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Volumn 127, Issue 1, 2014, Pages 3-9

The LC3 interactome at a glance

Author keywords

Aim; Atg8; Autophagy; Gabarap; Lc3; LIR motif

Indexed keywords

4 AMINOBUTYRIC ACID RECEPTOR ASSOCIATED PROTEIN; CELL PROTEIN; LIGHT CHAIN 3; PEPTIDES AND PROTEINS; PROTEIN ATG8; UNCLASSIFIED DRUG;

EID: 84891461247     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.140426     Document Type: Article
Times cited : (233)

References (125)
  • 2
    • 14944383217 scopus 로고    scopus 로고
    • Automated yeast two-hybrid screening for nuclear receptorinteracting proteins
    • Albers, M., Kranz, H., Kober, I., Kaiser, C., Klink, M., Suckow, J., Kern, R. and Koegl, M. (2005). Automated yeast two-hybrid screening for nuclear receptorinteracting proteins. MCP 4, 205-213.
    • (2005) MCP , vol.4 , pp. 205-213
    • Albers, M.1    Kranz, H.2    Kober, I.3    Kaiser, C.4    Klink, M.5    Suckow, J.6    Kern, R.7    Koegl, M.8
  • 5
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends, C., Sowa, M. E., Gygi, S. P. and Harper, J. W. (2010). Network organization of the human autophagy system. Nature 466, 68-76.
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 6
    • 84883414890 scopus 로고    scopus 로고
    • The LIR motif - crucial for selective autophagy
    • Birgisdottir, A. B., Lamark, T. and Johansen, T. (2013). The LIR motif - crucial for selective autophagy. J. Cell Sci. 126, 3237-3247.
    • (2013) J. Cell Sci. , vol.126 , pp. 3237-3247
    • Birgisdottir, A.B.1    Lamark, T.2    Johansen, T.3
  • 7
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Overvatn, A., Stenmark, H. and Johansen, T. (2005). p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171, 603-614.
    • (2005) J. Cell Biol. , vol.171 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 8
    • 77956519105 scopus 로고    scopus 로고
    • Cytoskeletal scaffolding proteins interact with Lynch-Syndrome associated mismatch repair protein MLH1
    • Brieger, A., Adryan, B., Wolpert, F., Passmann, S., Zeuzem, S. and Trojan, J. (2010). Cytoskeletal scaffolding proteins interact with Lynch-Syndrome associated mismatch repair protein MLH1. Proteomics 10, 3343-3355.
    • (2010) Proteomics , vol.10 , pp. 3343-3355
    • Brieger, A.1    Adryan, B.2    Wolpert, F.3    Passmann, S.4    Zeuzem, S.5    Trojan, J.6
  • 9
    • 79953331726 scopus 로고    scopus 로고
    • Structural and functional roles of Daxx SIM phosphorylation in SUMO paralog-selective binding and apoptosis modulation
    • Chang, C. C., Naik, M. T., Huang, Y. S., Jeng, J. C., Liao, P. H., Kuo, H. Y., Ho, C. C., Hsieh, Y. L., Lin, C. H., Huang, N. J. et al. (2011a). Structural and functional roles of Daxx SIM phosphorylation in SUMO paralog-selective binding and apoptosis modulation. Mol. Cell 42, 62-74.
    • (2011) Mol. Cell , vol.42 , pp. 62-74
    • Chang, C.C.1    Naik, M.T.2    Huang, Y.S.3    Jeng, J.C.4    Liao, P.H.5    Kuo, H.Y.6    Ho, C.C.7    Hsieh, Y.L.8    Lin, C.H.9    Huang, N.J.10
  • 11
    • 33646372722 scopus 로고    scopus 로고
    • GEC1 interacts with the kappa opioid receptor and enhances expression of the receptor
    • Chen, C., Li, J. G., Chen, Y., Huang, P., Wang, Y. and Liu-Chen, L. Y. (2006). GEC1 interacts with the kappa opioid receptor and enhances expression of the receptor. J. Biol. Chem. 281, 7983-7993.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7983-7993
    • Chen, C.1    Li, J.G.2    Chen, Y.3    Huang, P.4    Wang, Y.5    Liu-Chen, L.Y.6
  • 15
    • 82355175806 scopus 로고    scopus 로고
    • Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis
    • D'Agostino, C., Nogalska, A., Cacciottolo, M., Engel, W. K. and Askanas, V. (2011). Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis. Acta Neuropathol. 122, 627-636.
    • (2011) Acta Neuropathol , vol.122 , pp. 627-636
    • D'Agostino, C.1    Nogalska, A.2    Cacciottolo, M.3    Engel, W.K.4    Askanas, V.5
  • 20
    • 84877579321 scopus 로고    scopus 로고
    • Phosphorylation of mitophagy and pexophagy receptors coordinates their interaction with Atg8 and Atg11
    • Farré, J. C., Burkenroad, A., Burnett, S. F. and Subramani, S. (2013). Phosphorylation of mitophagy and pexophagy receptors coordinates their interaction with Atg8 and Atg11. EMBO Rep. 14, 441-449.
