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Volumn 4, Issue 3, 2003, Pages 202-212

Mannose 6-phosphate receptors: New twists in the tale

Author keywords

[No Author keywords available]

Indexed keywords

ACID HYDROLASE; GRANZYME B; LIGAND; LYSOSOME ENZYME; PLASMINOGEN; PROLIFERIN; RETINOIC ACID; SOMATOMEDIN B; SOMATOMEDIN B RECEPTOR; TRANSFORMING GROWTH FACTOR BETA1; UROKINASE RECEPTOR;

EID: 0037336348     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1050     Document Type: Review
Times cited : (868)

References (134)
  • 2
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/insulin like growth factor II receptors
    • Kornfeld, S. Structure and function of the mannose 6-phosphate/insulin like growth factor II receptors. Annu. Rev. Biochem. 61, 307-330 (1992).
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 3
    • 0029089823 scopus 로고
    • Mannose 6-phosphate receptors in sorting and transport of lysosomal enzymes
    • Hille-Rehfeld, A. Mannose 6-phosphate receptors in sorting and transport of lysosomal enzymes. Biochim. Biophys. Acta. 1241, 177-194 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 177-194
    • Hille-Rehfeld, A.1
  • 4
    • 0032516810 scopus 로고    scopus 로고
    • Protein transport from the secretory to the endocytic pathway in mammalian cells
    • Le Borgne, R. & Hoflack, B. Protein transport from the secretory to the endocytic pathway in mammalian cells Biochim. Biophys. Acta. 1404, 195-209 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 195-209
    • Le Borgne, R.1    Hoflack, B.2
  • 5
    • 0023840372 scopus 로고
    • Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor
    • Lobel, P., Dahms, N. M. & Kornfeld, S. Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor. J. Biol. Chem. 263, 2563-2570 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 2563-2570
    • Lobel, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 6
    • 0037192762 scopus 로고    scopus 로고
    • Identification of residues essential for carbohydrate recognition by the insulin-like growth factor II/mannose 6-phosphate receptor
    • Hancock, M. K., Haskins, D. J., Sun, G. & Dahms, N. M. Identification of residues essential for carbohydrate recognition by the insulin-like growth factor II/mannose 6-phosphate receptor J. Biol. Chem. 277, 11255-11264 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 11255-11264
    • Hancock, M.K.1    Haskins, D.J.2    Sun, G.3    Dahms, N.M.4
  • 7
    • 0034056050 scopus 로고    scopus 로고
    • Recognition of Dictyostelium discoideum lysosomal enzymes is conferred by the amino-terminal carbohydrate binding site of the insulin-like growth factor II/mannose 6-phosphate receptor
    • Marron-Terada, P. G., Hancock, D. J., Haskins, D. J. & Dahms, N, M. Recognition of Dictyostelium discoideum lysosomal enzymes is conferred by the amino-terminal carbohydrate binding site of the insulin-like growth factor II/mannose 6-phosphate receptor. Biochemistry 39, 2243-2253 (2000).
    • (2000) Biochemistry , vol.39 , pp. 2243-2253
    • Marron-Terada, P.G.1    Hancock, D.J.2    Haskins, D.J.3    Dahms, N.M.4
  • 8
    • 0029076383 scopus 로고
    • Localization of the insulin-like growth factor II binding site to amino aods 1508-1566 in repeat 11 of the mannose 6-phosphate/insulin-like growth factor II receptor
    • Schmidt, B., Kiecke-Siemsen, C., Waheed, A., Braulke, T. & von Figura, K. Localization of the insulin-like growth factor II binding site to amino aods 1508-1566 in repeat 11 of the mannose 6-phosphate/insulin-like growth factor II receptor J. Biol. Chem. 270, 14975-14982 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 14975-14982
    • Schmidt, B.1    Kiecke-Siemsen, C.2    Waheed, A.3    Braulke, T.4    Von Figura, K.5
  • 9
    • 0029969904 scopus 로고    scopus 로고
    • Truncated forms of the insulin-like growth factor II (IGF-II)/mannose 6-phosphate receptor encompassing the IGF-II binding site: Characterization of a point mutation that abolishes IGF-II binding
    • Garmroudi, F., Devi, G., Slentz, D. H. Schaffe, B. S. & MacDonald, R. G. Truncated forms of the insulin-like growth factor II (IGF-II)/mannose 6-phosphate receptor encompassing the IGF-II binding site: characterization of a point mutation that abolishes IGF-II binding. Mol. Endocrinol. 10, 642-651 (1996). References 6-9 characterize the carbohydrata-binding domain and the IGF-II-binding site on the Cl-MPR.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 642-651
    • Garmroudi, F.1    Devi, G.2    Slentz, D.H.3    Schaffe, B.S.4    MacDonald, R.G.5
  • 10
    • 0025195684 scopus 로고
    • Phosphorylation of the cytoplasmic domain to the bovine cation-independent mannose 6-phosphate receptor Serines 2421 and 2492 are the targets of a casein kinase II associated to the Golgi-derived HAI adaptor complex
    • Meresse, S., Ludwig, T. Frank, R. & Hoflack B. Phosphorylation of the cytoplasmic domain to the bovine cation-independent mannose 6-phosphate receptor Serines 2421 and 2492 are the targets of a casein kinase II associated to the Golgi-derived HAI adaptor complex. J. Biol. Chem, 265, 18833-18842 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 18833-18842
    • Meresse, S.1    Ludwig, T.2    Frank, R.3    Hoflack, B.4
  • 11
    • 0027296553 scopus 로고
    • Characterization of phosphorylation sites in the cytoplasmic domain of the 300 kDa mannose 6-phosphate receptor
    • Rosorius, O. et al. Characterization of phosphorylation sites in the cytoplasmic domain of the 300 kDa mannose 6-phosphate receptor. Biochem. J. 292, 833-838 (1993).
    • (1993) Biochem. J. , vol.292 , pp. 833-838
    • Rosorius, O.1
  • 12
    • 0029670903 scopus 로고    scopus 로고
    • Cysteine 34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting
    • Schweizer, A., Kornfeld, S. & Rohrer, J. Cysteine 34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting. J. Cell Biol. 132, 577-584 (1996).
    • (1996) J. Cell Biol. , vol.132 , pp. 577-584
    • Schweizer, A.1    Kornfeld, S.2    Rohrer, J.3
  • 13
    • 0033534489 scopus 로고    scopus 로고
    • The rate of internalization of the mannose 6-phosphate/insulin-like growth factor II receptor is enhanced by multivalent ligand binding
    • York, S. J., Arneson, L. S., Gregory, W T., Dahms, N. M. & Kornfeld, S. The rate of internalization of the mannose 6-phosphate/insulin-like growth factor II receptor is enhanced by multivalent ligand binding. J. Biol. Chem. 274, 1164-1171 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 1164-1171
    • York, S.J.1    Arneson, L.S.2    Gregory, W.T.3    Dahms, N.M.4    Kornfeld, S.5
  • 14
    • 0034705488 scopus 로고    scopus 로고
    • Mechanisms for high affinity mannose 6-phosphate ligand binding to the insulin-like growth factor II/mannose 6-phosphate receptor. Negative cooperativity and receptor oligomerization
    • Byrd, J. C. & MacDonald, R. G. Mechanisms for high affinity mannose 6-phosphate ligand binding to the insulin-like growth factor II/mannose 6-phosphate receptor. Negative cooperativity and receptor oligomerization. J. Biol. Chem. 275, 18638-18646 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 18638-18646
    • Byrd, J.C.1    MacDonald, R.G.2
  • 15
    • 0034705596 scopus 로고    scopus 로고
    • Dimerization of the insulin-like growth factor II/mannose 6-phosphate receptor
    • Byrd, J. C. Park, J. H., Schaffer, B. S., Garmroudi, F. & MacDonald, R. G. Dimerization of the insulin-like growth factor II/mannose 6-phosphate receptor. J. Biol. Chem. 275, 18647-18656 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 18647-18656
    • Byrd, J.C.1    Park, J.H.2    Schaffer, B.S.3    Garmroudi, F.4    MacDonald, R.G.5
  • 16
    • 0032524316 scopus 로고    scopus 로고
    • Molecular basis of lysosomal enzyme recognition: Three-dimensional structure of the cation-dependent mannose 6-phosphate receptor
    • Roberts, D. L., Weix, D. J., Dahms, N. M. & Kim, J.-J. P. Molecular basis of lysosomal enzyme recognition: three-dimensional structure of the cation-dependent mannose 6-phosphate receptor. Cell 93, 639-648 (1998).
