메뉴 건너뛰기




Volumn 136, Issue 2, 1997, Pages 287-297

Two separate signals act independently to localize a yeast late Golgi membrane protein through a combination of retrieval and retention

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; MEMBRANE PROTEIN;

EID: 0031055434     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.136.2.287     Document Type: Article
Times cited : (83)

References (51)
  • 1
    • 0030012162 scopus 로고    scopus 로고
    • Novel syntaxin homologue, Pep12p, required for the sorting of tumenal hydrolases to the lysosome-like vacuole in yeast
    • Becherer, K.A., S.E. Rieder, S.D. Emr, and E.W. Jones. 1996. Novel syntaxin homologue, Pep12p, required for the sorting of tumenal hydrolases to the lysosome-like vacuole in yeast. Mol. Biol. Cell. 7:579-594.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 579-594
    • Becherer, K.A.1    Rieder, S.E.2    Emr, S.D.3    Jones, E.W.4
  • 2
    • 0026334441 scopus 로고
    • Localization of cathepsin D in endosomes: Characterization and biological importance
    • Blum, J.S., M.L. Fiani, and P.D. Stahl. 1991. Localization of cathepsin D in endosomes: characterization and biological importance. Adv. Exp. Med. Biol. 306:281-287.
    • (1991) Adv. Exp. Med. Biol. , vol.306 , pp. 281-287
    • Blum, J.S.1    Fiani, M.L.2    Stahl, P.D.3
  • 3
    • 0027159260 scopus 로고
    • TGN38 is maintained in the transGolgi network by a tyrosine-containing motif in the cytoplasmic domain
    • Bos, K., C. Wraight, and K.K. Stanley. 1993. TGN38 is maintained in the transGolgi network by a tyrosine-containing motif in the cytoplasmic domain. EMBO (Eur. Mol. Biol. Organ.) J. 12:2219-2228.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 2219-2228
    • Bos, K.1    Wraight, C.2    Stanley, K.K.3
  • 4
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher, M.S., and S. Munro. 1993. Cholesterol and the Golgi apparatus. Science (Wash. DC). 261:1280-1281.
    • (1993) Science (Wash. DC) , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 5
    • 0027443775 scopus 로고
    • Immunoisolation of Kex2p-containing organelles from yeast demonstrates colocalisation of three processing proteinases to a single Golgi compartment
    • Bryant, N.J., and A. Boyd. 1993. Immunoisolation of Kex2p-containing organelles from yeast demonstrates colocalisation of three processing proteinases to a single Golgi compartment. J. Cell Sci. 106:815-822.
    • (1993) J. Cell Sci. , vol.106 , pp. 815-822
    • Bryant, N.J.1    Boyd, A.2
  • 6
    • 0025990745 scopus 로고
    • Localization of the signal for rapid internalization of the bovine cation-independent mannose 6-phosphate/insulin-like growth factor-II receptor to amino acids 24-29 of the cytoplasmic tail
    • Canfield, W.M., R.D. Johnson, R.D. Ye, W. Gregory, and S. Kornfeld. 1991. Localization of the signal for rapid internalization of the bovine cation-independent mannose 6-phosphate/insulin-like growth factor-II receptor to amino acids 24-29 of the cytoplasmic tail. J. Biol. Chem. 266:5682-5688.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5682-5688
    • Canfield, W.M.1    Johnson, R.D.2    Ye, R.D.3    Gregory, W.4    Kornfeld, S.5
  • 7
    • 0029088909 scopus 로고
    • The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function, and localization
    • Cereghino, J.L., E.G. Marcusson, and S.D. Emr. 1995. The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function, and localization. Mol. Biol. Cell. 6:1089-1102.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1089-1102
    • Cereghino, J.L.1    Marcusson, E.G.2    Emr, S.D.3
  • 8
    • 0027961075 scopus 로고
    • The functioning of the yeast Golgi apparatus requires an ER protein encoded by ANP1, a member of a new family of genes affecting the secretory pathway
    • Chapman, R.E., and S. Munro. 1994. The functioning of the yeast Golgi apparatus requires an ER protein encoded by ANP1, a member of a new family of genes affecting the secretory pathway. EMBO (Eur. Mol. Biol. Organ.) J. 13:4896-4907.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 4896-4907
    • Chapman, R.E.1    Munro, S.2
  • 9
    • 0027085824 scopus 로고
    • Yeast Kex1p is a Golgi-associated membrane protein: Deletions in a cytoplasmic targeting domain result in mislocalization to the vacuolar membrane
    • Cooper, A.A., and H. Bussey. 1992. Yeast Kex1p is a Golgi-associated membrane protein: deletions in a cytoplasmic targeting domain result in mislocalization to the vacuolar membrane. J. Cell Biol. 119:1459-1468.
