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Volumn 6, Issue 3, 2004, Pages 252-259

GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSPORTER; ARF PROTEIN; BINDING PROTEIN; CELL SURFACE PROTEIN; CLATHRIN; COAT PROTEIN; UBIQUITIN;

EID: 11144225699     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1107     Document Type: Article
Times cited : (135)

References (28)
  • 1
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke, L. & Dunn, R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 19, 141-172 (2003).
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 2
    • 0033588918 scopus 로고    scopus 로고
    • Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast
    • Beck, T., Schmidt, A. & Hall, M. N. Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast. J. Cell Biol. 146, 1227-1238 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 1227-1238
    • Beck, T.1    Schmidt, A.2    Hall, M.N.3
  • 3
    • 0030990121 scopus 로고    scopus 로고
    • Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae
    • Roberg, K. J., Rowley, N. & Kaiser, C. A. Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae. J. Cell Biol. 137,1469-1482 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 1469-1482
    • Roberg, K.J.1    Rowley, N.2    Kaiser, C.A.3
  • 4
    • 0035941266 scopus 로고    scopus 로고
    • The Npr1 kinase controls biosynthetic and endocytic sorting of the yeast Gap1 permease
    • De Craene, J. O., Soetens, O. & Andre, B. The Npr1 kinase controls biosynthetic and endocytic sorting of the yeast Gap1 permease. J. Biol. Chem. 276, 43939-43948 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 43939-43948
    • De Craene, J.O.1    Soetens, O.2    Andre, B.3
  • 5
    • 0035858866 scopus 로고    scopus 로고
    • Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease
    • Helliwell, S. B., Losko, S. & Kaiser, C. A. Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease. J. Cell Biol. 153, 649-662 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 649-662
    • Helliwell, S.B.1    Losko, S.2    Kaiser, C.A.3
  • 6
    • 0035941194 scopus 로고    scopus 로고
    • Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1
    • Soetens, O., De Craene, J. O. & Andre, B. Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1. J. Biol. Chem. 276, 43949-43957 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 43949-43957
    • Soetens, O.1    De Craene, J.O.2    Andre, B.3
  • 7
    • 0347762565 scopus 로고    scopus 로고
    • The GGA proteins: Adaptors on the move
    • Bonifacino, J. S. The GGA proteins: Adaptors on the move. Nature Rev Mol. Cell Biol. 5, 23-32 (2004).
    • (2004) Nature Rev. Mol. Cell Biol. , vol.5 , pp. 23-32
    • Bonifacino, J.S.1
  • 8
    • 0034752915 scopus 로고    scopus 로고
    • GGA proteins: New players in the sorting game
    • Boman, A. L. GGA proteins: New players in the sorting game. J. Cell Sci. 114, 3413-3418 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 3413-3418
    • Boman, A.L.1
  • 9
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley, D., Bartel, B. & Varshavsky, A. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature 338, 394-401 (1989).
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 10
    • 0036734542 scopus 로고    scopus 로고
    • ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization
    • Boman, A. L. et al. ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization. Mol. Biol. Cell 13, 3078-3095 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3078-3095
    • Boman, A.L.1
  • 11
    • 0033135511 scopus 로고    scopus 로고
    • TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1 and encode proteins similar to the endosomal proteins HGS and STAM
    • Seroussi, E. et al. TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1 and encode proteins similar to the endosomal proteins HGS and STAM. Genomics 57, 380-388 (1999).
    • (1999) Genomics , vol.57 , pp. 380-388
    • Seroussi, E.1
  • 12
    • 0347362792 scopus 로고    scopus 로고
    • Tom1, a VHS domain-containing protein, interacts with Tollip, ubiquitin, and clathrin
    • Yamakami, M., Yoshimori, T. & Yokosawa, H. Tom1, a VHS domain-containing protein, interacts with Tollip, ubiquitin, and clathrin. J. Biol. Chem. 278, 52865-52872 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 52865-52872
    • Yamakami, M.1    Yoshimori, T.2    Yokosawa, H.3
  • 13
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT.-I
    • Katzmann, D. J., Babst, M. & Emr, S. D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT.-I. Cell 106, 145-155 (2001).
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 14
    • 0242266922 scopus 로고    scopus 로고
    • Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome
    • Bilodeau, P. S., Winistorfer, S. C., Kearney, W. R., Robertson, A. D. & Piper, R. C. Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome. J. Cell Biol. 163, 237-243 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 237-243
    • Bilodeau, P.S.1    Winistorfer, S.C.2    Kearney, W.R.3    Robertson, A.D.4    Piper, R.C.5
  • 15
    • 1342346549 scopus 로고    scopus 로고