    • (1998) Cell , vol.93 , pp. 639-648
    • Roberts, D.L.1    Weix, D.J.2    Dahms, N.M.3    Kim, J.-J.P.4
  • 17
    • 0033569876 scopus 로고    scopus 로고
    • Structural basis for recognition of phosphorylated high mannose oligosaccharides by the cation-dependent mannose 6-phosphate receptor
    • Olson, L. J., Zhang, J., Lee, Y. C., Dahms, N. M. & Kim, J.-J. P. Structural basis for recognition of phosphorylated high mannose oligosaccharides by the cation-dependent mannose 6-phosphate receptor. J. Biol. Chem. 274, 29889-29896 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 29889-29896
    • Olson, L.J.1    Zhang, J.2    Lee, Y.C.3    Dahms, N.M.4    Kim, J.-J.P.5
  • 18
    • 0037155883 scopus 로고    scopus 로고
    • Twists and turns of the CD-MPR: Ligand-bound versus ligand-free receptor
    • Olson, L. J., Zhang, J., Dahms, N. M. & Kim, J.-J. P. Twists and turns of the CD-MPR: ligand-bound versus ligand-free receptor. J. Biol. Chem. 277, 10156-10161 (2002). References 16-18 provide useful insights into the structural basis for M6P-containing ligand recognition by the CD-MPR.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10156-10161
    • Olson, L.J.1    Zhang, J.2    Dahms, N.M.3    Kim, J.-J.P.4
  • 19
    • 0036499988 scopus 로고    scopus 로고
    • Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur
    • Brown, J. et al. Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur. EMBO J. 21, 1054-1062 (2002). This work presents a high-resolution crystal structure of the eleventh domain of the Cl-MPR that functions as the IGF-II-binding domain.
    • (2002) EMBO J. , vol.21 , pp. 1054-1062
    • Brown, J.1
  • 20
    • 0035898613 scopus 로고    scopus 로고
    • The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5
    • Zeslawski, W. et al. The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5. EMBO J. 20, 3638-3644 (2001).
    • (2001) EMBO J. , vol.20 , pp. 3638-3644
    • Zeslawski, W.1
  • 21
    • 0031724560 scopus 로고    scopus 로고
    • An insulin-like growth factor II (IGF-II) affinity-enhancing domain localized within extracytoplasmic repeat 13 of the IGF-II/mannose 6-phosphate receptor
    • Devi, G. R., Byrd, J. C., Slentz, D. H. & MacDonald, R. G. An insulin-like growth factor II (IGF-II) affinity-enhancing domain localized within extracytoplasmic repeat 13 of the IGF-II/mannose 6-phosphate receptor. Mol. Endocrinol. 12, 1661-1672 (1998).
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1661-1672
    • Devi, G.R.1    Byrd, J.C.2    Slentz, D.H.3    MacDonald, R.G.4
  • 22
    • 0035968216 scopus 로고    scopus 로고
    • Real time kinetics of insulin-like growth factor II (IGF-II) interaction with the IGF-II/mannose 6-phosphate receptor: The effects of domain 13 and pH
    • Linnell, J., Groeger, G. & Hassan, A. B. Real time kinetics of insulin-like growth factor II (IGF-II) interaction with the IGF-II/mannose 6-phosphate receptor: the effects of domain 13 and pH. J. Biol. Chem. 276, 23986-23991 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 23986-23991
    • Linnell, J.1    Groeger, G.2    Hassan, A.B.3
  • 23
    • 0035166947 scopus 로고    scopus 로고
    • Lysosomal hydrolase mannose 6-phosphate uncovering enzyme resides in the trans-Golgi network
    • Rohrer, J. & Kornfeld, R. Lysosomal hydrolase mannose 6-phosphate uncovering enzyme resides in the trans-Golgi network. Mol. Biol. Cell 12, 1623-1631 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1623-1631
    • Rohrer, J.1    Kornfeld, R.2
  • 24
    • 0027210570 scopus 로고
    • Differences in the endosomal distributions of the two mannose 6-phosphate receptors
    • Klumperman, J. et al. Differences in the endosomal distributions of the two mannose 6-phosphate receptors. J. Cell Biol. 121, 997-1010 (1993). This report established that the two receptors exit the trans-Golgi network through AP1-positive clathrincoated buds and vesicles.
    • (1993) J. Cell Biol. , vol.121 , pp. 997-1010
    • Klumperman, J.1
  • 25
    • 0021100238 scopus 로고
    • Coated vesicles from rat liver and calf brain contain lysosomal enzymes bound to mannose 6-phosphate receptors
    • Campbell, C. H. & Rome, L. H. Coated vesicles from rat liver and calf brain contain lysosomal enzymes bound to mannose 6-phosphate receptors. J. Biol. Chem. 258, 13347-13352 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 13347-13352
    • Campbell, C.H.1    Rome, L.H.2
  • 26
    • 0022252019 scopus 로고
    • Cathepsin D precursors in clathrin-coated organelles from human fibroblasts
    • Schulze-Lohoff, E., Hasilik, A. & von Figura, K. Cathepsin D precursors in clathrin-coated organelles from human fibroblasts. J. Cell Biol. 101, 824-829 (1985). References 25 and 26 showed that clathrin-coated vesicles function as transport carriers for lysosomal enzymes en route from the Golgi to the endosomal-lysosomal compartments.
    • (1985) J. Cell Biol. , vol.101 , pp. 824-829
    • Schulze-Lohoff, E.1    Hasilik, A.2    Von Figura, K.3
  • 27
    • 0026757062 scopus 로고
    • The cytoplasmic tail of the mannose 6-phosphate/insulin-like growth factor-II receptor has two signals for lysosomal enzyme sorting in the Golgi
    • Johnson, K. F. & Kornfeld, S. The cytoplasmic tail of the mannose 6-phosphate/insulin-like growth factor-II receptor has two signals for lysosomal enzyme sorting in the Golgi. J. Cell Biol. 119, 249-257 (1992).