    • (1992) J. Cell Biol. , vol.119 , pp. 1459-1468
    • Cooper, A.A.1    Bussey, H.2
  • 10
    • 0029905298 scopus 로고    scopus 로고
    • Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases
    • Cooper, A.A., and T.H. Stevens. 1996. Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases. J. Cell Biol. 133:529-541.
    • (1996) J. Cell Biol. , vol.133 , pp. 529-541
    • Cooper, A.A.1    Stevens, T.H.2
  • 11
    • 0026097957 scopus 로고
    • Localization of components involved in protein transport and processing through the yeast Golgi apparatus
    • Franzusoff, A., K. Redding, J. Crosby, R.S. Fuller, and R. Schekman. 1991. Localization of components involved in protein transport and processing through the yeast Golgi apparatus. J. Cell Biol. 112:27-37.
    • (1991) J. Cell Biol. , vol.112 , pp. 27-37
    • Franzusoff, A.1    Redding, K.2    Crosby, J.3    Fuller, R.S.4    Schekman, R.5
  • 12
    • 0025823035 scopus 로고
    • Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant
    • Graham, T.R., and S.D. Emr. 1991. Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant. J. Cell Biol. 114:207-218.
    • (1991) J. Cell Biol. , vol.114 , pp. 207-218
    • Graham, T.R.1    Emr, S.D.2
  • 13
    • 0028980860 scopus 로고
    • Sorting of yeast alpha 1,3 mannosyltransferase is mediated by a lumenal domain interaction, and a transmembrane domain signal that can confer clathrin-dependent Golgi localization to a secreted protein
    • Graham, T.R., and V.A. Krasnov. 1995. Sorting of yeast alpha 1,3 mannosyltransferase is mediated by a lumenal domain interaction, and a transmembrane domain signal that can confer clathrin-dependent Golgi localization to a secreted protein. Mol. Biol. Cell. 6:809-824.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 809-824
    • Graham, T.R.1    Krasnov, V.A.2
  • 14
    • 0029864907 scopus 로고    scopus 로고
    • Localization of a yeast early Golgi mannosyltransferase, Och1p, involves retrograde transport
    • Harris, S., and M.G. Waters. 1996. Localization of a yeast early Golgi mannosyltransferase, Och1p, involves retrograde transport. J. Cell Biol. 132:985-988.
    • (1996) J. Cell Biol. , vol.132 , pp. 985-988
    • Harris, S.1    Waters, M.G.2
  • 15
    • 0027395956 scopus 로고
    • Localization of TGN38 to the trans-Golgi network: Involvement of a cytoplasmic tyrosine-containing sequence
    • Humphrey, J.S., P.J. Peters, L.C. Yuan, and J.S. Bonifacino. 1992. Localization of TGN38 to the trans-Golgi network: involvement of a cytoplasmic tyrosine-containing sequence. J. Cell Biol. 120:1123-1135.
    • (1992) J. Cell Biol. , vol.120 , pp. 1123-1135
    • Humphrey, J.S.1    Peters, P.J.2    Yuan, L.C.3    Bonifacino, J.S.4
  • 16
    • 0024447838 scopus 로고
    • Membrane protein sorting: Biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase
    • Kilonsky, D.J., and S.D. Emr. 1989. Membrane protein sorting: biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase. EMBO (Eur. Mol. Biol. Organ.) J. 8:2241-2250.
    • (1989) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 2241-2250
    • Kilonsky, D.J.1    Emr, S.D.2
  • 17
    • 0026637316 scopus 로고
    • Structure and function of the mannose-6-phosphate/insulin growth factor-II receptors
    • Kornfeld, S. 1992. Structure and function of the mannose-6-phosphate/insulin growth factor-II receptors. Annu. Rev. Biochem. 61:307-330.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 18
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., J.D. Roberts, and R.A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 19
    • 0026604647 scopus 로고
    • Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum
    • Lewis, M.J., and H.R. Pelham. 1992. Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum. Cell. 68:353-364.
