanson, G.T.3    Zhang, C.4    Ehlers, M.D.5
  • 32
    • 0033538549 scopus 로고    scopus 로고
    • Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles
    • Martinez-Menarguez JA, Geuze HJ, Slot JW, Klumperman J. Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles. Cell 1999;98:81-90.
    • (1999) Cell , vol.98 , pp. 81-90
    • Martinez-Menarguez, J.A.1    Geuze, H.J.2    Slot, J.W.3    Klumperman, J.4
  • 33
    • 0035900480 scopus 로고    scopus 로고
    • Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles
    • Belden WJ, Barlowe C. Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles. Science 2001;294:1528-1531.
    • (2001) Science , vol.294 , pp. 1528-1531
    • Belden, W.J.1    Barlowe, C.2
  • 34
    • 0036196829 scopus 로고    scopus 로고
    • Erv14p Directs a transmembrane secretory protein into COPII-coated transport vesicles
    • Powers J, Barlowe C. Erv14p Directs a transmembrane secretory protein into COPII-coated transport vesicles. Mol Biol Cell 2002;13:880-891.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 880-891
    • Powers, J.1    Barlowe, C.2
  • 35
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • Schimmoller F, Singer-Kruger B, Schroder S, Kruger U, Barlowe C, Riezman H. The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBOJ 1995;14:1329-1339.
    • (1995) EMBO J. , vol.14 , pp. 1329-1339
    • Schimmoller, F.1    Singer-Kruger, B.2    Schroder, S.3    Kruger, U.4    Barlowe, C.5    Riezman, H.6
  • 36
    • 0034611009 scopus 로고    scopus 로고
    • The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles
    • Muniz M, Nuoffer C, Hauri HP, Riezman H. The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles. J Cell Biol 2000;148:925-930.
    • (2000) J. Cell Biol. , vol.148 , pp. 925-930
    • Muniz, M.1    Nuoffer, C.2    Hauri, H.P.3    Riezman, H.4
  • 37
    • 0030015550 scopus 로고    scopus 로고
    • Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations
    • Elrod-Erickson MJ, Kaiser CA. Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations. Mol Biol Cell 1996;7:1043-1058.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1043-1058
    • Elrod-Erickson, M.J.1    Kaiser, C.A.2
  • 38
    • 0035159694 scopus 로고    scopus 로고
    • Deletion of yeast p24 genes activates the unfolded protein response
    • Belden WJ, Barlowe C. Deletion of yeast p24 genes activates the unfolded protein response. Mol Biol Cell 2001;12:957-969.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 957-969
    • Belden, W.J.1    Barlowe, C.2
  • 43
    • 0032704952 scopus 로고    scopus 로고
    • Mannose-dependent endoplasmic reticulum (ER)-Golgi intermediate compartment-53-mediated ER to Golgi trafficking of coagulation factors V and VIII
    • Moussalli M, Pipe SW, Hauri HP, Nichols WC, Ginsburg D, Kaufman RJ. Mannose-dependent endoplasmic reticulum (ER)-Golgi intermediate compartment-53-mediated ER to Golgi trafficking of coagulation factors V and VIII. J Biol Chem 1999;274:32539-32542.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32539-32542
    • Moussalli, M.1    Pipe, S.W.2    Hauri, H.P.3    Nichols, W.C.4    Ginsburg, D.5    Kaufman, R.J.6
  • 45
    • 0033577803 scopus 로고    scopus 로고
    • LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum
    • Roberg KJ, Crotwell M, Espenshade P, Gimeno R, Kaiser CA. LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. J Cell Biol 1999;145:659-672.
    • (1999) J. Cell Biol. , vol.145 , pp. 659-672
    • Roberg, K.J.1    Crotwell, M.2    Espenshade, P.3    Gimeno, R.4    Kaiser, C.A.5
  • 46
    • 0034722347 scopus 로고    scopus 로고
    • Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae
    • Shimoni Y, Kurihara T, Ravazzola M, Amherdt M, Orci L, Schekman R. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol 2000;151:973-984.