    • (2013) EMBO Rep , vol.14 , pp. 441-449
    • Farré, J.C.1    Burkenroad, A.2    Burnett, S.F.3    Subramani, S.4
  • 21
    • 79953227034 scopus 로고    scopus 로고
    • A genome-wide enhancer screen implicates sphingolipid composition in vacuolar ATPase function in Saccharomyces cerevisiae
    • Finnigan, G. C., Ryan, M. and Stevens, T. H. (2011). A genome-wide enhancer screen implicates sphingolipid composition in vacuolar ATPase function in Saccharomyces cerevisiae. Genetics 187, 771-783.
    • (2011) Genetics , vol.187 , pp. 771-783
    • Finnigan, G.C.1    Ryan, M.2    Stevens, T.H.3
  • 22
    • 77955172368 scopus 로고    scopus 로고
    • Autophagy negatively regulates Wnt signalling by promoting Dishevelled degradation
    • Gao, C., Cao, W., Bao, L., Zuo, W., Xie, G., Cai, T., Fu, W., Zhang, J., Wu, W., Zhang, X. et al. (2010). Autophagy negatively regulates Wnt signalling by promoting Dishevelled degradation. Nat. Cell Biol. 12, 781-790.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 781-790
    • Gao, C.1    Cao, W.2    Bao, L.3    Zuo, W.4    Xie, G.5    Cai, T.6    Fu, W.7    Zhang, J.8    Wu, W.9    Zhang, X.10
  • 24
    • 0037042222 scopus 로고    scopus 로고
    • Association of human transferrin receptor with GABARAP
    • Green, F., O'Hare, T., Blackwell, A. and Enns, C. A. (2002). Association of human transferrin receptor with GABARAP. FEBS Lett. 518, 101-106.
    • (2002) FEBS Lett , vol.518 , pp. 101-106
    • Green, F.1    O'Hare, T.2    Blackwell, A.3    Enns, C.A.4
  • 25
    • 3242877218 scopus 로고    scopus 로고
    • Rab7 is required for the normal progression of the autophagic pathway in mammalian cells
    • Gutierrez, M. G., Munafö, D. B., Berön, W. and Colombo, M. I. (2004). Rab7 is required for the normal progression of the autophagic pathway in mammalian cells. J. Cell Sci. 117, 2687-2697.
    • (2004) J. Cell Sci. , vol.117 , pp. 2687-2697
    • Gutierrez, M.G.1    Munafö, D.B.2    Berön, W.3    Colombo, M.I.4
  • 26
    • 84861733247 scopus 로고    scopus 로고
    • Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy
    • Hanna, R. A., Quinsay, M. N., Orogo, A. M., Giang, K., Rikka, S. and Gustafsson, A. B. (2012). Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy. J. Biol. Chem. 287, 19094-19104.
    • (2012) J. Biol. Chem. , vol.287 , pp. 19094-19104
    • Hanna, R.A.1    Quinsay, M.N.2    Orogo, A.M.3    Giang, K.4    Rikka, S.5    Gustafsson, A.B.6
  • 28
    • 66349086236 scopus 로고    scopus 로고
    • Mutation at the cargo-receptor binding site of Atg8 also affects its general autophagy regulation function
    • Ho, K. H., Chang, H. E. and Huang, W. P. (2009). Mutation at the cargo-receptor binding site of Atg8 also affects its general autophagy regulation function. Autophagy 5, 461-471.
    • (2009) Autophagy , vol.5 , pp. 461-471
    • Ho, K.H.1    Chang, H.E.2    Huang, W.P.3
  • 29
    • 48849089284 scopus 로고    scopus 로고
    • Systematic genetic array analysis links the Saccharomyces cerevisiae SAGA/SLIK and NuA4 component Tra1 to multiple cellular processes
    • Hoke, S. M., Guzzo, J., Andrews, B. and Brandl, C. J. (2008). Systematic genetic array analysis links the Saccharomyces cerevisiae SAGA/SLIK and NuA4 component Tra1 to multiple cellular processes. BMC Genet. 9, 46.
    • (2008) BMC Genet , vol.9 , pp. 46
    • Hoke, S.M.1    Guzzo, J.2    Andrews, B.3    Brandl, C.J.4
  • 34
    • 50249098491 scopus 로고    scopus 로고
    • Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation
    • Itoh, T., Fujita, N., Kanno, E., Yamamoto, A., Yoshimori, T. and Fukuda, M. (2008). Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation. Mol. Biol. Cell 19, 2916-2925.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2916-2925
    • Itoh, T.1    Fujita, N.2    Kanno, E.3    Yamamoto, A.4    Yoshimori, T.5    Fukuda, M.6
  • 35
    • 79952422876 scopus 로고    scopus 로고
    • OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation
    • Itoh, T., Kanno, E., Uemura, T., Waguri, S. and Fukuda, M. (2011). OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation. J. Cell Biol. 192, 839-853.