    • (1992) Cell , vol.68 , pp. 353-364
    • Lewis, M.J.1    Pelham, H.R.2
  • 20
    • 0028832626 scopus 로고
    • Localization and targeting of the Saccharomyces cerevisiae Kre2p/Mnt1p alpha 1,2-mannosyltransferase to a medial-Golgi compartment
    • Lussier, M., M. Sdicu, T. Ketela, and H. Bussey. 1995. Localization and targeting of the Saccharomyces cerevisiae Kre2p/Mnt1p alpha 1,2-mannosyltransferase to a medial-Golgi compartment. J. Cell Biol. 131:913-927.
    • (1995) J. Cell Biol. , vol.131 , pp. 913-927
    • Lussier, M.1    Sdicu, M.2    Ketela, T.3    Bussey, H.4
  • 21
    • 0027227549 scopus 로고
    • Retention of a cis-Golgi protein requires polar residues on one face of a predicted alpha-helix in the transmembrane domain
    • Machamer, C.E., M.G. Grim, A. Esquela, S.W. Chung, M. Rolls, K. Ryan, and A.M. Swift. 1993. Retention of a cis-Golgi protein requires polar residues on one face of a predicted alpha-helix in the transmembrane domain. Mol. Biol. Cell. 4:695-704.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 695-704
    • Machamer, C.E.1    Grim, M.G.2    Esquela, A.3    Chung, S.W.4    Rolls, M.5    Ryan, K.6    Swift, A.M.7
  • 23
    • 0028332917 scopus 로고
    • The sorting receptor for yeast carboxypeptidase Y is en- Coded by the VPS10 gene
    • Marcusson, E.G., B.F. Horazdovsky, J.L. Cereghino, E. Gharakhanian, and S.D. Emr. 1994. The sorting receptor for yeast carboxypeptidase Y is en- coded by the VPS10 gene. Cell. 77:579-586.
    • (1994) Cell , vol.77 , pp. 579-586
    • Marcusson, E.G.1    Horazdovsky, B.F.2    Cereghino, J.L.3    Gharakhanian, E.4    Emr, S.D.5
  • 24
    • 0025990802 scopus 로고
    • Sequences within and adjacent to the transmembrane segment of alpha-2,6-sialyltransferase specify Golgi retention
    • Munro, S. 1991. Sequences within and adjacent to the transmembrane segment of alpha-2,6-sialyltransferase specify Golgi retention. EMBO (Eur. Mol. Biol. Organ.) J. 10:3577-3588.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 3577-3588
    • Munro, S.1
  • 25
    • 0026072695 scopus 로고
    • The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization
    • Nilsson, T., J.M. Lucocq, D. Mackay, and G. Warren. 1991. The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization. EMBO (Eur. Mol. Biol. Organ.) J. 10:3567-3575.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 3567-3575
    • Nilsson, T.1    Lucocq, J.M.2    Mackay, D.3    Warren, G.4
  • 26
    • 0027318045 scopus 로고
    • Kin recognition. A model for the retention of Golgi enzymes
    • Nilsson, T., P. Slusarewicz, M.H. Hoe, and G. Warren. 1993. Kin recognition. A model for the retention of Golgi enzymes. FEBS Lett. 330:1-4.
    • (1993) FEBS Lett. , vol.330 , pp. 1-4
    • Nilsson, T.1    Slusarewicz, P.2    Hoe, M.H.3    Warren, G.4
  • 27
    • 0028283489 scopus 로고
    • Sorting of membrane proteins in the yeast secretory pathway
    • Nothwehr, S.F., and T.H. Stevens. 1994. Sorting of membrane proteins in the yeast secretory pathway. J. Biol. Chem. 269:10185-10188.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10185-10188
    • Nothwehr, S.F.1    Stevens, T.H.2
  • 28
    • 0027204816 scopus 로고
    • Membrane protein retention in the yeast Golgi apparatus: Dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues
    • Nothwehr, S.F., C.J. Roberts, and T.H. Stevens. 1993. Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues. J Cell Biol. 121:1197-1209.
    • (1993) J Cell Biol. , vol.121 , pp. 1197-1209
    • Nothwehr, S.F.1    Roberts, C.J.2    Stevens, T.H.3
  • 29
    • 0028953080 scopus 로고
    • Golgi and vacuolar membrane proteins reach the vacuole in vps1 mutant yeast cells via the plasma membrane
    • Nothwehr, S.F., E. Conibear, and T.H. Stevens. 1995. Golgi and vacuolar membrane proteins reach the vacuole in vps1 mutant yeast cells via the plasma membrane. J. Cell Biol. 129:35-46.