    • (2000) J. Cell Biol. , vol.151 , pp. 973-984
    • Shimoni, Y.1    Kurihara, T.2    Ravazzola, M.3    Amherdt, M.4    Orci, L.5    Schekman, R.6
  • 47
    • 0032743154 scopus 로고    scopus 로고
    • Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles
    • Gilstring CF, Melin-Larsson M, Ljungdahl PO. Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles. Mol Biol Cell 1999;10:3549-3565.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3549-3565
    • Gilstring, C.F.1    Melin-Larsson, M.2    Ljungdahl, P.O.3
  • 48
    • 0032584717 scopus 로고    scopus 로고
    • Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs
    • Springer S, Schekman R. Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs. Science 1998;281:698-700.
    • (1998) Science , vol.281 , pp. 698-700
    • Springer, S.1    Schekman, R.2
  • 49
    • 0033616660 scopus 로고    scopus 로고
    • Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat protein complex II component Sec24p of endoplasmic reticulum-derived transport vesicles
    • Peng R, Grabowski R, De Antoni A, Gallwitz D. Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat protein complex II component Sec24p of endoplasmic reticulum-derived transport vesicles. Proc Natl Acad Sci USA 1999;96:3751-3756.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3751-3756
    • Peng, R.1    Grabowski, R.2    De Antoni, A.3    Gallwitz, D.4
  • 50
    • 0034698202 scopus 로고    scopus 로고
    • Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion
    • Allan BB, Moyer BD, Balch WE. Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion. Science 2000;289:444-448.
    • (2000) Science , vol.289 , pp. 444-448
    • Allan, B.B.1    Moyer, B.D.2    Balch, W.E.3
  • 51
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muniz M, Morsomme P, Riezman H. Protein sorting upon exit from the endoplasmic reticulum. Cell 2001;104:313-320.
    • (2001) Cell , vol.104 , pp. 313-320
    • Muniz, M.1    Morsomme, P.2    Riezman, H.3
  • 52
    • 0036200146 scopus 로고    scopus 로고
    • The Rab GTPase Ypt1p and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus
    • Morsomme P, Riezman H. The Rab GTPase Ypt1p and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus. Dev Cell 2002;2:307-317.
    • (2002) Dev. Cell , vol.2 , pp. 307-317
    • Morsomme, P.1    Riezman, H.2
  • 54
    • 0036187456 scopus 로고    scopus 로고
    • Direct interactions between rab GTPases and cargo
    • Smythe E. Direct interactions between rab GTPases and cargo. Mol Cell 2002;9:205-206.
    • (2002) Mol. Cell , vol.9 , pp. 205-206
    • Smythe, E.1
  • 55
    • 0036480017 scopus 로고    scopus 로고
    • Direct interaction between Rab3b and the polymeric immunoglobulin receptor controls ligand-stimulated transcytosis in epithelial cells
    • van ISC, Tuvim MJ, Weimbs T, Dickey BF, Mostov KE. Direct interaction between Rab3b and the polymeric immunoglobulin receptor controls ligand-stimulated transcytosis in epithelial cells. Dev Cell 2002:2:219-228.
    • (2002) Dev. Cell , vol.2 , pp. 219-228
    • van, I.S.C.1    Tuvim, M.J.2    Weimbs, T.3    Dickey, B.F.4    Mostov, K.E.5
  • 56
    • 0033153279 scopus 로고    scopus 로고
    • Functional organization of clathrin in coats: Combining electron cryomicroscopy and X-ray crystallography
    • Musacchio A, Smith CJ, Roseman AM, Harrison SC, Kirchhausen T, Pearse BM. Functional organization of clathrin in coats: Combining electron cryomicroscopy and X-ray crystallography. Mol Cell 1999;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
  • 57
    • 0024120843 scopus 로고
    • Receptors compete for adaptors found in plasma membrane coated pits
    • Pearse BM. Receptors compete for adaptors found in plasma membrane coated pits. EMBO J 1988;7:3331-3336.