    • (2011) J. Cell Biol. , vol.192 , pp. 839-853
    • Itoh, T.1    Kanno, E.2    Uemura, T.3    Waguri, S.4    Fukuda, M.5
  • 40
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki, T., Wang, K., Cao, Y., Baba, M. and Klionsky, D. J. (2009). Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev. Cell 17, 98-109.
    • (2009) Dev. Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 41
    • 79953182366 scopus 로고    scopus 로고
    • A new autophagy-related checkpoint in the degradation of an ERAD-M target
    • Kario, E., Amar, N., Elazar, Z. and Navon, A. (2011). A new autophagy-related checkpoint in the degradation of an ERAD-M target. J. Biol. Chem. 286, 11479-11491.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11479-11491
    • Kario, E.1    Amar, N.2    Elazar, Z.3    Navon, A.4
  • 42
    • 0037016752 scopus 로고    scopus 로고
    • Convergence of multiple autophagy and cytoplasm to vacuole targeting components to a perivacuolar membrane compartment prior to de novo vesicle formation
    • Kim, J., Huang, W. P., Stromhaug, P. E. and Klionsky, D. J. (2002). Convergence of multiple autophagy and cytoplasm to vacuole targeting components to a perivacuolar membrane compartment prior to de novo vesicle formation. J. Biol. Chem. 277, 763-773.
    • (2002) J. Biol. Chem. , vol.277 , pp. 763-773
    • Kim, J.1    Huang, W.P.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 44
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin, V., McEwan, D. G., Novak, I. and Dikic, I. (2009b). A role for ubiquitin in selective autophagy. Mol. Cell 34, 259-269.
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 45
    • 0034919997 scopus 로고    scopus 로고
    • The subcellular distribution of GABARAP and its ability to interact with NSF suggest a role for this protein in the intracellular transport of GABA(A) receptors
    • Kittler, J. T., Rostaing, P., Schiavo, G., Fritschy, J. M., Olsen, R., Triller, A. and Moss, S. J. (2001). The subcellular distribution of GABARAP and its ability to interact with NSF suggest a role for this protein in the intracellular transport of GABA(A) receptors. Mol. Cell. Neurosci. 18, 13-25.
    • (2001) Mol. Cell. Neurosci. , vol.18 , pp. 13-25
    • Kittler, J.T.1    Rostaing, P.2    Schiavo, G.3    Fritschy, J.M.4    Olsen, R.5    Triller, A.6    Moss, S.J.7
  • 47
    • 0035971160 scopus 로고    scopus 로고
    • The C-terminal region of an Apg7p/Cvt2p is required for homodimerization and is essential for its E1 activity and E1-E2 complex formation
    • Komatsu, M., Tanida, I., Ueno, T., Ohsumi, M., Ohsumi, Y. and Kominami, E. (2001). The C-terminal region of an Apg7p/Cvt2p is required for homodimerization and is essential for its E1 activity and E1-E2 complex formation. J. Biol. Chem. 276, 9846-9854.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9846-9854
    • Komatsu, M.1    Tanida, I.2    Ueno, T.3    Ohsumi, M.4    Ohsumi, Y.5    Kominami, E.6
  • 48
    • 36849089101 scopus 로고    scopus 로고
    • Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice
    • Komatsu, M., Waguri, S., Koike, M., Sou, Y. S., Ueno, T., Hara, T., Mizushima, N., Iwata, J., Ezaki, J., Murata, S. et al. (2007). Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131, 1149-1163.
    • (2007) Cell , vol.131 , pp. 1149-1163
    • Komatsu, M.1    Waguri, S.2    Koike, M.3    Sou, Y.S.4    Ueno, T.5    Hara, T.6    Mizushima, N.7    Iwata, J.8    Ezaki, J.9    Murata, S.10
  • 51
    • 77956410115 scopus 로고    scopus 로고
    • Selective autophagy: ubiquitinmediated recognition and beyond
    • Kraft, C., Peter, M. and Hofmann, K. (2010). Selective autophagy: ubiquitinmediated recognition and beyond. Nat. Cell Biol. 12, 836-841.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 836-841
    • Kraft, C.1    Peter, M.2    Hofmann, K.3
  • 52
    • 77957200921 scopus 로고    scopus 로고
    • Cdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert with ubiquitin-like Atg8
    • Krick, R., Bremer, S., Welter, E., Schlotterhose, P., Muehe, Y., Eskelinen, E. L. and Thumm, M. (2010). Cdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert with ubiquitin-like Atg8. J. Cell Biol. 190, 965-973.
    • (2010) J. Cell Biol. , vol.190 , pp. 965-973
    • Krick, R.1    Bremer, S.2    Welter, E.3    Schlotterhose, P.4    Muehe, Y.5    Eskelinen, E.L.6    Thumm, M.7
  • 54
    • 0023156677 scopus 로고
    • 18 kDa microtubule-associated protein: identification as a new light chain (LC-3) of microtubule-associated protein 1 (MAP-1)
    • Kuznetsov, S. A. and Gelfand, V. I. (1987). 18 kDa microtubule-associated protein: identification as a new light chain (LC-3) of microtubule-associated protein 1 (MAP-1). FEBS Lett. 212, 145-148.
