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Volumn 9, Issue 7, 2004, Pages 611-618

The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID A RECEPTOR; ADENOSINE TRIPHOSPHATASE; MICROTUBULE ASSOCIATED PROTEIN; MICROTUBULE ASSOCIATED PROTEIN LIGHT CHAIN 3; NEDD8 PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 4344696843     PISSN: 13569597     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1356-9597.2004.00750.x     Document Type: Article
Times cited : (146)

References (38)
  • 1
    • 0028230738 scopus 로고
    • Ultrastructural analysis of the autophagic process in yeast: Detection of autophagosomes and their characterization
    • Baba, M., Takeshige, K., Baba, N. & Ohsumi, Y. (1994) Ultrastructural analysis of the autophagic process in yeast: detection of autophagosomes and their characterization. J. Cell Biol. 124, 903-913.
    • (1994) J. Cell Biol. , vol.124 , pp. 903-913
    • Baba, M.1    Takeshige, K.2    Baba, N.3    Ohsumi, Y.4
  • 2
    • 0036193182 scopus 로고    scopus 로고
    • Crystal structure of the GABA (A) - Receptor-associated protein, GABARAP
    • Bavro, V.N., Sola, M., Bracher, A., Kneussel, M., Betz, H. & Weissenhorn, W. (2002) Crystal structure of the GABA (A) - receptor-associated protein, GABARAP. EMBO Rep. 3, 183-189.
    • (2002) EMBO Rep. , vol.3 , pp. 183-189
    • Bavro, V.N.1    Sola, M.2    Bracher, A.3    Kneussel, M.4    Betz, H.5    Weissenhorn, W.6
  • 3
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T., Adams, P.D., Clore, G.M., et al. (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1    Adams, P.D.2    Clore, G.M.3
  • 4
    • 0003999245 scopus 로고    scopus 로고
    • Version OpenGL. 1. Marseille: Universite Aix-Marseille II
    • Cambillau, C. & Roussel, A. (1997) Turbo-Frodo, Version OpenGL. 1. Marseille: Universite Aix-Marseille II.
    • (1997) Turbo-Frodo
    • Cambillau, C.1    Roussel, A.2
  • 5
    • 0037012104 scopus 로고    scopus 로고
    • Structure of GABARAP in two conformations: Implications for GABA (A) receptor localization and tubulin binding
    • Coyle, J.E., Qamar, S., Rajashankar, K.R. & Nikolov, D.B. (2002) Structure of GABARAP in two conformations: implications for GABA (A) receptor localization and tubulin binding. Neuron 33, 63-74.
    • (2002) Neuron , vol.33 , pp. 63-74
    • Coyle, J.E.1    Qamar, S.2    Rajashankar, K.R.3    Nikolov, D.B.4
  • 6
    • 0347695019 scopus 로고    scopus 로고
    • A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L
    • Hemelaar, J., Lelyveld, V.S., Kessler, B.M. & Ploegh, H.L. (2003) A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L. J. Biol. Chem. 278, 51841-51850.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51841-51850
    • Hemelaar, J.1    Lelyveld, V.S.2    Kessler, B.M.3    Ploegh, H.L.4
  • 7
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm, L. & Sander, C. (1996) Mapping the protein universe. Science 273, 595-603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 8
    • 0034707036 scopus 로고    scopus 로고
    • A ubiquitin-like system mediates protein lipidation
    • Ichimura, Y., Kirisako, T., Takao, T., et al. (2000) A ubiquitin-like system mediates protein lipidation. Nature 408, 489-493.
    • (2000) Nature , vol.408 , pp. 489-493
    • Ichimura, Y.1    Kirisako, T.2    Takao, T.3
  • 9
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya, Y., Mizushima, N., Ueno, T., et al. (2000) LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J. 19, 5720-5728.
    • (2000) EMBO J. , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3
  • 11
    • 0034676037 scopus 로고    scopus 로고
    • The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway
    • Kirisako, T., Ichimura, Y., Okada, H., et al. (2000) The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway. J. Cell Biol. 151, 263-275.