    • (1992) J. Cell Biol. , vol.119 , pp. 249-257
    • Johnson, K.F.1    Kornfeld, S.2
  • 28
    • 0026806542 scopus 로고
    • A His-Leu-Leu sequence near the carboxyl terminus of the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor is necessary for the lysosomal enzyme sorting function
    • Johnson, K. F. & Kornfeld, S. A His-Leu-Leu sequence near the carboxyl terminus of the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor is necessary for the lysosomal enzyme sorting function. J. Biol. Chem. 267, 17110-17115 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 17110-17115
    • Johnson, K.F.1    Kornfeld, S.2
  • 29
    • 0027431848 scopus 로고
    • Mutational analysis of the cation-independent mannose 6-phosphate/insulin-like growth factor II receptor. A consensus casein kinase II site followed by 2 leucines near the carboxyl terminus is important for intracellular targeting of lysosomal enzymes
    • Chen, H. J., Remmler, J., Delaney, J. C., Messner, D. J. & Lobel, P. Mutational analysis of the cation-independent mannose 6-phosphate/insulin-like growth factor II receptor. A consensus casein kinase II site followed by 2 leucines near the carboxyl terminus is important for intracellular targeting of lysosomal enzymes. J. Biol. Chem. 268, 22338-22346 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 22338-22346
    • Chen, H.J.1    Remmler, J.2    Delaney, J.C.3    Messner, D.J.4    Lobel, P.5
  • 30
    • 0000864308 scopus 로고    scopus 로고
    • Systematic mutational analysis of the cation-independent mannose 6-phosphate/insulin-like growth factor II receptor cytoplasmic domain. An acidic cluster containing a key aspartate is important for function in lysosomal enzyme sorting
    • Chan, H. J., Yuan, J. & Lobel, P. Systematic mutational analysis of the cation-independent mannose 6-phosphate/insulin-like growth factor II receptor cytoplasmic domain. An acidic cluster containing a key aspartate is important for function in lysosomal enzyme sorting. J. Biol. Chem. 272, 7003-7012 (1997). References 27-30 establish the role of the AC-LL signal in trafficking of the mannose 6-phosphate receptors from the trans-Golgi network to endosomes.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7003-7012
    • Chan, H.J.1    Yuan, J.2    Lobel, P.3
  • 31
    • 0030022935 scopus 로고    scopus 로고
    • A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes
    • Mauxion, F., Le Borgne, R., Munier-Lehmann, H. & Hoflack, B. A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes. J. Biol. Chem. 271, 2171-2178 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 2171-2178
    • Mauxion, F.1    Le Borgne, R.2    Munier-Lehmann, H.3    Hoflack, B.4
  • 32
    • 0039109677 scopus 로고    scopus 로고
    • The 46-kDa mannose 6-phosphate receptor contains multiple binding sites for clathrin adaptors
    • Honing S., Sosa, M., Hille-Rehfeld, A. & von Figura, K. The 46-kDa mannose 6-phosphate receptor contains multiple binding sites for clathrin adaptors. J. Biol. Chem. 272, 19884-19890 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 19884-19890
    • Honing, S.1    Sosa, M.2    Hille-Rehfeld, A.3    Von Figura, K.4
  • 33
    • 0034629469 scopus 로고    scopus 로고
    • Vear, a novel Golgi-associated protein with VHS and γ-adaptin 'ear' domains
    • Poussu A., Lohi, O. & Lehto, V. P. Vear, a novel Golgi-associated protein with VHS and γ-adaptin 'ear' domains. J. Biol. Chem. 275, 7176-7183 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 7176-7183
    • Poussu, A.1    Lohi, O.2    Lehto, V.P.3
  • 34
    • 0034599537 scopus 로고    scopus 로고
    • A family of proteins with γ-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome
    • Hirst, J. et al. A family of proteins with γ-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome. J. Cell Biol. 149, 67-80 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 67-80
    • Hirst, J.1
  • 35
    • 0034599528 scopus 로고    scopus 로고
    • GGAs: A family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex
    • Dell'Angelica, E. C. et al. GGAs: A family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex. J. Cell Biol. 149, 81-94 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 81-94
    • Dell'Angelica, E.C.1
  • 36
    • 0034036097 scopus 로고    scopus 로고
    • A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi
    • Boman, A. L., Zhang, C., Zhu, X. & Kahn, R. A. A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi. Mol. Biol. Cell 11, 1241-1255 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1241-1255
    • Boman, A.L.1    Zhang, C.2    Zhu, X.3    Kahn, R.A.4
  • 37
    • 0034685644 scopus 로고    scopus 로고
    • Adaptor γ ear homology domain conserved in γ-adaptin and GGA proteins that interact with γ-synergin
    • Takatsu, H., Yoshino, K. & Nakayama, K. Adaptor γ ear homology domain conserved in γ-adaptin and GGA proteins that interact with γ-synergin. Biochem. Biophys. Res. Commun. 271, 719-725 (2000). References 33-37 cite the five groups that simultaneously and independently discovered the GGA family of adaptors.
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 719-725
    • Takatsu, H.1    Yoshino, K.2    Nakayama, K.3
  • 39
    • 0035369692 scopus 로고    scopus 로고
    • Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor
    • Zhu, Y., Doray, B., Poussu, A., Lehto, V. P. & Kornfeld, S. Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor. Science 292, 1716-1718 (2001).
    • (2001) Science , vol.292 , pp. 1716-1718
    • Zhu, Y.1    Doray, B.2    Poussu, A.3    Lehto, V.P.4    Kornfeld, S.5
  • 40
    • 0035958856 scopus 로고    scopus 로고
    • Golgi-localizing, γ-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) protains interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains
    • Takatsu, H., Katoh, Y., Shiba, Y. & Nakayama, K. Golgi-localizing, γ-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) protains interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. J. Biol. Chem. 276, 28541-28545 (2001). References 38-40 implicated the GGAs in sorting of mannose 6-phosphate receptors at the trans-Golgi network.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28541-28545
    • Takatsu, H.1    Katoh, Y.2    Shiba, Y.3    Nakayama, K.4
  • 41
    • 0037148787 scopus 로고    scopus 로고
    • Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains
    • Misra, S., Puertollano, R. Kato, Y., Bonifacino, J. S. & Hurley, J. H. Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains. Nature 415, 933-937 (2002).
    • (2002) Nature , vol.415 , pp. 933-937
    • Misra, S.1    Puertollano, R.2    Kato, Y.3    Bonifacino, J.S.4    Hurley, J.H.5
  • 42
    • 18244400470 scopus 로고    scopus 로고
    • Structural basis for recognition of acidic-cluster dileucine sequence by GGA1
    • Shiba, T. et al. Structural basis for recognition of acidic-cluster dileucine sequence by GGA1. Nature 415, 937-941 (2002). References 41 and 42 demonstrate the structural basis for the recognition of the AC-LL signal in the cytoplasmic tail of the MPR by the VHS domain of the GGA protein.
    • (2002) Nature , vol.415 , pp. 937-941
    • Shiba, T.1
  • 43
    • 0037196416 scopus 로고    scopus 로고
    • The sorLA cytoplasmic domain interacts with GGA1 and - 2 and defines minimum requirements for GGA binding
    • Jacobsen, L. et al. The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding. FEBS Lett. 511, 155-158 (2002).
    • (2002) FEBS Lett. , vol.511 , pp. 155-158
    • Jacobsen, L.1
  • 44
    • 0037166331 scopus 로고    scopus 로고
    • Interaction of the cation-dependant mannose 6-phosphate receptor with GGA proteins
    • Doray, B., Bruns, K., Ghosh, P. & Kornfeld, S. Interaction of the cation-dependant mannose 6-phosphate receptor with GGA proteins. J. Biol. Chem. 277, 18477-18482 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 18477-18482
    • Doray, B.1    Bruns, K.2    Ghosh, P.3    Kornfeld, S.4
  • 46
    • 0030792177 scopus 로고    scopus 로고
    • Interaction of turin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation
    • Dittie, A S., Thomas, L., Thomas, G. & Tooze, S. A. Interaction of turin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation. EMBO J. 16, 4859-4870 (1997).
    • (1997) EMBO J. , vol.16 , pp. 4859-4870
    • Dittie, A.S.1    Thomas, L.2    Thomas, G.3    Tooze, S.A.4
  • 47
    • 0027371853 scopus 로고
    • Binding of AP-1 Golgi adaptors to membranes requires phosphorylated cytoplasmic domains of the mannose 6-phosphate/insulin-like growth factor II receptor
    • Le Borgne, R., Schmidt, A., Mauxion, F., Griffiths, G. & Hoflack, B. Binding of AP-1 Golgi adaptors to membranes requires phosphorylated cytoplasmic domains of the mannose 6-phosphate/insulin-like growth factor II receptor J. Biol. Chem. 268, 22552-22556 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 22552-22556
    • Le Borgne, R.1    Schmidt, A.2    Mauxion, F.3    Griffiths, G.4    Hoflack, B.5
  • 48
    • 0032476017 scopus 로고    scopus 로고
    • The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals
    • Ohno, H. et al. The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals. J. Biol. Chem. 273, 25915-25921 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 25915-25921
    • Ohno, H.1
  • 49
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytic signals
    • Owen, D. J. & Evans, P. R. A structural explanation for the recognition of tyrosine-based endocytic signals. Science. 282, 1327-1332 (1998).