    • (1988) EMBO J. , vol.7 , pp. 3331-3336
    • Pearse, B.M.1
  • 59
    • 0033522506 scopus 로고    scopus 로고
    • Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant μ2 subunit and its effects on endocytosis
    • Nesterov A, Carter RE, Sorkina T, Gill GN, Sorkin A. Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant μ2 subunit and its effects on endocytosis. EMBO J 1999;18:2489-2499.
    • (1999) EMBO J. , vol.18 , pp. 2489-2499
    • Nesterov, A.1    Carter, R.E.2    Sorkina, T.3    Gill, G.N.4    Sorkin, A.5
  • 60
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen DJ, Evans PR. A structural explanation for the recognition of tyrosine-based endocytotic signals. Science 1998;282:1327-1332.
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 62
    • 0033545185 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p
    • Zeng G, Cai M. Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p. J Cell Biol 1999;144:71-82.
    • (1999) J. Cell Biol. , vol.144 , pp. 71-82
    • Zeng, G.1    Cai, M.2
  • 63
    • 0037018152 scopus 로고    scopus 로고
    • Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis
    • Conner SD, Schmid SL. Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis. J Cell Biol 2002:156:921-929.
    • (2002) J. Cell Biol. , vol.156 , pp. 921-929
    • Conner, S.D.1    Schmid, S.L.2
  • 64
    • 0034118754 scopus 로고    scopus 로고
    • Identification of the universal cofactor (auxilin 2) in clathrin coat dissociation
    • [in Process Citation]
    • Umeda A, Meyerholz A, Ungewickell E. Identification of the universal cofactor (auxilin 2) in clathrin coat dissociation [in Process Citation]. Eur J Cell Biol 2000;79:336-342.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 336-342
    • Umeda, A.1    Meyerholz, A.2    Ungewickell, E.3
  • 65
    • 0035810915 scopus 로고    scopus 로고
    • Phosphorylation of threonine 156 of the μ2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo
    • Olusanya O, Andrews PD, Swedlow JR, Smythe E. Phosphorylation of threonine 156 of the μ2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo. Curr Biol 2001;11:896-900.
    • (2001) Curr. Biol. , vol.11 , pp. 896-900
    • Olusanya, O.1    Andrews, P.D.2    Swedlow, J.R.3    Smythe, E.4
  • 66
    • 0037018156 scopus 로고    scopus 로고
    • Phosphorylation of the AP2 μ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals
    • Ricotta D, Conner SD, Schmid SL, von Figura K, Honing S. Phosphorylation of the AP2 μ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals. J Cell Biol 2002;156:791-795.
    • (2002) J. Cell Biol. , vol.156 , pp. 791-795
    • Ricotta, D.1    Conner, S.D.2    Schmid, S.L.3    von Figura, K.4    Honing, S.5
  • 67
    • 0034669194 scopus 로고    scopus 로고
    • Dual interaction of synaptotagmin with μ2- and α-adaptin facilitates clathrin-coated pit nucleation
    • Haucke V, Wenk MR, Chapman ER, Farsad K, De Camilli P. Dual interaction of synaptotagmin with μ2- and α-adaptin facilitates clathrin-coated pit nucleation. EMBO J 2000;19:6011-6019.
    • (2000) EMBO J. , vol.19 , pp. 6011-6019
    • Haucke, V.1    Wenk, M.R.2    Chapman, E.R.3    Farsad, K.4    De Camilli, P.5
  • 68
    • 0033598129 scopus 로고    scopus 로고
    • Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits
    • Gaidarov I, Keen JH. Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits. J Cell Biol 1999;146:755-764.
    • (1999) J. Cell Biol. , vol.146 , pp. 755-764
    • Gaidarov, I.1    Keen, J.H.2
  • 69
    • 0035074215 scopus 로고    scopus 로고
    • Phosphoinositides in membrane traffic at the synapse
    • Cremona O, De Camilli P. Phosphoinositides in membrane traffic at the synapse. J Cell Sci 2001;114:1041-1052.
    • (2001) J. Cell Sci. , vol.114 , pp. 1041-1052
    • Cremona, O.1    De Camilli, P.2
  • 70
    • 0032585530 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation
    • Jost M, Simpson F, Kavran JM, Lemmon MA, Schmid SL. Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation. Curr Biol 1998;8:1399-1402.