    • (2000) J. Cell Biol. , vol.151 , pp. 263-275
    • Kirisako, T.1    Ichimura, Y.2    Okada, H.3
  • 12
    • 0033280667 scopus 로고    scopus 로고
    • Vacuolar import of proteins and organelles from the cytoplasm
    • Klionsky, D.J. & Ohsumi, Y. (1999) Vacuolar import of proteins and organelles from the cytoplasm. Annu. Rev. Cell Dev. Biol. 15, 1-32.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 1-32
    • Klionsky, D.J.1    Ohsumi, Y.2
  • 13
    • 0037085253 scopus 로고    scopus 로고
    • The X-ray crystal structure and putative ligand-derived peptide binding properties of gamma-aminobutyric acid receptor type A receptor-associated protein
    • Knight, D., Harris, R., McAlister, M.S., et al. (2002) The X-ray crystal structure and putative ligand-derived peptide binding properties of gamma-aminobutyric acid receptor type A receptor-associated protein. J. Biol. Chem. 277, 5556-5561.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5556-5561
    • Knight, D.1    Harris, R.2    McAlister, M.S.3
  • 14
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 15
    • 0032579507 scopus 로고    scopus 로고
    • Isolation and characterization of a novel low molecular weight protein involved in intra-Golgi traffic
    • Legesse-Miller, A., Sagiv, Y., Porat, A. & Elazar, Z. (1998) Isolation and characterization of a novel low molecular weight protein involved in intra-Golgi traffic. J. Biol. Chem. 273, 3105-3109.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3105-3109
    • Legesse-Miller, A.1    Sagiv, Y.2    Porat, A.3    Elazar, Z.4
  • 16
    • 0028289946 scopus 로고
    • Molecular characterization of light chain 3. A micrombule binding subunit of MAP1A and MAP1B
    • Mann, S.S. & Hammarback, J.A. (1994) Molecular characterization of light chain 3. A micrombule binding subunit of MAP1A and MAP1B. J. Biol. Chem. 269, 11492-11497.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11492-11497
    • Mann, S.S.1    Hammarback, J.A.2
  • 17
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E.A. & Bacon, D.J. (1997) Raster3D: photorealistic molecular graphics. Meth. Enzymol. 277, 505-524.
    • (1997) Meth. Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 18
    • 0023065242 scopus 로고
    • Intracellular protein catabolism and its control during nutrient deprivation and supply
    • Mortimore, G.E. & Poso, A.R. (1987) Intracellular protein catabolism and its control during nutrient deprivation and supply. Annu. Rev. Nutr. 7, 539-564.
    • (1987) Annu. Rev. Nutr. , vol.7 , pp. 539-564
    • Mortimore, G.E.1    Poso, A.R.2
  • 19
    • 0029107760 scopus 로고
    • The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
    • Nassar, N., Horn, G., Herrmann, C., Scherer, A., McCormick, F. & Wittinghofer, A. (1995) The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature 375, 554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 20
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. & Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 21
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Ohsumi, Y. (2001) Molecular dissection of autophagy: two ubiquitin-like systems. Nature Rev. Mol. Cell Biol. 2, 211-216.
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Meth. Enzymol. 276, 307-326.
    • (1997) Meth. Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 23
    • 0034682843 scopus 로고    scopus 로고
    • Structure of GATE-16, membrane transport modulator and mammalian ortholog of autophagocytosis factor Aut7p
    • Paz, Y., Elazar, Z. & Fass, D. (2000) Structure of GATE-16, membrane transport modulator and mammalian ortholog of autophagocytosis factor Aut7p. J. Biol. Chem. 275, 25445-25450.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25445-25450
    • Paz, Y.1    Elazar, Z.2    Fass, D.3
  • 25
    • 0001417555 scopus 로고    scopus 로고
    • GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28
    • Sagiv, Y., Legesse-Miller, A., Porat, A. & Elazar, Z. (2000) GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28. EMBO J. 19, 1494-1504.
    • (2000) EMBO J. , vol.19 , pp. 1494-1504
    • Sagiv, Y.1    Legesse-Miller, A.2    Porat, A.3    Elazar, Z.4
  • 26
    • 0037515749 scopus 로고    scopus 로고
    • The COOH terminus of GATE-16, an intra-Golgi transport modulator, is cleaved by the human cysteine protease HsApg4A
    • Scherz-Shouval, R., Sagiv, Y., Shorer, H. & Elazar, Z. (2003) The COOH terminus of GATE-16, an intra-Golgi transport modulator, is cleaved by the human cysteine protease HsApg4A. J. Biol. Chem. 278, 14053-14058.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14053-14058
    • Scherz-Shouval, R.1    Sagiv, Y.2    Shorer, H.3    Elazar, Z.4
  • 27
    • 0037134507 scopus 로고    scopus 로고
    • Solution structure of human GABA (A) receptor-associated protein GABARAP: Implications for biological function and its regulation
    • Stangler, T., Mayr, L.M. & Willbold, D. (2002) Solution structure of human GABA (A) receptor-associated protein GABARAP: implications for biological function and its regulation. J. Biol. Chem. 19, 13363-13366.