    • GAT (GGA and Tom1) domain responsible for ubiquitin binding and ubiquitination
    • DOI: 10.1074/jbc.M311702200
    • Shiba, Y. et al. GAT (GGA and Tom1) domain responsible for ubiquitin binding and ubiquitination. J. Biol. Chem. DOI: 10.1074/jbc.M311702200 (2003).
    • (2003) J. Biol. Chem.
    • Shiba, Y.1
  • 16
    • 0141816772 scopus 로고    scopus 로고
    • A nonconserved Ala401 in the yeast Rsp5 ubiquitin ligase is involved in degradation of Gap1 permease and stress-induced abnormal proteins
    • Hoshikawa, C., Shichiri, M., Nakamori, S. & Takagi, H. A nonconserved Ala401 in the yeast Rsp5 ubiquitin ligase is involved in degradation of Gap1 permease and stress-induced abnormal proteins. Proc. Natl Acad. Sci. USA 100, 11505-11510 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11505-11510
    • Hoshikawa, C.1    Shichiri, M.2    Nakamori, S.3    Takagi, H.4
  • 17
    • 0027175829 scopus 로고
    • Cis- and trans-acting functions required for endocytosis of the yeast pheromone receptors
    • Davis, N. G., Horecka, J. L. & Sprague, G. F. Jr. Cis- and trans-acting functions required for endocytosis of the yeast pheromone receptors. J. Cell Biol. 122, 53-65 (1993).
    • (1993) J. Cell Biol. , vol.122 , pp. 53-65
    • Davis, N.G.1    Horecka, J.L.2    Sprague Jr., G.F.3
  • 18
    • 0034852403 scopus 로고    scopus 로고
    • Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole
    • Urbanowski, J. L. & Piper, R. C. Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole. Traffic 2, 622-630 (2001).
    • (2001) Traffic , vol.2 , pp. 622-630
    • Urbanowski, J.L.1    Piper, R.C.2
  • 19
    • 0035862757 scopus 로고    scopus 로고
    • Yeast GGA proteins interact with GTP-bound Arf and facilitate transport through the Golgi
    • Zhdankina, O., Strand, N. L., Redmond, J. M. & Boman, A. L. Yeast GGA proteins interact with GTP-bound Arf and facilitate transport through the Golgi. Yeast 18, 1-18 (2001).
    • (2001) Yeast , vol.18 , pp. 1-18
    • Zhdankina, O.1    Strand, N.L.2    Redmond, J.M.3    Boman, A.L.4
  • 20
    • 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
  • 21
    • 0344304559 scopus 로고    scopus 로고
    • Mammalian GGAs act together to sort mannose 6-phosphate receptors
    • Ghosh, P., Griffith, J., Geuze, H. J. & Kornfeld, S. Mammalian GGAs act together to sort mannose 6-phosphate receptors. J. Cell Biol. 163, 755-766 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 755-766
    • Ghosh, P.1    Griffith, J.2    Geuze, H.J.3    Kornfeld, S.4
  • 22
    • 0034677207 scopus 로고    scopus 로고
    • Monoubiquitin carries a novel internalization signal that is appended to activated receptors
    • Shih, S. C., Sloper-Mould, K. E. & Hicke, L. Monoubiquitin carries a novel internalization signal that is appended to activated receptors. EMBO J. 19, 187-198 (2000).
    • (2000) EMBO J. , vol.19 , pp. 187-198
    • Shih, S.C.1    Sloper-Mould, K.E.2    Hicke, L.3
  • 23
    • 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
  • 24
    • 0037129945 scopus 로고    scopus 로고
    • Electrostatic interactions in ubiquitin: Stabilization of carboxylates by lysine amino groups
    • Sundd, M., Iverson, N., Ibarra-Molero, B., Sanchez-Ruiz, J. M. & Robertson, A. D. Electrostatic interactions in ubiquitin: stabilization of carboxylates by lysine amino groups. Biochemistry 41, 7586-7596 (2002).
    • (2002) Biochemistry , vol.41 , pp. 7586-7596
    • Sundd, M.1    Iverson, N.2    Ibarra-Molero, B.3    Sanchez-Ruiz, J.M.4    Robertson, A.D.5
  • 25
    • 0035075187 scopus 로고    scopus 로고
    • Kinetics of unfolding and folding from amide hydrogen exchange in native ubiquitin
    • Sivaraman, T., Arrington, C. B. & Robertson, A. D. Kinetics of unfolding and folding from amide hydrogen exchange in native ubiquitin. Nature Struct. Biol. 8, 331-333 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 331-333
    • Sivaraman, T.1    Arrington, C.B.2    Robertson, A.D.3
  • 26
    • 10744232828 scopus 로고    scopus 로고
    • Synthesis, structural and biological studies of ubiquitin mutants containing (2S, 4S)-5-fluoroleucine residues strategically placed in the hydrophobic core
    • Alexeev, D. et al. Synthesis, structural and biological studies of ubiquitin mutants containing (2S, 4S)-5-fluoroleucine residues strategically placed in the hydrophobic core. Chembiochem. 4, 894-896 (2003).
    • (2003) Chembiochem. , vol.4 , pp. 894-896
    • Alexeev, D.1
  • 27
    • 0036304360 scopus 로고    scopus 로고
    • The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein sorting
    • Bilodeau, P. S., Urbanowski, J. L., Winistorfer, S. C. & Piper, R. C. The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nature Cell Biol. 4, 534-539 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 534-539
    • Bilodeau, P.S.1    Urbanowski, J.L.2    Winistorfer, S.C.3    Piper, R.C.4
  • 28
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S. et al. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 953-961 (1998).
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1


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