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 50
    • 0032502661 scopus 로고    scopus 로고
    • A region from the medium chain adaptor subunit (μ) recognizes leucine- and tyrosine-based sorting signals
    • Bremnes, T., Lauvrak, V., Lindqvist, B. & Bakke, O. A region from the medium chain adaptor subunit (μ) recognizes leucine- and tyrosine-based sorting signals. J. Biol. Chem. 273, 8638-8645 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 8638-8645
    • Bremnes, T.1    Lauvrak, V.2    Lindqvist, B.3    Bakke, O.4
  • 51
    • 0032522517 scopus 로고    scopus 로고
    • Dileucine-based sorting signals bind to the β chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site
    • Rapoport, I., Chen, Y. C., Cupers, P., Shoelson, S. E. & Kirchhausen, T. Dileucine-based sorting signals bind to the β chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site. EMBO J. 17, 2148-2155 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2148-2155
    • Rapoport, I.1    Chen, Y.C.2    Cupers, P.3    Shoelson, S.E.4    Kirchhausen, T.5
  • 52
    • 0034735540 scopus 로고    scopus 로고
    • A selective transport route from Golgi to late endosomes that requires the yeast GGA proteins
    • Black, M. W. & Pelham, H. R. A selective transport route from Golgi to late endosomes that requires the yeast GGA proteins. J. Cell Biol. 151, 587-600 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 587-600
    • Black, M.W.1    Pelham, H.R.2
  • 53
    • 0035166326 scopus 로고    scopus 로고
    • Yeast GGA coat proteins function with clathrin in Golgi to endosome transport
    • Costaguta, G. Stefan, C. J., Bensen, E. S., Emr, S. D. & Payne, G. S. Yeast GGA coat proteins function with clathrin in Golgi to endosome transport. Mol. Biol. Cell 12, 1885-1896 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1885-1896
    • Costaguta, G.1    Stefan, C.J.2    Bensen, E.S.3    Emr, S.D.4    Payne, G.S.5
  • 54
    • 0035192658 scopus 로고    scopus 로고
    • GGAs: Roles of the different domains and comparison with AP-1 and clathrin
    • Hirst, J., Lindsay, M. R. & Robinson, M. S. GGAs: Roles of the different domains and comparison with AP-1 and clathrin. Mol. Biol. Cell 12, 3573-3588 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3573-3588
    • Hirst, J.1    Lindsay, M.R.2    Robinson, M.S.3
  • 55
    • 0033594080 scopus 로고    scopus 로고
    • Golgi structure in three dimensions: Functional insights from the normal rat kidney cell
    • Ladinsky, M. S., Maatronarde, D. N., MaIntosh, J. R., Howell, K. E. & Staehelin, L. A. Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J. Cell Biol. 144, 1135-1149 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 1135-1149
    • Ladinsky, M.S.1    Maatronarde, D.N.2    MaIntosh, J.R.3    Howell, K.E.4    Staehelin, L.A.5
  • 56
    • 0035956989 scopus 로고    scopus 로고
    • Organellar relationships in the Golgi region of the pancreatic β-cell line, HIT-T15, visualized by high resolution electron tomography
    • Marsh, B. J., Mastronarde, D. N., Buttle, K. F., Howell, K. E. & McIntosh, J. R. Organellar relationships in the Golgi region of the pancreatic β-cell line, HIT-T15, visualized by high resolution electron tomography. Proc. Natl Acad. Sci. USA 98, 2399-2406 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2399-2406
    • Marsh, B.J.1    Mastronarde, D.N.2    Buttle, K.F.3    Howell, K.E.4    McIntosh, J.R.5
  • 57
    • 0037031658 scopus 로고    scopus 로고
    • Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network
    • Doray, B., Ghosh, P., Griffith, J., Geuze, H. & Kornfeld, S. Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network. Science, 297, 1700-1703 (2002). This work showed that GGAs and AP1 colocalize within clathrin-coated buds and vesicles at the trans-Golgi network (TGN) of mammalian cells, which indicates a cooperative model for AP1 and GGAs in trafficking of MPRs from the TGN to endosomes, as opposed to the independent pathways proposed in yeast.
    • (2002) Science , vol.297 , pp. 1700-1703
    • Doray, B.1    Ghosh, P.2    Griffith, J.3    Geuze, H.4    Kornfeld, S.5
  • 58
    • 0037062410 scopus 로고    scopus 로고
    • Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif
    • Doray, B., Bruns, K., Ghosh, P. & Kornfeld, S. A. Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif. Proc. Natl. Acad. Sci. USA 99, 8072-8077 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8072-8077
    • Doray, B.1    Bruns, K.2    Ghosh, P.3    Kornfeld, S.A.4
  • 59
    • 0035021147 scopus 로고    scopus 로고
    • Trafficking of yellow-fluorescent-protein-tagged μ1 subunit of clathrin adaptor AP-1 complex in living cells
    • Huang, F., Nesterov, A., Carter, R. E. & Sorkin, A. Trafficking of yellow-fluorescent-protein-tagged μ1 subunit of clathrin adaptor AP-1 complex in living cells. Traffic 2, 345-357 (2001). The first evidence of AP1 in anterograde trafficking of MPRs using live-cell imaging techniques.
    • (2001) Traffic , vol.2 , pp. 345-357
    • Huang, F.1    Nesterov, A.2    Carter, R.E.3    Sorkin, A.4
  • 60
    • 0037240484 scopus 로고    scopus 로고
    • Visualization of TGN to endosomes trafficking through fluorescently labeled MPR and AP-1 in living cells
    • Waguri, S. et al. Visualization of TGN to endosomes trafficking through fluorescently labeled MPR and AP-1 in living cells. Mol. Biol. Cell 14, 142-155 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 142-155
    • Waguri, S.1
  • 61
    • 0030991809 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors regulate the formation of clathrin-coated vesicles in the TGN
    • Le Borgne, R. & Hoflack, B. Mannose 6-phosphate receptors regulate the formation of clathrin-coated vesicles in the TGN. J. Cell Biol. 137, 336-345 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 336-345
    • Le Borgne, R.1    Hoflack, B.2
  • 62
    • 0034118754 scopus 로고    scopus 로고
    • Identification of the universal cofactor (auxilin 2) in clathrin coat dissociation
    • Umeda, A., Meyerholz, A. & Ungewickell, E. Identification of the universal cofactor (auxilin 2) in clathrin coat dissociation. Eur. J. Cell Biol. 79, 336-342 (2000).
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 336-342
    • Umeda, A.1    Meyerholz, A.2    Ungewickell, E.3
  • 63
    • 0033978513 scopus 로고    scopus 로고
    • Role of cyclin G-associated kinase in uncoating clathrin-coated vesicles from non-neuronal cells
    • Greener, T., Zhao, X., Nojima, H., Eisenberg, E. & Greene, L. E. Role of cyclin G-associated kinase in uncoating clathrin-coated vesicles from non-neuronal cells. J. Biol. Chem. 275, 1365-1370 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 1365-1370
    • Greener, T.1    Zhao, X.2    Nojima, H.3    Eisenberg, E.4    Greene, L.E.5
  • 64
    • 0031859055 scopus 로고    scopus 로고
    • ATP- and cytosol-dependent release of adaptor proteins from clathrin-coated vesicles: A dual role for Hsc70
    • Hannan, L. A., Newmyer, S. L. & Schmid, S. L. ATP- and cytosol-dependent release of adaptor proteins from clathrin-coated vesicles: a dual role for Hsc70. Miol. Biol. Cell 9, 2217-2229 (1998).
    • (1998) Miol. Biol. Cell , vol.9 , pp. 2217-2229
    • Hannan, L.A.1    Newmyer, S.L.2    Schmid, S.L.3
  • 65
    • 0033697037 scopus 로고    scopus 로고
    • A novel motor, KIF13A, transports mannose 6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex
    • Nakagawa, T. et al. A novel motor, KIF13A. transports mannose 6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex. Cell 103, 569-581 (2000).
    • (2000) Cell , vol.103 , pp. 569-581
    • Nakagawa, T.1
  • 66
    • 0026318365 scopus 로고
    • Distribution of newly synthesized lysosomal enzymes in the endocytic pathway of normal rat kidney cells
    • Ludwig, T., Griffiths, G. & Hoflack, B. Distribution of newly synthesized lysosomal enzymes in the endocytic pathway of normal rat kidney cells. J. Cell Biol. 115, 1561-1572 (1991).