    • (2002) J. Biol. Chem. , vol.19 , pp. 13363-13366
    • Stangler, T.1    Mayr, L.M.2    Willbold, D.3
  • 29
    • 0037449938 scopus 로고    scopus 로고
    • GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and Apg3
    • Tanida, I., Komatsu, M., Ueno, T. & Kominami, E. (2003) GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and Apg3. Biochem. Biophys. Res. Commun. 300, 637-644.
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 637-644
    • Tanida, I.1    Komatsu, M.2    Ueno, T.3    Kominami, E.4
  • 30
    • 0037134443 scopus 로고    scopus 로고
    • Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p
    • Tanida, I., Tanida-Miyake, E., Komatsu, M., Ueno, T. & Kominami, E. (2002) Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p. J. Biol. Chem. 277, 13739-13744.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13739-13744
    • Tanida, I.1    Tanida-Miyake, E.2    Komatsu, M.3    Ueno, T.4    Kominami, E.5
  • 31
    • 0035910423 scopus 로고    scopus 로고
    • The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP and MAP-LC3
    • Tanida, I., Tanida-Miyake, E., Ueno, T. & Kominami, E. (2001) The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP and MAP-LC3. J. Biol. Chem. 276, 1701-1706.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1701-1706
    • Tanida, I.1    Tanida-Miyake, E.2    Ueno, T.3    Kominami, E.4
  • 32
    • 0035421234 scopus 로고    scopus 로고
    • Structure and ligand recognition of the PB1 domain: A novel protein module binding to the PC motif
    • Terasawa, H., Noda, Y, Ito, T., et al. (2001) Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif EMBO J. 20, 3947-3956.
    • (2001) EMBO J. , vol.20 , pp. 3947-3956
    • Terasawa, H.1    Noda, Y.2    Ito, T.3
  • 33
    • 0027936092 scopus 로고
    • Isolation of autophagocytosis mutants of Saccharomyces cerevisiae
    • Thumm, M., Egner, R., Koch, B., et al. (1994) Isolation of autophagocytosis mutants of Saccharomyces cerevisiae. FEBS Lett. 349, 275-280.
    • (1994) FEBS Lett. , vol.349 , pp. 275-280
    • Thumm, M.1    Egner, R.2    Koch, B.3
  • 34
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada, M. & Ohsumi, Y. (1993) Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett. 333, 169-174.
    • (1993) FEBS Lett. , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 36
    • 0347416977 scopus 로고    scopus 로고
    • The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1
    • Walden, H., Podgorski, M.S., Huang, D.T., et al. (2003) The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1. Mol. Cell 12, 1427-1437.
    • (2003) Mol. Cell , vol.12 , pp. 1427-1437
    • Walden, H.1    Podgorski, M.S.2    Huang, D.T.3
  • 37
    • 0033531225 scopus 로고    scopus 로고
    • GABA (A) - Receptor-associated protein links GABA (A) receptors and the cytoskeleton
    • Wang, H., Bedford, F.K., Brandon, N.J., Moss, S.J. & Olsen, R.W. (1999) GABA (A) - receptor-associated protein links GABA (A) receptors and the cytoskeleton. Nature 397, 69-72.
    • (1999) Nature , vol.397 , pp. 69-72
    • Wang, H.1    Bedford, F.K.2    Brandon, N.J.3    Moss, S.J.4    Olsen, R.W.5
  • 38
    • 0141642043 scopus 로고    scopus 로고
    • The PB1 domain and the PC motif-containing region are structurally similar protein binding modules
    • Yoshinaga, S., Kohjima, M., Ogura, K., et al. (2003) The PB1 domain and the PC motif-containing region are structurally similar protein binding modules. EMBO J. 22, 4888-4897.
    • (2003) EMBO J. , vol.22 , pp. 4888-4897
    • Yoshinaga, S.1    Kohjima, M.2    Ogura, K.3


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