    • (1998) Curr. Biol. , vol.8 , pp. 1399-1402
    • Jost, M.1    Simpson, F.2    Kavran, J.M.3    Lemmon, M.A.4    Schmid, S.L.5
  • 71
    • 0033580933 scopus 로고    scopus 로고
    • Coupled inositide phosphorylation and phospholipase D activation initiates clathrin-coat assembly on lysosomes
    • Arneson LS, Kunz J, Anderson RA, Traub LM. Coupled inositide phosphorylation and phospholipase D activation initiates clathrin-coat assembly on lysosomes. J Biol Chem 1999:274:17794-17805.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17794-17805
    • Arneson, L.S.1    Kunz, J.2    Anderson, R.A.3    Traub, L.M.4
  • 74
    • 0035824673 scopus 로고    scopus 로고
    • Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins
    • Mishra SK, Agostinelli NR, Brett TJ, Mizukami I, Ross TS, Traub LM. Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins. J Biol Chem 2001;276:46230-46236.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46230-46236
    • Mishra, S.K.1    Agostinelli, N.R.2    Brett, T.J.3    Mizukami, I.4    Ross, T.S.5    Traub, L.M.6
  • 75
    • 0032479444 scopus 로고    scopus 로고
    • Distinct saturable pathways for the endocytosis of different tyrosine motifs
    • Warren RA, Green FA, Stenberg PE, Enns CA. Distinct saturable pathways for the endocytosis of different tyrosine motifs. J Biol Chem 1998;273:17056-17063.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17056-17063
    • Warren, R.A.1    Green, F.A.2    Stenberg, P.E.3    Enns, C.A.4
  • 76
    • 12644259509 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain
    • Goodman OB Jr, Krupnick JG, Gurevich VV, Benovic JL, Keen JH. Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. J Biol Chem 1997;272:15017-15022.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15017-15022
    • Goodman O.B., Jr.1    Krupnick, J.G.2    Gurevich, V.V.3    Benovic, J.L.4    Keen, J.H.5
  • 77
    • 0037088608 scopus 로고    scopus 로고
    • β-arrestin/AP-2 interaction in G protein-coupled receptor internalization. Identification of a β-arrestin binding site in β2-adaptin
    • Laporte SA, Miller WE, Kim KM, Caron MG. β-arrestin/AP-2 interaction in G protein-coupled receptor internalization. Identification of a β-arrestin binding site in β2-adaptin. J Biol Chem 2002;277:9247-9254.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9247-9254
    • Laporte, S.A.1    Miller, W.E.2    Kim, K.M.3    Caron, M.G.4
  • 78
    • 0033557715 scopus 로고    scopus 로고
    • Arrestin function in G protein-coupled receptor endocytosis requires phosphoinositide binding
    • Gaidarov I, Krupnick JG, Falck JR, Benovic JL, Keen JH. Arrestin function in G protein-coupled receptor endocytosis requires phosphoinositide binding. EMBO J 1999;18:871-881.
    • (1999) EMBO J. , vol.18 , pp. 871-881
    • Gaidarov, I.1    Krupnick, J.G.2    Falck, J.R.3    Benovic, J.L.4    Keen, J.H.5
  • 79
    • 0037128214 scopus 로고    scopus 로고
    • G protein-coupled receptor/arrestin3 modulation of the endocytic machinery
    • Santini F, Gaidarov I, Keen JH. G protein-coupled receptor/arrestin3 modulation of the endocytic machinery. J Cell Biol 2002;156:665-676.
    • (2002) J. Cell Biol. , vol.156 , pp. 665-676
    • Santini, F.1    Gaidarov, I.2    Keen, J.H.3
  • 80
    • 0036278105 scopus 로고    scopus 로고
    • Accessory protein recruitment motifs in clathrin-mediated endocytosis
    • Brett TJ, Traub LM, Fremont DH. Accessory protein recruitment motifs in clathrin-mediated endocytosis. Structure 2002;10:797-809.