    • (1987) FEBS Lett , vol.212 , pp. 145-148
    • Kuznetsov, S.A.1    Gelfand, V.I.2
  • 55
    • 0032126632 scopus 로고    scopus 로고
    • Aut2p and Aut7p, two novel microtubule-associated proteins are essential for delivery of autophagic vesicles to the vacuole
    • Lang, T., Schaeffeler, E., Bernreuther, D., Bredschneider, M., Wolf, D. H. and Thumm, M. (1998). Aut2p and Aut7p, two novel microtubule-associated proteins are essential for delivery of autophagic vesicles to the vacuole. EMBO J. 17, 3597-3607.
    • (1998) EMBO J , vol.17 , pp. 3597-3607
    • Lang, T.1    Schaeffeler, E.2    Bernreuther, D.3    Bredschneider, M.4    Wolf, D.H.5    Thumm, M.6
  • 58
    • 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. and 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
  • 59
    • 0034693065 scopus 로고    scopus 로고
    • Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes
    • Legesse-Miller, A., Sagiv, Y., Glozman, R. and Elazar, Z. (2000). Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes. J. Biol. Chem. 275, 32966-32973.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32966-32973
    • Legesse-Miller, A.1    Sagiv, Y.2    Glozman, R.3    Elazar, Z.4
  • 60
    • 10644254853 scopus 로고    scopus 로고
    • GABAA receptorassociated protein traffics GABAA receptors to the plasma membrane in neurons
    • Leil, T. A., Chen, Z. W., Chang, C. S. and Olsen, R. W. (2004). GABAA receptorassociated protein traffics GABAA receptors to the plasma membrane in neurons. J. Neurosci. 24, 11429-11438.
    • (2004) J. Neurosci. , vol.24 , pp. 11429-11438
    • Leil, T.A.1    Chen, Z.W.2    Chang, C.S.3    Olsen, R.W.4
  • 61
    • 74549184412 scopus 로고    scopus 로고
    • The polarisome is required for segregation and retrograde transport of protein aggregates
    • Liu, B., Larsson, L., Caballero, A., Hao, X., Oling, D., Grantham, J. and Nyström, T. (2010). The polarisome is required for segregation and retrograde transport of protein aggregates. Cell 140, 257-267.
    • (2010) Cell , vol.140 , pp. 257-267
    • Liu, B.1    Larsson, L.2    Caballero, A.3    Hao, X.4    Oling, D.5    Grantham, J.6    Nyström, T.7
  • 62
    • 84862789618 scopus 로고    scopus 로고
    • Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
    • Liu, L., Feng, D., Chen, G., Chen, M., Zheng, Q., Song, P., Ma, Q., Zhu, C., Wang, R., Qi, W. et al. (2012). Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells. Nat. Cell Biol. 14, 177-185.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 177-185
    • Liu, L.1    Feng, D.2    Chen, G.3    Chen, M.4    Zheng, Q.5    Song, P.6    Ma, Q.7    Zhu, C.8    Wang, R.9    Qi, W.10
  • 63
    • 0028289946 scopus 로고
    • Molecular characterization of light chain 3. A microtubule binding subunit of MAP1A and MAP1B
    • Mann, S. S. and Hammarback, J. A. (1994). Molecular characterization of light chain 3. A microtubule 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
  • 64
    • 82455172117 scopus 로고    scopus 로고
    • Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins
    • Matsumoto, G., Wada, K., Okuno, M., Kurosawa, M. and Nukina, N. (2011). Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins. Mol. Cell 44, 279-289.
    • (2011) Mol. Cell , vol.44 , pp. 279-289
    • Matsumoto, G.1    Wada, K.2    Okuno, M.3    Kurosawa, M.4    Nukina, N.5
  • 66
    • 79953163464 scopus 로고    scopus 로고
    • The Three Musketeers of Autophagy: phosphorylation, ubiquitylation and acetylation
    • McEwan, D. G. and Dikic, I. (2011). The Three Musketeers of Autophagy: phosphorylation, ubiquitylation and acetylation. Trends Cell Biol. 21, 195-201.
    • (2011) Trends Cell Biol , vol.21 , pp. 195-201
    • McEwan, D.G.1    Dikic, I.2
  • 67
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima, N., Levine, B., Cuervo, A. M. and Klionsky, D. J. (2008). Autophagy fights disease through cellular self-digestion. Nature 451, 1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 68
    • 37249005256 scopus 로고    scopus 로고
    • Identification of clathrin heavy chain as a direct interaction partner for the gamma-aminobutyric acid type A receptor associated protein
    • Mohrlüder, J., Hoffmann, Y., Stangler, T., Hänel, K. and Willbold, D. (2007a). Identification of clathrin heavy chain as a direct interaction partner for the gamma-aminobutyric acid type A receptor associated protein. Biochemistry 46, 14537-14543.