    • (1995) J. Cell Biol. , vol.129 , pp. 35-46
    • Nothwehr, S.F.1    Conibear, E.2    Stevens, T.H.3
  • 30
    • 0030013324 scopus 로고    scopus 로고
    • The newly identified yeast GRD genes are required for retention of late-Golgi membrane proteins
    • Nothwehr, S.F., N.J. Bryant, and T.H. Stevens. 1996. The newly identified yeast GRD genes are required for retention of late-Golgi membrane proteins. Mol. Cell. Biol. 16:2700-2707.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2700-2707
    • Nothwehr, S.F.1    Bryant, N.J.2    Stevens, T.H.3
  • 31
    • 0027067882 scopus 로고
    • Alternative pathways for the sorting of soluble vacuolar proteins in yeast: A vps35 null mutant missorts and secretes only a subset of vacuolar hydrolases
    • Paravicini, G., B.F. Horazdovsky, and S.D. Emr. 1992. Alternative pathways for the sorting of soluble vacuolar proteins in yeast: a vps35 null mutant missorts and secretes only a subset of vacuolar hydrolases. Mol. Biol. Cell. 3:415-427.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 415-427
    • Paravicini, G.1    Horazdovsky, B.F.2    Emr, S.D.3
  • 32
    • 0027489133 scopus 로고
    • Sorting of membrane proteins in the secretory pathway
    • Pelham, H.R., and S. Munro. 1993. Sorting of membrane proteins in the secretory pathway. Cell. 75:603-605.
    • (1993) Cell , vol.75 , pp. 603-605
    • Pelham, H.R.1    Munro, S.2
  • 33
    • 0028800173 scopus 로고
    • VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae
    • Piper, R.C., A.A. Cooper, H. Yang, and T.H. Stevens. 1995. VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae. J. Cell Biol. 131:603-617.
    • (1995) J. Cell Biol. , vol.131 , pp. 603-617
    • Piper, R.C.1    Cooper, A.A.2    Yang, H.3    Stevens, T.H.4
  • 34
    • 0028595960 scopus 로고
    • Yeast Vps45p is a Sec1p-like protein required for the consumption of vacuole-targeted, post-Golgi transport vesicles
    • Piper, R.C., E.A. Whitters, and T.H. Stevens. 1994. Yeast Vps45p is a Sec1p-like protein required for the consumption of vacuole-targeted, post-Golgi transport vesicles. Eur. J. Cell Biol. 65:305-318.
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 305-318
    • Piper, R.C.1    Whitters, E.A.2    Stevens, T.H.3
  • 35
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class E vps mutants
    • Raymond, C.K., I. Howald-Stevenson, C.A. Vater, and T.H. Stevens. 1992. Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants. Mol. Biol. Cell. 3:1389-1402.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1389-1402
    • Raymond, C.K.1    Howald-Stevenson, I.2    Vater, C.A.3    Stevens, T.H.4
  • 36
    • 0025752784 scopus 로고
    • Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae
    • Redding, K., C. Holcomb, and R.S. Fuller. 1991. Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae. J. Cell Biol. 113:527-538.
    • (1991) J. Cell Biol. , vol.113 , pp. 527-538
    • Redding, K.1    Holcomb, C.2    Fuller, R.S.3
  • 37
    • 0026727566 scopus 로고
    • Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default compartment
    • Roberts, C.J., S.F. Nothwehr, and T.H. Stevens. 1992. Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment. J. Cell Biol. 119:69-83.
    • (1992) J. Cell Biol. , vol.119 , pp. 69-83
    • Roberts, C.J.1    Nothwehr, S.F.2    Stevens, T.H.3
  • 38
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. 1994. Mechanisms of intracellular protein transport. Nature (Lond.). 372:55-63.
    • (1994) Nature (Lond.) , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 39
    • 0029071584 scopus 로고
    • Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin
    • Schafer, W., A. Stroh, S. Berghofer, J. Seiler, M. Vey, M.L. Kruse, H.F. Kern, H.D. Klenk, and W. Garten. 1995. Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin. EMBO (Eur. Mol. Biol. Organ.) J. 14:2424-2435.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 2424-2435
    • Schafer, W.1    Stroh, A.2    Berghofer, S.3    Seiler, J.4    Vey, M.5    Kruse, M.L.6    Kern, H.F.7    Klenk, H.D.8    Garten, W.9
  • 40
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and L. Orci. 1996. Coat proteins and vesicle budding. Science (Wash. DC). 271:1526-1533.