    • (2002) Structure , vol.10 , pp. 797-809
    • Brett, T.J.1    Traub, L.M.2    Fremont, D.H.3
  • 81
    • 0033005568 scopus 로고    scopus 로고
    • Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery
    • Kay BK, Yamabhai M, Wendland B, Emr SD. Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery. Protein Sci 1999;8:435-438.
    • (1999) Protein Sci. , vol.8 , pp. 435-438
    • Kay, B.K.1    Yamabhai, M.2    Wendland, B.3    Emr, S.D.4
  • 82
    • 0035134328 scopus 로고    scopus 로고
    • Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis
    • Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science 2001:291:1047-1051.
    • (2001) Science , vol.291 , pp. 1047-1051
    • Itoh, T.1    Koshiba, S.2    Kigawa, T.3    Kikuchi, A.4    Yokoyama, S.5    Takenawa, T.6
  • 84
    • 0037066145 scopus 로고    scopus 로고
    • Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis
    • Milano SK, Pace HC, Kim YM, Brenner C, Benovic JL Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis. Biochemistry 2002;41:3321-3328.
    • (2002) Biochemistry , vol.41 , pp. 3321-3328
    • Milano, S.K.1    Pace, H.C.2    Kim, Y.M.3    Brenner, C.4    Benovic, J.L.5
  • 86
    • 0034235434 scopus 로고    scopus 로고
    • Ubiquitination and endocytosis of plasma membrane proteins: Role of Nedd4/Rsp5p family of ubiquitin-protein ligases
    • Rotin D, Staub O, Haguenauer-Tsapis R. Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4/Rsp5p family of ubiquitin-protein ligases. J Membr Biol 2000;176:1-17.
    • (2000) J. Membr. Biol. , vol.176 , pp. 1-17
    • Rotin, D.1    Staub, O.2    Haguenauer-Tsapis, R.3
  • 87
    • 0035369556 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems
    • Hofmann K, Falquet L. A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems. Trends Biochem Sci 2001:26:347-350.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 347-350
    • Hofmann, K.1    Falquet, L.2
  • 89
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Shih SC, Katzmann DJ, Schnell JD, Sutanto M, Emr SD, Hicke L. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat Cell Biol 2002;4:389-393.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 389-393
    • Shih, S.C.1    Katzmann, D.J.2    Schnell, J.D.3    Sutanto, M.4    Emr, S.D.5    Hicke, L.6
  • 90
    • 0035099375 scopus 로고    scopus 로고
    • Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2
    • Morris SM, Cooper JA. Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2. Traffic 2001;2:111-123.
    • (2001) Traffic , vol.2 , pp. 111-123
    • Morris, S.M.1    Cooper, J.A.2
  • 92
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor
    • Chen WJ, Goldstein JL, Brown MS. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J Biol Chem 1990;265:3116-3123.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3116-3123
    • Chen, W.J.1    Goldstein, J.L.2    Brown, M.S.3
  • 93
    • 0037007229 scopus 로고    scopus 로고
    • Dual roles for the Dab2 adaptor protein in embryonic development and kidney transport
    • Morris SM, Tallquist MD, Rock CO, Cooper JA. Dual roles for the Dab2 adaptor protein in embryonic development and kidney transport. EMBO J 2002;21:1555-1564.
    • (2002) EMBO J. , vol.21 , pp. 1555-1564
    • Morris, S.M.1    Tallquist, M.D.2    Rock, C.O.3    Cooper, J.A.4
  • 94
    • 0034193309 scopus 로고    scopus 로고
    • Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin
    • Oleinikov AV, Zhao J, Makker SP. Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin. Biochem J 2000;347 Part 3:613-621.
    • (2000) Biochem. J. , vol.347 , Issue.PART 3 , pp. 613-621
    • Oleinikov, A.V.1    Zhao, J.2    Makker, S.P.3
  • 97
    • 0036668808 scopus 로고    scopus 로고
    • The μ2 subunit of the clathrin AP-2 binds to FDNPVY and YppΦ sorting signals at distinct sites
    • in press
    • Boll W, Prapoport I, Brunner C, Modis Y, Prehn S, Kirchhausen T. The μ2 subunit of the clathrin AP-2 binds to FDNPVY and YppΦ sorting signals at distinct sites. Traffic 2002;3:in press.