    • (2007) Biochemistry , vol.46 , pp. 14537-14543
    • Mohrlüder, J.1    Hoffmann, Y.2    Stangler, T.3    Hänel, K.4    Willbold, D.5
  • 69
    • 35448936487 scopus 로고    scopus 로고
    • Identification of calreticulin as a ligand of GABARAP by phage display screening of a peptide library
    • Mohrlüder, J., Stangler, T., Hoffmann, Y., Wiesehan, K., Mataruga, A. and Willbold, D. (2007b). Identification of calreticulin as a ligand of GABARAP by phage display screening of a peptide library. FEBS J. 274, 5543-5555.
    • (2007) FEBS J , vol.274 , pp. 5543-5555
    • Mohrlüder, J.1    Stangler, T.2    Hoffmann, Y.3    Wiesehan, K.4    Mataruga, A.5    Willbold, D.6
  • 70
    • 84863843241 scopus 로고    scopus 로고
    • Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae
    • Motley, A. M., Nuttall, J. M. and Hettema, E. H. (2012). Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae. EMBO J. 31, 2852-2868.
    • (2012) EMBO J , vol.31 , pp. 2852-2868
    • Motley, A.M.1    Nuttall, J.M.2    Hettema, E.H.3
  • 71
    • 84865251228 scopus 로고    scopus 로고
    • The autophagy-related protein kinase Atg1 interacts with the ubiquitinlike protein Atg8 via the Atg8 family interacting motif to facilitate autophagosome formation
    • Nakatogawa, H., Ohbayashi, S., Sakoh-Nakatogawa, M., Kakuta, S., Suzuki, S. W., Kirisako, H., Kondo-Kakuta, C., Noda, N. N., Yamamoto, H. and Ohsumi, Y. (2012). The autophagy-related protein kinase Atg1 interacts with the ubiquitinlike protein Atg8 via the Atg8 family interacting motif to facilitate autophagosome formation. J. Biol. Chem. 287, 28503-28507.
    • (2012) J. Biol. Chem. , vol.287 , pp. 28503-28507
    • Nakatogawa, H.1    Ohbayashi, S.2    Sakoh-Nakatogawa, M.3    Kakuta, S.4    Suzuki, S.W.5    Kirisako, H.6    Kondo-Kakuta, C.7    Noda, N.N.8    Yamamoto, H.9    Ohsumi, Y.10
  • 72
    • 67649467294 scopus 로고    scopus 로고
    • Dynamics and diversity in autophagy mechanisms: lessons from yeast
    • Nakatogawa, H., Suzuki, K., Kamada, Y. and Ohsumi, Y. (2009). Dynamics and diversity in autophagy mechanisms: lessons from yeast. Nat. Rev. Mol. Cell Biol. 10, 458-467.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 458-467
    • Nakatogawa, H.1    Suzuki, K.2    Kamada, Y.3    Ohsumi, Y.4
  • 73
    • 84870527124 scopus 로고    scopus 로고
    • TBK1 kinase addiction in lung cancer cells is mediated via autophagy of Tax1bp1/Ndp52 and non-canonical NF-kB signalling
    • Newman, A. C., Scholefield, C. L., Kemp, A. J., Newman, M., McIver, E. G., Kamal, A. and Wilkinson, S. (2012). TBK1 kinase addiction in lung cancer cells is mediated via autophagy of Tax1bp1/Ndp52 and non-canonical NF-kB signalling. PLoS ONE 7, e50672.
    • (2012) PLoS ONE , vol.7
    • Newman, A.C.1    Scholefield, C.L.2    Kemp, A.J.3    Newman, M.4    McIver, E.G.5    Kamal, A.6    Wilkinson, S.7
  • 76
    • 0036312631 scopus 로고    scopus 로고
    • Subunit specificity and interaction domain between GABA(A) receptor-associated protein (GABARAP) and GABA(A) receptors
    • Nymann-Andersen, J., Wang, H., Chen, L., Kittler, J. T., Moss, S. J. and Olsen, R. W. (2002). Subunit specificity and interaction domain between GABA(A) receptor-associated protein (GABARAP) and GABA(A) receptors. J. Neurochem. 80, 815-823.
    • (2002) J. Neurochem. , vol.80 , pp. 815-823
    • Nymann-Andersen, J.1    Wang, H.2    Chen, L.3    Kittler, J.T.4    Moss, S.J.5    Olsen, R.W.6
  • 77
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondriaanchored receptor Atg32 mediates degradation of mitochondria via selective autophagy
    • Okamoto, K., Kondo-Okamoto, N. and Ohsumi, Y. (2009). Mitochondriaanchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. Dev. Cell 17, 87-97.
    • (2009) Dev. Cell , vol.17 , pp. 87-97
    • Okamoto, K.1    Kondo-Okamoto, N.2    Ohsumi, Y.3
  • 78
    • 0034727876 scopus 로고    scopus 로고
    • Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: possible role of vesicular transport in axonal elongation
    • Okazaki, N., Yan, J., Yuasa, S., Ueno, T., Kominami, E., Masuho, Y., Koga, H. and Muramatsu, M. (2000). Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: possible role of vesicular transport in axonal elongation. Brain Res. Mol. Brain Res. 85, 1-12.