    • (1991) J. Cell Biol. , vol.115 , pp. 1561-1572
    • Ludwig, T.1    Griffiths, G.2    Hoflack, B.3
  • 67
    • 0032498795 scopus 로고    scopus 로고
    • Mutant rab7 causes the accumulation of cathepsin D and cation-independent mannose 6-phosphate receptor in an early endocytic compartment
    • Press, B., Feng, Y., Hoflack, B. & Wandingernese, A. Mutant rab7 causes the accumulation of cathepsin D and cation-independent mannose 6-phosphate receptor in an early endocytic compartment. J. Cell Biol. 140, 1075-1089 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 1075-1089
    • Press, B.1    Feng, Y.2    Hoflack, B.3    Wandingernese, A.4
  • 69
    • 0036221890 scopus 로고    scopus 로고
    • γ-adaptin interacts directly with rabaptin-5 through its ear domain
    • Shiba, Y., Takatsu, H., Shin, H. W. & Nakayama, K. γ-adaptin interacts directly with rabaptin-5 through its ear domain. J. Biochem. 131, 327-336 (2002).
    • (2002) J. Biochem. , vol.131 , pp. 327-336
    • Shiba, Y.1    Takatsu, H.2    Shin, H.W.3    Nakayama, K.4
  • 70
    • 0028791634 scopus 로고
    • Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion
    • Stenmark, H., Vitale, G., Ullrich, O. & Zerial, M. Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. Cell 83, 423-432 (1995).
    • (1995) Cell , vol.83 , pp. 423-432
    • Stenmark, H.1    Vitale, G.2    Ullrich, O.3    Zerial, M.4
  • 71
    • 0030797279 scopus 로고    scopus 로고
    • Syntaxin 6 functions in trans-Golgi network vesicle trafficking
    • Buck, J. B., Klumperman, J., Davangar, S. & Scheller, R. H. Syntaxin 6 functions in trans-Golgi network vesicle trafficking. Mol. Biol. Cell 8, 1261-1271 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1261-1271
    • Buck, J.B.1    Klumperman, J.2    Davangar, S.3    Scheller, R.H.4
  • 72
    • 0032538835 scopus 로고    scopus 로고
    • Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes
    • Prekeris, R., Klumperman, O., Chen, Y. A. & Scheller, R. H. Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes. J. Cell Biol. 143, 957-971 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 957-971
    • Prekeris, R.1    Klumperman, O.2    Chen, Y.A.3    Scheller, R.H.4
  • 73
    • 0032978225 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking
    • Steegmaier, M., Klumperman, J., Foletti, D. L., Yao, J. S. & Scheller, R. H. Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking. Mol. Biol. Cell 10, 1957-1972 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1957-1972
    • Steegmaier, M.1    Klumperman, J.2    Foletti, D.L.3    Yao, J.S.4    Scheller, R.H.5
  • 74
    • 0032550222 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors are sorted from immature secretory granules via adaptor protein AP-1, clathrin, and syntaxin 6-positive vesicles
    • Klumperman, J., Kuliawat, R., Griffith, J. M., Geuze, H. J. & Aryan, P. Mannose 6-phosphate receptors are sorted from immature secretory granules via adaptor protein AP-1, clathrin, and syntaxin 6-positive vesicles. J. Cell Biol. 141, 359-371 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 359-371
    • Klumperman, J.1    Kuliawat, R.2    Griffith, J.M.3    Geuze, H.J.4    Aryan, P.5
  • 75
    • 0035966098 scopus 로고    scopus 로고
    • The di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding
    • Peden, A. A., Park, G. Y. & Scheller, R. H. The di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding. J. Biol. Chem. 276, 49183-49187 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 49183-49187
    • Peden, A.A.1    Park, G.Y.2    Scheller, R.H.3
  • 76
    • 0032879685 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 interacts directly with syntaxin-6
    • Simonsen, A., Gauilier, J. M., D'Arrigo, A. & Stenmark, H. The Rab5 effector EEA1 interacts directly with syntaxin-6. J. Biol. Chem. 274, 28857-28860 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 28857-28860
    • Simonsen, A.1    Gauilier, J.M.2    D'Arrigo, A.3    Stenmark, H.4
  • 77
    • 0030298068 scopus 로고    scopus 로고
    • The biogenesis of lysosomes: Is it a kiss and run, continuous fusion and fission process?
    • Storrie, B. & Desjardins, M. The biogenesis of lysosomes: is it a kiss and run, continuous fusion and fission process? Bioessays 18, 895-903 (1996).
    • (1996) Bioessays , vol.18 , pp. 895-903
    • Storrie, B.1    Desjardins, M.2
  • 78
    • 0031446640 scopus 로고    scopus 로고
    • Proper sorting of the cation-dependent mannose 6-phosphate receptor in endosomes depends on a pair of aromatic amino acids in its cytoplasmic tail
    • Schweizer, A., Kornfeld, S. & Rohrer, J. Proper sorting of the cation-dependent mannose 6-phosphate receptor in endosomes depends on a pair of aromatic amino acids in its cytoplasmic tail. Proc. Natl Acad. Sci USA 94, 14471-14476 (1997). This work established the importance of a all-aromatic sequence on the cytoplasmic tail of the CD-MPR in preventing it from entering lysosomes.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14471-14476
    • Schweizer, A.1    Kornfeld, S.2    Rohrer, J.3
  • 79
    • 0032076636 scopus 로고    scopus 로고
    • TIP47: A cargo selection device for mannose 6-phosphate receptor trafficking
    • Diaz, E. & Pfeffer, S. R. TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking. Cell 93, 433-443 (1996).
    • (1996) Cell , vol.93 , pp. 433-443
    • Diaz, E.1    Pfeffer, S.R.2
  • 80
    • 0034255375 scopus 로고    scopus 로고
    • Recognition of the 300-kDa mannose 6-phosphate receptor cytoplasmic domain by 47-kDa tail-interacting protein
    • Orsel, J. G., Sincock, P. M., Krise, J. P. & Pfeffer, S. R. Recognition of the 300-kDa mannose 6-phosphate receptor cytoplasmic domain by 47-kDa tail-interacting protein. Proc. Natl Acad. Sci. USA 91, 9047-9051 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9047-9051
    • Orsel, J.G.1    Sincock, P.M.2    Krise, J.P.3    Pfeffer, S.R.4
  • 81
    • 0035906951 scopus 로고    scopus 로고
    • Role of Rab9 GTPase in facilitating receptor recruitment by TIP47
    • Carroll, K. S. et al. Role of Rab9 GTPase in facilitating receptor recruitment by TIP47. Science 292, 1373-1376 (2001).
    • (2001) Science , vol.292 , pp. 1373-1376
    • Carroll, K.S.1
  • 82
    • 0037017395 scopus 로고    scopus 로고
    • Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells
    • Barbero, P., Bittova, L. & Pfeffer, S. R. Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells J. Cell Biol. 156, 511-518 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 511-518
    • Barbero, P.1    Bittova, L.2    Pfeffer, S.R.3
  • 83
    • 0028224561 scopus 로고
    • Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network
    • Riederer, M. A., Soldati, T., Shapiro, A. D., Lin, J. & Pfeffer, S. R. Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network. J. Cell Biol. 125, 573-582 (1994). References 79-83 provide evidence that TIP47/Rab9 mediates sorting of the MPRs at the late endosome and has a role in retrograde trafficking to the Golgi.
    • (1994) J. Cell Biol. , vol.125 , pp. 573-582
    • Riederer, M.A.1    Soldati, T.2    Shapiro, A.D.3    Lin, J.4    Pfeffer, S.R.5
  • 84
    • 0034657033 scopus 로고    scopus 로고
    • μ1A-adaptin-deficient mice: Lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors
    • Meyer, C. et al. μ1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors. EMBO J. 19, 2193-2203 (2000).
    • (2000) EMBO J. , vol.19 , pp. 2193-2203
    • Meyer, C.1
  • 85
    • 0035691925 scopus 로고    scopus 로고
    • μ1A deficiency induces a profound increase in MPR300/IGF-II receptor internalization rate
    • Meyer, C., Eskelinen, E. L., Guruprasad, M. R., von Figura, K. & Schu, P. μ1A deficiency induces a profound increase in MPR300/IGF-II receptor internalization rate. J Cell Sci. 114, 4469-4476 (2001). References 84 and 85 were the first studies to implicate AP1 in retrograde trafficking of MPRs from endosomes to the trans-Golgi network.