    • (2002) Traffic , vol.3
    • Boll, W.1    Prapoport, I.2    Brunner, C.3    Modis, Y.4    Prehn, S.5    Kirchhausen, T.6
  • 98
    • 0032728972 scopus 로고    scopus 로고
    • Characterization of a novel cellular defect in patients with phenotypic homozygous familial hypercholesterolemia
    • Norman D, Sun XM, Bourbon M, Knight BL, Naoumova RP, Soutar AK. Characterization of a novel cellular defect in patients with phenotypic homozygous familial hypercholesterolemia. J Clin Invest 1999;104:619-628.
    • (1999) J. Clin. Invest. , vol.104 , pp. 619-628
    • Norman, D.1    Sun, X.M.2    Bourbon, M.3    Knight, B.L.4    Naoumova, R.P.5    Soutar, A.K.6
  • 99
    • 0033575748 scopus 로고    scopus 로고
    • Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis
    • Wendland B, Steece KE, Emr SD. Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. EMBO J 1999;18:4383-4393.
    • (1999) EMBO J. , vol.18 , pp. 4383-4393
    • Wendland, B.1    Steece, K.E.2    Emr, S.D.3
  • 100
    • 0037092043 scopus 로고    scopus 로고
    • Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis
    • Howard JP, Hutton JL, Olson JM, Payne GS. Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis. J Cell Biol 2002;157:315-326.
    • (2002) J. Cell Biol. , vol.157 , pp. 315-326
    • Howard, J.P.1    Hutton, J.L.2    Olson, J.M.3    Payne, G.S.4
  • 101
    • 0035834428 scopus 로고    scopus 로고
    • Regulation of receptor fate by ubiquitination of activated β2-adrenergic receptor and β-arrestin
    • Shenoy SK, McDonald PH, Kohout TA, Lefkowitz RJ. Regulation of receptor fate by ubiquitination of activated β2-adrenergic receptor and β-arrestin. Science 2001;294:1307-1313.
    • (2001) Science , vol.294 , pp. 1307-1313
    • Shenoy, S.K.1    McDonald, P.H.2    Kohout, T.A.3    Lefkowitz, R.J.4
  • 102
    • 0035510916 scopus 로고    scopus 로고
    • The dephosphins: Dephosphorylation by calcineurin triggers synaptic vesicle endocytosis
    • Cousin MA, Robinson PJ. The dephosphins: Dephosphorylation by calcineurin triggers synaptic vesicle endocytosis. Trends Neurosci 2001;24:659-665.
    • (2001) Trends Neurosci. , vol.24 , pp. 659-665
    • Cousin, M.A.1    Robinson, P.J.2
  • 103
    • 0035196516 scopus 로고    scopus 로고
    • In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation
    • Watson HA, Cope MJ, Groen AC, Drubin DG, Wendland B. In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation. Mol Biol Cell 2001;12:3668-3679.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3668-3679
    • Watson, H.A.1    Cope, M.J.2    Groen, A.C.3    Drubin, D.G.4    Wendland, B.5
  • 104
    • 0035943416 scopus 로고    scopus 로고
    • Intracellular cycling of lysosomal enzyme receptors: Cytoplasmic tails' tales
    • Dell'Angelica EC, Payne GS. Intracellular cycling of lysosomal enzyme receptors: Cytoplasmic tails' tales. Cell 2001;106:395-398.
    • (2001) Cell , vol.106 , pp. 395-398
    • Dell'Angelica, E.C.1    Payne, G.S.2
  • 105
    • 0035341464 scopus 로고    scopus 로고
    • PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic
    • Crump CM, Xiang Y, Thomas L, Gu F, Austin C, Tooze SA, Thomas G. PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic. EMBO J 2001;20:2191-2201.
    • (2001) EMBO J. , vol.20 , pp. 2191-2201
    • Crump, C.M.1    Xiang, Y.2    Thomas, L.3    Gu, F.4    Austin, C.5    Tooze, S.A.6    Thomas, G.7


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