    • (2000) Brain Res. Mol. Brain Res. , vol.85 , pp. 1-12
    • Okazaki, N.1    Yan, J.2    Yuasa, S.3    Ueno, T.4    Kominami, E.5    Masuho, Y.6    Koga, H.7    Muramatsu, M.8
  • 79
    • 79960325950 scopus 로고    scopus 로고
    • Inhibition of protein degradation induces apoptosis through a microtubule-associated protein 1 light chain 3-mediated activation of caspase-8 at intracellular membranes
    • Pan, J. A., Ullman, E., Dou, Z. and Zong, W. X. (2011). Inhibition of protein degradation induces apoptosis through a microtubule-associated protein 1 light chain 3-mediated activation of caspase-8 at intracellular membranes. Mol. Cell. Biol. 31, 3158-3170.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3158-3170
    • Pan, J.A.1    Ullman, E.2    Dou, Z.3    Zong, W.X.4
  • 80
    • 76149086512 scopus 로고    scopus 로고
    • FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport
    • Pankiv, S., Alemu, E. A., Brech, A., Bruun, J. A., Lamark, T., Overvatn, A., Bjørkøy, G. and Johansen, T. (2010). FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport. J. Cell Biol. 188, 253-269.
    • (2010) J. Cell Biol. , vol.188 , pp. 253-269
    • Pankiv, S.1    Alemu, E.A.2    Brech, A.3    Bruun, J.A.4    Lamark, T.5    Overvatn, A.6    Bjørkøy, G.7    Johansen, T.8
  • 82
    • 84871911332 scopus 로고    scopus 로고
    • Identifying protein partners of CLN8, an ER-resident protein involved in neuronal ceroid lipofuscinosis
    • Passantino, R., Cascio, C., Deidda, I., Galizzi, G., Russo, D., Spedale, G. and Guarneri, P. (2013). Identifying protein partners of CLN8, an ER-resident protein involved in neuronal ceroid lipofuscinosis. Biochim. Biophys. Acta 1833, 529-540.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 529-540
    • Passantino, R.1    Cascio, C.2    Deidda, I.3    Galizzi, G.4    Russo, D.5    Spedale, G.6    Guarneri, P.7
  • 84
    • 84861396483 scopus 로고    scopus 로고
    • Rab GTPase-activating proteins in autophagy: regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers
    • Popovic, D., Akutsu, M., Novak, I., Harper, J. W., Behrends, C. and Dikic, I. (2012). Rab GTPase-activating proteins in autophagy: regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers. Mol. Cell. Biol. 32, 1733-1744.
    • (2012) Mol. Cell. Biol , vol.32 , pp. 1733-1744
    • Popovic, D.1    Akutsu, M.2    Novak, I.3    Harper, J.W.4    Behrends, C.5    Dikic, I.6
  • 88
    • 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. and 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
  • 91
    • 65649136884 scopus 로고    scopus 로고
    • The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy
    • Satoo, K., Noda, N. N., Kumeta, H., Fujioka, Y., Mizushima, N., Ohsumi, Y. and Inagaki, F. (2009). The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy. EMBO J. 28, 1341-1350.
    • (2009) EMBO J , vol.28 , pp. 1341-1350
    • Satoo, K.1    Noda, N.N.2    Kumeta, H.3    Fujioka, Y.4    Mizushima, N.5    Ohsumi, Y.6    Inagaki, F.7
  • 93
    • 84864809503 scopus 로고    scopus 로고
    • Ubiquitin-like proteins and autophagy at a glance
    • Shpilka, T., Mizushima, N. and Elazar, Z. (2012). Ubiquitin-like proteins and autophagy at a glance. J. Cell Sci. 125, 2343-2348.
    • (2012) J. Cell Sci. , vol.125 , pp. 2343-2348
    • Shpilka, T.1    Mizushima, N.2    Elazar, Z.3
  • 94
    • 79959950861 scopus 로고    scopus 로고
    • Dissecting the involvement of LC3B and GATE-16 in p62 recruitment into autophagosomes
    • Shvets, E., Abada, A., Weidberg, H. and Elazar, Z. (2011). Dissecting the involvement of LC3B and GATE-16 in p62 recruitment into autophagosomes. Autophagy 7, 683-688.
    • (2011) Autophagy , vol.7 , pp. 683-688
    • Shvets, E.1    Abada, A.2    Weidberg, H.3    Elazar, Z.4
  • 95
    • 52649121942 scopus 로고    scopus 로고
    • The N-terminus and Phe52 residue of LC3 recruit p62/SQSTM1 into autophagosomes
    • Shvets, E., Fass, E., Scherz-Shouval, R. and Elazar, Z. (2008). The N-terminus and Phe52 residue of LC3 recruit p62/SQSTM1 into autophagosomes. J. Cell Sci. 121, 2685-2695.