    • (1996) Science (Wash. DC) , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 41
    • 0027449288 scopus 로고
    • Involvement of Ypt7p, a small GTPase, in traffic from late endosome to the vacuole in yeast
    • Schimmoller, F., and H. Riezman. 1993. Involvement of Ypt7p, a small GTPase, in traffic from late endosome to the vacuole in yeast. J. Cell Sci. 106:823-830.
    • (1993) J. Cell Sci. , vol.106 , pp. 823-830
    • Schimmoller, F.1    Riezman, H.2
  • 42
    • 0003529274 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sherman, F., G.R. Fink, and J. Hicks. 1986. Methods in yeast genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 61-64.
    • (1986) Methods in Yeast Genetics , pp. 61-64
    • Sherman, F.1    Fink, G.R.2    Hicks, J.3
  • 43
    • 0001134626 scopus 로고
    • Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sprague, G.F., and J. Thorner. 1992. Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae. In The Molecular and Cellular Biology of the Yeast Saccharomyces cerevisiae. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 657-744.
    • (1992) The Molecular and Cellular Biology of the Yeast Saccharomyces Cerevisiae , pp. 657-744
    • Sprague, G.F.1    Thorner, J.2
  • 44
    • 0025940737 scopus 로고
    • A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein
    • Swift, A.M., and C.E. Machamer. 1991, A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein. J. Cell Biol. 115:19-30.
    • (1991) J. Cell Biol. , vol.115 , pp. 19-30
    • Swift, A.M.1    Machamer, C.E.2
  • 45
    • 0028875689 scopus 로고
    • Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain
    • Takahashi, S., T. Nakagawa, T. Banno, T. Watanabe, K. Murakami, and K. Nakayama. 1995. Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain. J. Biol. Chem. 270:28397-28401.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28397-28401
    • Takahashi, S.1    Nakagawa, T.2    Banno, T.3    Watanabe, T.4    Murakami, K.5    Nakayama, K.6
  • 46
    • 0027326627 scopus 로고
    • Mutational analysis of the human KDEL receptor: Distinct structural requirements for Golgi retention, ligand binding and retrograde transport
    • Townsley, F.M., D.W. Wilson, and H.R. Pelham. 1993. Mutational analysis of the human KDEL receptor: distinct structural requirements for Golgi retention, ligand binding and retrograde transport. EMBO (Eur. Mol. Biol. Organ.) J. 12:2821-2829.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 2821-2829
    • Townsley, F.M.1    Wilson, D.W.2    Pelham, H.R.3
  • 47
    • 0028839910 scopus 로고
    • An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface
    • Voorhees, P., E. Deignan, E. van Donselaar, J. Humphrey, M.S. Marks, P.J. Peters, and J.S. Bonifacino. 1995. An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface. EMBO (Eur. Mol. Biol. Organ.) J. 14:4961-1975.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 4961-11975
    • Voorhees, P.1    Deignan, E.2    Van Donselaar, E.3    Humphrey, J.4    Marks, M.S.5    Peters, P.J.6    Bonifacino, J.S.7
  • 48
    • 0025930734 scopus 로고
    • Posttranslational processing of the prohormone-cleaving Kex2 protease in the Saccharomyces cerevisiae secretory pathway
    • Wilcox, C.A., and R.S. Fuller. 1991. Posttranslational processing of the prohormone-cleaving Kex2 protease in the Saccharomyces cerevisiae secretory pathway. J. Cell Biol. 115:297-307.
    • (1991) J. Cell Biol. , vol.115 , pp. 297-307
    • Wilcox, C.A.1    Fuller, R.S.2
  • 49
    • 0027080272 scopus 로고
    • Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole
    • Wilcox, CA., K. Redding, R. Wright, and R.S. Fuller. 1992. Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole. Mol. Biol. Cell. 3:1353-1371.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1353-1371
    • Wilcox, C.A.1    Redding, K.2    Wright, R.3    Fuller, R.S.4
  • 50
    • 0027379234 scopus 로고
    • Dynamic retention of TGN membrane proteins in Saccharomyces cerevisiae
    • Wilsbach, K., and G. Payne. 1993. Dynamic retention of TGN membrane proteins in Saccharomyces cerevisiae. Trends Cell Biol. 3:426-432.
    • (1993) Trends Cell Biol. , vol.3 , pp. 426-432
    • Wilsbach, K.1    Payne, G.2
  • 51
    • 0027519431 scopus 로고
    • The SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans Golgi network localization
    • Wong, S.H., and W. Hong. 1993. The SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans Golgi network localization. J. Biol. Chem. 268:22853-22862.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22853-22862
    • Wong, S.H.1    Hong, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.