    • (2001) J. Cell Sci. , vol.114 , pp. 4469-4476
    • Meyer, C.1    Eskelinen, E.L.2    Guruprasad, M.R.3    Von Figura, K.4    Schu, P.5
  • 86
    • 0032563306 scopus 로고    scopus 로고
    • PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization
    • Wan, L. et al. PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization. Cell 94, 205-216 (1998).
    • (1998) Cell , vol.94 , pp. 205-216
    • Wan, L.1
  • 87
    • 0035341464 scopus 로고    scopus 로고
    • PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic
    • Crump, C. M. et al. PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic. EMBO J. 20, 2191-2201 (2001). This reference cites the first evidence in support of PACS-1/AP1-mediated retrograde transport of MPRs from early endosomes to the trans-Golgi network.
    • (2001) EMBO J. , vol.20 , pp. 2191-2201
    • Crump, C.M.1
  • 88
    • 0034252326 scopus 로고    scopus 로고
    • The dileucine motif within the tail of the MPR 46 is required for sorting of the receptor in endosomes
    • Tikkanen, R. et al. The dileucine motif within the tail of the MPR46 is required for sorting of the receptor in endosomes Traffic 1, 631-640 (2000).
    • (2000) Traffic , vol.1 , pp. 631-640
    • Tikkanen, R.1
  • 89
    • 0037009046 scopus 로고    scopus 로고
    • Enthoprotin: A novel clathrin-associated protein identified through subcellular proteomics
    • Wasiak, S. et al. Enthoprotin: a novel clathrin-associated protein identified through subcellular proteomics. J. Cell Biol. 158, 855-862 (2002).
    • (2002) J. Cell Biol. , vol.158 , pp. 855-862
    • Wasiak, S.1
  • 90
    • 0026755982 scopus 로고
    • Characterization of the signal for rapid internalization of the bovine mannose 6-phosphate/insulin-like growth factor-II receptor
    • Jadot, M., Canfield, W. M., Gregory, W. & Kornfeld, S. Characterization of the signal for rapid internalization of the bovine mannose 6-phosphate/insulin-like growth factor-II receptor. J. Biol. Chem. 267, 11069-11077 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 11069-11077
    • Jadot, M.1    Canfield, W.M.2    Gregory, W.3    Kornfeld, S.4
  • 91
    • 0025600403 scopus 로고
    • Cation-dependent mannose 6-phosphate receptor contains two internalization signals in its cytoplasmic domain
    • Johnson, K. F., Chan, W. & Kornfeld, S. Cation-dependent mannose 6-phosphate receptor contains two internalization signals in its cytoplasmic domain. Proc. Natl Acad. Sci. USA 87, 10010-10014 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 10010-10014
    • Johnson, K.F.1    Chan, W.2    Kornfeld, S.3
  • 92
    • 0030875937 scopus 로고    scopus 로고
    • Identification of three internalization sequences in the pytoplasmic tail of the 46 kDa mannose 6-phosphate receptor
    • Denzer, K., Weber, B., Hille-Rehfeld, A., von Figura, K. & Pohlmann, R. Identification of three internalization sequences in the pytoplasmic tail of the 46 kDa mannose 6-phosphate receptor. Biochem. J. 326, 497-505 (1997).
    • (1997) Biochem. J. , vol.326 , pp. 497-505
    • Denzer, K.1    Weber, B.2    Hille-Rehfeld, A.3    Von Figura, K.4    Pohlmann, R.5
  • 93
    • 0035830849 scopus 로고    scopus 로고
    • Multiple C-terminal motifs of the 46-kDa mannose 6-phosphate receptor tail contribute to efficient binding of medium chains of AP-2 and AP-3
    • Storch, S. & Braulke, T. Multiple C-terminal motifs of the 46-kDa mannose 6-phosphate receptor tail contribute to efficient binding of medium chains of AP-2 and AP-3. J. Biol. Chem. 276, 4298-4303 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 4298-4303
    • Storch, S.1    Braulke, T.2
  • 94
    • 0030221121 scopus 로고    scopus 로고
    • Mouse mutants lacking the type 21GF receptor (IGF2R) are rescued from perinatal lethality in IGF2 and IGF1R null backgrounds
    • Ludwig, T. et al. Mouse mutants lacking the type 21GF receptor (IGF2R) are rescued from perinatal lethality in IGF2 and IGF1R null backgrounds. Dev. Biol. 177, 517-535 (1996).
    • (1996) Dev. Biol. , vol.177 , pp. 517-535
    • Ludwig, T.1
  • 95
    • 0027999284 scopus 로고
    • Regulation of embryonic growth and lysosomal targeting by the imprinted IGF2/MPR gene
    • Wang, Z. Q., Fung, M. R., Barlow, D. P. & Wagner, E. F. Regulation of embryonic growth and lysosomal targeting by the imprinted IGF2/MPR gene. Nature 372, 464-467 (1994).
    • (1994) Nature , vol.372 , pp. 464-467
    • Wang, Z.Q.1    Fung, M.R.2    Barlow, D.P.3    Wagner, E.F.4
  • 96
    • 0028575985 scopus 로고
    • Loss of the imprinted IGF2/cation-independent mannose 6-phosphate receptor results in fetal overgrowth and perinatal lethality
    • Lau, M. M. et al. Loss of the imprinted IGF2/cation- independent mannose 6-phosphate receptor results in fetal overgrowth and perinatal lethality. Genes Dev. 8, 2953-2963 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 2953-2963
    • Lau, M.M.1
  • 97
    • 0028788172 scopus 로고
    • In vivo coupling of insulin-like growth factor II/mannose 6-phosphate receptor to heteromeric G proteins. Distinct roles of cytoplasmic domains and signal sequestration by the receptor
    • Ikezu, T., Okamoto, T., Giambarella, U., Yokota, T. & Nishimoto, I. In vivo coupling of insulin-like growth factor II/mannose 6-phosphate receptor to heteromeric G proteins. Distinct roles of cytoplasmic domains and signal sequestration by the receptor. J. Biol. Chem. 270, 29224-29228 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 29224-29228
    • Ikezu, T.1    Okamoto, T.2    Giambarella, U.3    Yokota, T.4    Nishimoto, I.5
  • 98
    • 0030995501 scopus 로고    scopus 로고
    • Insulin-like growth factor II signaling through the insulin-like growth factor II/mannose 6-phosphate receptor promotes exocytosis in insulin-secreting cells
    • Zhang, Q. et al. Insulin-like growth factor II signaling through the insulin-like growth factor II/mannose 6-phosphate receptor promotes exocytosis in insulin-secreting cells. Proc. Natl Acad. Sci. USA 94, 6232-6237 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6232-6237
    • Zhang, Q.1
  • 99
    • 0034885755 scopus 로고    scopus 로고
    • Stimulation of human extravillous trophoblast migration by IGF-II is mediated by IGF type 2 receptor involving inhibitory G protein(s) and phosphorylation of MAPK
    • McKinnon, T., Chakraborty, C., Gleeson, L. M., Chidiac, P. & Lala, P. K. Stimulation of human extravillous trophoblast migration by IGF-II is mediated by IGF type 2 receptor involving inhibitory G protein(s) and phosphorylation of MAPK. J. Clin Endocrinol. Metab. 86, 3665-3674 (2001).
    • (2001) J. Clin Endocrinol. Metab. , vol.86 , pp. 3665-3674
    • McKinnon, T.1    Chakraborty, C.2    Gleeson, L.M.3    Chidiac, P.4    Lala, P.K.5
  • 100
    • 0030922133 scopus 로고    scopus 로고
    • Proliferin induces endothelial cell chemotaxis through a G protein-coupled, mitogen-activated protein kinase-dependent pathway
    • Groskopf, J. C., Syu, L. J. Saltiel, A. R. & Linzer, D. I. Proliferin induces endothelial cell chemotaxis through a G protein-coupled, mitogen-activated protein kinase-dependent pathway. Endocrinology 138, 2835-2840 (1997).