    • (2008) J. Cell Sci , vol.121 , pp. 2685-2695
    • Shvets, E.1    Fass, E.2    Scherz-Shouval, R.3    Elazar, Z.4
  • 96
    • 59649087451 scopus 로고    scopus 로고
    • Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling
    • Stehmeier, P. and Muller, S. (2009). Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling. Mol. Cell 33, 400-409.
    • (2009) Mol. Cell , vol.33 , pp. 400-409
    • Stehmeier, P.1    Muller, S.2
  • 98
    • 77956924900 scopus 로고    scopus 로고
    • Selective transport of alpha-mannosidase by autophagic pathways: identification of a novel receptor, Atg34p
    • Suzuki, K., Kondo, C., Morimoto, M. and Ohsumi, Y. (2010). Selective transport of alpha-mannosidase by autophagic pathways: identification of a novel receptor, Atg34p. J. Biol. Chem. 285, 30019-30025.
    • (2010) J. Biol. Chem. , vol.285 , pp. 30019-30025
    • Suzuki, K.1    Kondo, C.2    Morimoto, M.3    Ohsumi, Y.4
  • 99
    • 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 MAPLC3
    • Tanida, I., Tanida-Miyake, E., Ueno, T. and 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 MAPLC3. 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
  • 100
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston, T. L., Ryzhakov, G., Bloor, S., von Muhlinen, N. and Randow, F. (2009). The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat. Immunol. 10, 1215-1221.
    • (2009) Nat. Immunol , vol.10 , pp. 1215-1221
    • Thurston, T.L.1    Ryzhakov, G.2    Bloor, S.3    von Muhlinen, N.4    Randow, F.5
  • 101
    • 84857071710 scopus 로고    scopus 로고
    • Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
    • Thurston, T. L., Wandel, M. P., von Muhlinen, N., Foeglein, A. and Randow, F. (2012). Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion. Nature 482, 414-418.
    • (2012) Nature , vol.482 , pp. 414-418
    • Thurston, T.L.1    Wandel, M.P.2    von Muhlinen, N.3    Foeglein, A.4    Randow, F.5
  • 102
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada, M. and 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
  • 103
    • 84867103427 scopus 로고    scopus 로고
    • Autophagy receptors link myosin VI to autophagosomes to mediate Tom1-dependent autophagosome maturation and fusion with the lysosome
    • Tumbarello, D. A., Waxse, B. J., Arden, S. D., Bright, N. A., Kendrick-Jones, J. and Buss, F. (2012). Autophagy receptors link myosin VI to autophagosomes to mediate Tom1-dependent autophagosome maturation and fusion with the lysosome. Nat. Cell Biol. 14, 1024-1035.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 1024-1035
    • Tumbarello, D.A.1    Waxse, B.J.2    Arden, S.D.3    Bright, N.A.4    Kendrick-Jones, J.5    Buss, F.6
  • 106
    • 77954604855 scopus 로고    scopus 로고
    • J domain co-chaperone specificity defines the role of BiP during protein translocation
    • Vembar, S. S., Jonikas, M. C., Hendershot, L. M., Weissman, J. S. and Brodsky, J. L. (2010). J domain co-chaperone specificity defines the role of BiP during protein translocation. J. Biol. Chem. 285, 22484-22494.
    • (2010) J. Biol. Chem. , vol.285 , pp. 22484-22494
    • Vembar, S.S.1    Jonikas, M.C.2    Hendershot, L.M.3    Weissman, J.S.4    Brodsky, J.L.5
  • 110
    • 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. and 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
  • 112
    • 67349216078 scopus 로고    scopus 로고
    • Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover
    • Waters, S., Marchbank, K., Solomon, E., Whitehouse, C. and Gautel, M. (2009). Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover. FEBS Lett. 583, 1846-1852.
    • (2009) FEBS Lett , vol.583 , pp. 1846-1852
    • Waters, S.1    Marchbank, K.2    Solomon, E.3    Whitehouse, C.4    Gautel, M.5
  • 113
    • 79954544250 scopus 로고    scopus 로고
    • LC3 and GATE-16 N termini mediate membrane fusion processes required for autophagosome biogenesis
    • Weidberg, H., Shpilka, T., Shvets, E., Abada, A., Shimron, F. and Elazar, Z. (2011). LC3 and GATE-16 N termini mediate membrane fusion processes required for autophagosome biogenesis. Dev. Cell 20, 444-454.
    • (2011) Dev. Cell , vol.20 , pp. 444-454
    • Weidberg, H.1    Shpilka, T.2    Shvets, E.3    Abada, A.4    Shimron, F.5    Elazar, Z.6
  • 114
    • 77953122645 scopus 로고    scopus 로고
    • LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis
    • Weidberg, H., Shvets, E., Shpilka, T., Shimron, F., Shinder, V. and Elazar, Z. (2010). LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis. EMBO J. 29, 1792-1802.
    • (2010) EMBO J , vol.29 , pp. 1792-1802
    • Weidberg, H.1    Shvets, E.2    Shpilka, T.3    Shimron, F.4    Shinder, V.5    Elazar, Z.6
  • 116
    • 79953226634 scopus 로고    scopus 로고
    • Microtubule-associated protein 1S (MAP1S) bridges autophagic components with microtubules and mitochondria to affect autophagosomal biogenesis and degradation
    • Xie, R., Nguyen, S., McKeehan, K., Wang, F., McKeehan, W. L. and Liu, L. (2011). Microtubule-associated protein 1S (MAP1S) bridges autophagic components with microtubules and mitochondria to affect autophagosomal biogenesis and degradation. J. Biol. Chem. 286, 10367-10377.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10367-10377
    • Xie, R.1    Nguyen, S.2    McKeehan, K.3    Wang, F.4    McKeehan, W.L.5    Liu, L.6
  • 117
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: core machinery and adaptations
    • Xie, Z. and Klionsky, D. J. (2007). Autophagosome formation: core machinery and adaptations. Nat. Cell Biol. 9, 1102-1109.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 118
    • 0035874881 scopus 로고    scopus 로고
    • Cloning, expression patterns, and chromosome localization of three human and two mouse homologues of GABA(A) receptor-associated protein
    • Xin, Y., Yu, L., Chen, Z., Zheng, L., Fu, Q., Jiang, J., Zhang, P., Gong, R. and Zhao, S. (2001). Cloning, expression patterns, and chromosome localization of three human and two mouse homologues of GABA(A) receptor-associated protein. Genomics 74, 408-413.
    • (2001) Genomics , vol.74 , pp. 408-413
    • Xin, Y.1    Yu, L.2    Chen, Z.3    Zheng, L.4    Fu, Q.5    Jiang, J.6    Zhang, P.7    Gong, R.8    Zhao, S.9
  • 119
    • 77956499358 scopus 로고    scopus 로고
    • Autophagy-related protein 8 (Atg8) family interacting motif in Atg3 mediates the Atg3-Atg8 interaction and is crucial for the cytoplasm-tovacuole targeting pathway
    • Yamaguchi, M., Noda, N. N., Nakatogawa, H., Kumeta, H., Ohsumi, Y. and Inagaki, F. (2010). Autophagy-related protein 8 (Atg8) family interacting motif in Atg3 mediates the Atg3-Atg8 interaction and is crucial for the cytoplasm-tovacuole targeting pathway. J. Biol. Chem. 285, 29599-29607.
    • (2010) J. Biol. Chem. , vol.285 , pp. 29599-29607
    • Yamaguchi, M.1    Noda, N.N.2    Nakatogawa, H.3    Kumeta, H.4    Ohsumi, Y.5    Inagaki, F.6
  • 120
    • 0142039039 scopus 로고    scopus 로고
    • The carboxyl terminal 17 amino acids within Apg7 are essential for Apg8 lipidation, but not for Apg12 conjugation
    • Yamazaki-Sato, H., Tanida, I., Ueno, T. and Kominami, E. (2003). The carboxyl terminal 17 amino acids within Apg7 are essential for Apg8 lipidation, but not for Apg12 conjugation. FEBS Lett. 551, 71-77.
    • (2003) FEBS Lett , vol.551 , pp. 71-77
    • Yamazaki-Sato, H.1    Tanida, I.2    Ueno, T.3    Kominami, E.4
  • 121
    • 84860203624 scopus 로고    scopus 로고
    • Function and molecular mechanism of acetylation in autophagy regulation
    • Yi, C., Ma, M., Ran, L., Zheng, J., Tong, J., Zhu, J., Ma, C., Sun, Y., Zhang, S., Feng, W. et al. (2012). Function and molecular mechanism of acetylation in autophagy regulation. Science 336, 474-477.
    • (2012) Science , vol.336 , pp. 474-477
    • Yi, C.1    Ma, M.2    Ran, L.3    Zheng, J.4    Tong, J.5    Zhu, J.6    Ma, C.7    Sun, Y.8    Zhang, S.9    Feng, W.10
  • 123
    • 84876488298 scopus 로고    scopus 로고
    • Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy machinery
    • Lee, D. Y., Arnott, D. and Brown, E. J. (2013). Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy machinery. EMBO Rep. 14, 373-381.
    • (2013) EMBO Rep , vol.14 , pp. 373-381
    • Lee, D.Y.1    Arnott, D.2    Brown, E.J.3
  • 124
    • 74049126112 scopus 로고    scopus 로고
    • The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway
    • Zheng, Y. T., Shahnazari, S., Brech, A., Lamark, T., Johansen, T. and Brumell, J. H. (2009). The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway. J. Immunol. 183, 5909-5916.
    • (2009) J. Immunol. , vol.183 , pp. 5909-5916
    • Zheng, Y.T.1    Shahnazari, S.2    Brech, A.3    Lamark, T.4    Johansen, T.5    Brumell, J.H.6


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