    • (1997) Endocrinology , vol.138 , pp. 2835-2840
    • Groskopf, J.C.1    Syu, L.J.2    Saltiel, A.R.3    Linzer, D.I.4
  • 101
    • 0026808908 scopus 로고
    • The insulin-like growth factor II (IGF-II)/mannose 6-phosphate receptor mediates IGF-II-induced motility in human rhabdomyo sarcoma cells
    • Minniti, C. P. et al. The insulin-like growth factor II (IGF-II)/mannose 6-phosphate receptor mediates IGF-II-induced motility in human rhabdomyo sarcoma cells. J. Biol. Chem. 267, 9000-9004 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 9000-9004
    • Minniti, C.P.1
  • 102
    • 0033797041 scopus 로고    scopus 로고
    • Insulin-like growth factor-II/cation-independent mannose 6-phosphate receptor mediates paracrine interactions during spermatogonial development
    • Tsuruta, J. K., Eddy, E. M. & O'Brien, D. A. Insulin-like growth factor-II/cation-independent mannose 6-phosphate receptor mediates paracrine interactions during spermatogonial development. Biol. Reprod. 63, 1006-1013 (2000).
    • (2000) Biol. Reprod. , vol.63 , pp. 1006-1013
    • Tsuruta, J.K.1    Eddy, E.M.2    O'Brien, D.A.3
  • 103
    • 0034682458 scopus 로고    scopus 로고
    • Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation
    • Ikushima, H. et al. Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation. Proc. Natl Acad. Sci. USA 97, 8439-8444 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8439-8444
    • Ikushima, H.1
  • 104
    • 0027182116 scopus 로고
    • The IGF-II receptor system: A G protein-linked mechanism
    • Nishimoto, I. The IGF-II receptor system: a G protein-linked mechanism. Mol. Reprod. Dev 35, 398-406 (1993).
    • (1993) Mol. Reprod. Dev. , vol.35 , pp. 398-406
    • Nishimoto, I.1
  • 105
    • 0032932822 scopus 로고    scopus 로고
    • Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells
    • Frasca, F. et al. Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells. Mol. Cell. Biol. 19, 3278-3288 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3278-3288
    • Frasca, F.1
  • 106
    • 0028861822 scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor II receptor fails to interact with G-proteins. Analysis of mutant cytoplasmic receptor domains
    • Korner, C., Nurnberg, B., Uhde, M. & Braulke, T. Mannose 6-phosphate/insulin-like growth factor II receptor fails to interact with G-proteins. Analysis of mutant cytoplasmic receptor domains. J. Biol. Chem. 270, 287-295 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 287-295
    • Korner, C.1    Nurnberg, B.2    Uhde, M.3    Braulke, T.4
  • 107
    • 0036346299 scopus 로고    scopus 로고
    • Soluble CD26/dipeptidyl paptidase IV enhances transendothelial migration via its interaction with mannose 6-phosphate/insulin-like growth factor II receptor
    • Ikushima, H. et al. Soluble CD26/dipeptidyl paptidase IV enhances transendothelial migration via its interaction with mannose 6-phosphate/insulin-like growth factor II receptor. Cell. Immunol. 215, 106-110 (2002).
    • (2002) Cell. Immunol. , vol.215 , pp. 106-110
    • Ikushima, H.1
  • 108
    • 0023710423 scopus 로고
    • Identification of mannose 6-phosphate in two asparagine-linked sugar chains of recombinant transforming growth factor-β1 precursor
    • Purchio, A. F. et al. Identification of mannose 6-phosphate in two asparagine-linked sugar chains of recombinant transforming growth factor-β1 precursor. J. Biol. Chem. 263, 14211-14215 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 14211-14215
    • Purchio, A.F.1
  • 109
    • 12344320716 scopus 로고    scopus 로고
    • Thrombospondin-1 is a major activator of TGF-β1 in vivo
    • Crawford, S. E. et al. Thrombospondin-1 is a major activator of TGF-β1 in vivo. Cell 93, 1159-1170 (1998).
    • (1998) Cell , vol.93 , pp. 1159-1170
    • Crawford, S.E.1
  • 110
    • 0026059613 scopus 로고
    • Cellular activation of latent transforming growth factor β requires binding to the cation-independent mannose 6-phosphate/insulin-like growth factor type II receptor
    • Dennis, P. A. & Rifkin, D. B. Cellular activation of latent transforming growth factor β requires binding to the cation-independent mannose 6-phosphate/insulin-like growth factor type II receptor Proc. Natl Acad. Sci. USA 88, 580-584 (1991). This work showed for the first time that the Cl-MPR plays a significant role in activation of the latent form of TGF-β1.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 580-584
    • Dennis, P.A.1    Rifkin, D.B.2
  • 111
    • 0028984569 scopus 로고
    • Characterization of latent TGF-β activation by murine peritoneal macrophages
    • Nunes, I., Shapiro, R. L. & Rifkin, D. B. Characterization of latent TGF-β activation by murine peritoneal macrophages. J. Immunol. 155, 1450-1459 (1995).
    • (1995) J. Immunol. , vol.155 , pp. 1450-1459
    • Nunes, I.1    Shapiro, R.L.2    Rifkin, D.B.3
  • 112
    • 0344026339 scopus 로고    scopus 로고
    • M6P/IGFII-receptor complexes urokinase receptor and plasminogec for activation of transforming growth factor-β 1
    • Godar, S. et al. M6P/IGFII-receptor complexes urokinase receptor and plasminogec for activation of transforming growth factor-β1. Eur. J. Immunol. 29, 1004-1013 (1999).
    • (1999) Eur. J. Immunol. , vol.29 , pp. 1004-1013
    • Godar, S.1
  • 113
    • 0033008016 scopus 로고    scopus 로고
    • Insulin-like growth factor-II/mannose 6 phosphate receptors lacilitate the matrix effects of latent transforming growth factor-β1 released from genetically modified keratinocytes in a fibroblast/keretinocyte co-culture system
    • Ghahary, A. Tredget, E. E. & Shen, Q. Insulin-like growth factor-II/mannose 6 phosphate receptors lacilitate the matrix effects of latent transforming growth factor-β1 released from genetically modified keratinocytes in a fibroblast/keretinocyte co-culture system. J. Cell Physiol. 180, 61-70 (1999).
    • (1999) J. Cell Physiol. , vol.180 , pp. 61-70
    • Ghahary, A.1    Tredget, E.E.2    Shen, Q.3
  • 115
    • 0037174862 scopus 로고    scopus 로고
    • The N-terminus of mannose 6-phosphate/insulin-like growth factor 2 receptor in regulation of fibrinolysis and cell migration
    • Leksa, V. et al. The N-terminus of mannose 6-phosphate/insulin-like growth factor 2 receptor in regulation of fibrinolysis and cell migration. J. Biol. Chem. 277, 40575-40582 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 40575-40582
    • Leksa, V.1
  • 116
    • 15144361572 scopus 로고    scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor-II receptor targets the urokinase receptor to lysosomes via a novel binding interaction
    • Nykjaer, A. et al. Mannose 6-phosphate/insulin-like growth factor-II receptor targets the urokinase receptor to lysosomes via a novel binding interaction. J. Cell Biol. 141, 815-828 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 815-828
    • Nykjaer, A.1
  • 117
    • 0032766413 scopus 로고    scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor II receptor mediates the growth-inhibitory effects of retinoids
    • Kang, J. X., Bell, J., Beard, R. L. & Chandraratna, R. A. Mannose 6-phosphate/insulin-like growth factor II receptor mediates the growth-inhibitory effects of retinoids. Cell Growth Differ. 10, 591-600 (1999).
    • (1999) Cell Growth Differ. , vol.10 , pp. 591-600
    • Kang, J.X.1    Bell, J.2    Beard, R.L.3    Chandraratna, R.A.4
  • 118
    • 0032582668 scopus 로고    scopus 로고
    • The soluble type 2 insulin-like growth factor (IGF-II) receptor reduces organ size by IGF-II-mediated and IGF-II-indapendent mechanisms
    • Zaina, S. & Squire, S. The soluble type 2 insulin-like growth factor (IGF-II) receptor reduces organ size by IGF-II- mediated and IGF-II-indapendent mechanisms. J. Biol. Chem. 273, 28610-28616 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 28610-28616
    • Zaina, S.1    Squire, S.2
  • 119
    • 0036827629 scopus 로고    scopus 로고
    • Insulin-like growth factor-II/mannose 6-phosphate receptor overexpression reduces growth of choriocarcinoma cells in vitro and in vivo
    • O'Gorman, D. B., Weiss, J., Hettiarstchi, A., Firth, S. M. & Scott, C. D. Insulin-like growth factor-II/mannose 6-phosphate receptor overexpression reduces growth of choriocarcinoma cells in vitro and in vivo. Endocrinology 143, 4287-4294 (2002).
    • (2002) Endocrinology , vol.143 , pp. 4287-4294
    • O'Gorman, D.B.1    Weiss, J.2    Hettiarstchi, A.3    Firth, S.M.4    Scott, C.D.5
  • 120
    • 0028804071 scopus 로고
    • M6P/IGF2R gene is mutated in human hepatocellular carcinomas with loss of heterozygosity
    • DeSouza, A. T., Hankins, G. R., Washington, M. K., Orton, T. C. & Jirtle, R. L. M6P/IGF2R gene is mutated in human hepatocellular carcinomas with loss of heterozygosity. Nature Genet. 11, 447-449 (1995). The first evidence that Cl-MPR is mutated in human cancers.
    • (1995) Nature Genet. , vol.11 , pp. 447-449
    • DeSouza, A.T.1    Hankins, G.R.2    Washington, M.K.3    Orton, T.C.4    Jirtle, R.L.5
  • 121
    • 0030928653 scopus 로고    scopus 로고
    • Loss of the gene encoding manoose 6-phosphate/insulin-like growth factor II receptor is an early event in liver carcinogenesis
    • Yamada, T., DeSouza, A. T., Finkelstein, S. & Jirtle, R. L. Loss of the gene encoding manoose 6-phosphate/insulin-like growth factor II receptor is an early event in liver carcinogenesis. Proc. Natl Acad. Sci. USA 94, 10351-10355 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10351-10355
    • Yamada, T.1    DeSouza, A.T.2    Finkelstein, S.3    Jirtle, R.L.4
  • 122
    • 18344372735 scopus 로고    scopus 로고
    • M6P/IGF 2R tumor suppressor gene mutated in hepatocellular carcinomas in Japan
    • Oka, Y. et al. M6P/IGF2R tumor suppressor gene mutated in hepatocellular carcinomas in Japan. Hepatology 35, 1153-1163 (2002).
    • (2002) Hepatology , vol.35 , pp. 1153-1163
    • Oka, Y.1
  • 123
    • 0029934868 scopus 로고    scopus 로고
    • M6P/IGF2 receptor: A candidare breast tumor suppressor gene
    • Hankins, G. R. et al. M6P/IGF2 receptor: a candidare breast tumor suppressor gene. Oncogene 12, 2003-2009 (1996).
    • (1996) Oncogene , vol.12 , pp. 2003-2009
    • Hankins, G.R.1
  • 124
    • 0030716258 scopus 로고    scopus 로고
    • Loss of heterozygosity at the mannose 6-phosphate insulin-like growth factor 2 receptor gene correlates with poor differentiation in early breast carcinomas
    • Chappell, S. A., Walsh, T., Walker, R. A. & Shaw, J. A. Loss of heterozygosity at the mannose 6-phosphate insulin-like growth factor 2 receptor gene correlates with poor differentiation in early breast carcinomas. Br. J. Cancer 76, 1558-1561 (1997).
    • (1997) Br. J. Cancer , vol.76 , pp. 1558-1561
    • Chappell, S.A.1    Walsh, T.2    Walker, R.A.3    Shaw, J.A.4
  • 126
    • 0033959501 scopus 로고    scopus 로고
    • Stable amino-acid sequence of the mannose-6-phosphate/insulin-like growth-factor-II receptor in Ovarian carcinomas with loss of heterozygosity and in breast-cancer cell lines
    • Rey, J. M., Theillet, C., Brouillet, J. P. & Rochefort, H. Stable amino-acid sequence of the mannose-6-phosphate/insulin- like growth-factor-II receptor in Ovarian carcinomas with loss of heterozygosity and in breast-cancer cell lines. Int. J. Cancer 85, 466-473 (2000).
    • (2000) Int. J. Cancer , vol.85 , pp. 466-473
    • Rey, J.M.1    Theillet, C.2    Brouillet, J.P.3    Rochefort, H.4
  • 127
    • 0034745791 scopus 로고    scopus 로고
    • Loss of heterozygosity at the mannose 6-phosphate/insulin-like growth factor receptor locus: A frequent but late event in adrenocortical tumorigenesis
    • Lebouleux, S., Gaston, V., Boulle, N., LeBouc, Y. & Gioquel, C. Loss of heterozygosity at the mannose 6-phosphate/insulin-like growth factor receptor locus: a frequent but late event in adrenocortical tumorigenesis. Eur. J. Endocrinol. 144, 163-168 (2001).
    • (2001) Eur. J. Endocrinol. , vol.144 , pp. 163-168
    • Lebouleux, S.1    Gaston, V.2    Boulle, N.3    LeBouc, Y.4    Gioquel, C.5
  • 129
    • 0033588086 scopus 로고    scopus 로고
    • Disruption of ligand binding to the insulin-like growth factor II/mannose 6-phosphate receptor by cancer-associated missense mutations
    • Byrd, J. C., Devi, G. R., DeSouza, A. T., Jirtle, R. L. & MacDonald, R. G. Disruption of ligand binding to the insulin-like growth factor II/mannose 6-phosphate receptor by cancer-associated missense mutations. J. Biol. Chem. 274, 24408-24416 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 24408-24416
    • Byrd, J.C.1    Devi, G.R.2    DeSouza, A.T.3    Jirtle, R.L.4    MacDonald, R.G.5
  • 130
    • 0033199917 scopus 로고    scopus 로고
    • Altered ligand binding by insulin-like growth factor II/mannose 6-phosphate receptors bearing missense mutations in human cancers
    • Devi, G. R., DeSouza, A. T., Byrd, J. C., Jirtle, R. L. & MacDonald, R. G. Altered ligand binding by insulin-like growth factor II/mannose 6-phosphate receptors bearing missense mutations in human cancers. Cancer Res. 59, 4314-4319 (1999). References 128-130 show that cancer-associated mutations in the Cl-MPR impair receptor function.
    • (1999) Cancer Res. , vol.59 , pp. 4314-4319
    • Devi, G.R.1    DeSouza, A.T.2    Byrd, J.C.3    Jirtle, R.L.4    MacDonald, R.G.5
  • 131
    • 0037123766 scopus 로고    scopus 로고
    • Molecular architecture and functional model of the endocytic AP 2 complex
    • Collins, B. M., McCoy, A. J., Kent, H. M., Evans, P. R. & Owen, D. J. Molecular architecture and functional model of the endocytic AP 2 complex. Cell 109, 523-535 (2002).
    • (2002) Cell , vol.109 , pp. 523-535
    • Collins, B.M.1    McCoy, A.J.2    Kent, H.M.3    Evans, P.R.4    Owen, D.J.5
  • 132
    • 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, S. D., Schmid, S. L., 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. 156, 791-795 (2002).
    • (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
  • 133
    • 0033857523 scopus 로고    scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor 2 receptor, a bona fide tumor suppressor gene or just a promising candidate?
    • DaCosta, S. A., Schumaker, L. M. & Ellis, M. J. Mannose 6-phosphate/insulin-like growth factor 2 receptor, a bona fide tumor suppressor gene or just a promising candidate? J. Mammary Gland Biol. Neoplasia 5, 85-94 (2000).
    • (2000) J. Mammary Gland Biol. Neoplasia , vol.5 , pp. 85-94
    • DaCosta, S.A.1    Schumaker, L.M.2    Ellis, M.J.3
  • 134
    • 0034721646 scopus 로고    scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor II receptor is a death receptor for granzyme B during cytotoxic T cell-induced apoptosis
    • Motyka, B. et al. Mannose 6-phosphate/insulin-like growth factor II receptor is a death receptor for granzyme B during cytotoxic T cell-induced apoptosis. Cell 103, 491-500 (2000).
    • (2000) Cell , vol.103 , pp. 491-500
    • Motyka, B.1


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