메뉴 건너뛰기




Volumn 19, Issue 12, 2012, Pages 1250-1256

Noncanonical recognition and UBL loading of distinct E2s by autophagy-essential Atg7

Author keywords

[No Author keywords available]

Indexed keywords

UBIQUITIN;

EID: 84870834728     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2451     Document Type: Article
Times cited : (52)

References (36)
  • 2
    • 67649467294 scopus 로고    scopus 로고
    • Dynamics and diversity in autophagy mechanisms: Lessons from yeast
    • Nakatogawa, H., Suzuki, K., Kamada, Y. & Ohsumi, Y. Dynamics and diversity in autophagy mechanisms: lessons from yeast. Nat. Rev. Mol. Cell Biol. 10, 458-467 (2009).
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 458-467
    • Nakatogawa, H.1    Suzuki, K.2    Kamada, Y.3    Ohsumi, Y.4
  • 3
    • 65249111528 scopus 로고    scopus 로고
    • ATG systems from the protein structural point of view
    • Noda, N.N., Ohsumi, Y. & Inagaki, F. ATG systems from the protein structural point of view. Chem. Rev. 109, 1587-1598 (2009).
    • (2009) Chem. Rev. , vol.109 , pp. 1587-1598
    • Noda, N.N.1    Ohsumi, Y.2    Inagaki, F.3
  • 4
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: The apex for downstream signaling pathways
    • Schulman, B.A. & Harper, J.W. Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signaling pathways. Nat. Rev. Mol. Cell Biol. 10, 319-331 (2009).
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 319-331
    • Schulman, B.A.1    Harper, J.W.2
  • 5
    • 0034707036 scopus 로고    scopus 로고
    • A ubiquitin-like system mediates protein lipidation
    • Ichimura, Y. et al. A ubiquitin-like system mediates protein lipidation. Nature 408, 488-492 (2000).
    • (2000) Nature , vol.408 , pp. 488-492
    • Ichimura, Y.1
  • 6
    • 0032563798 scopus 로고    scopus 로고
    • A protein conjugation system essential for autophagy
    • Mizushima, N. et al. A protein conjugation system essential for autophagy. Nature 395, 395-398 (1998).
    • (1998) Nature , vol.395 , pp. 395-398
    • Mizushima, N.1
  • 7
    • 80555144181 scopus 로고    scopus 로고
    • Structural basis of Atg8 activation by a homodimeric E1 Atg7
    • Noda, N.N. et al. Structural basis of Atg8 activation by a homodimeric E1, Atg7. Mol. Cell 44, 462-475 (2011).
    • (2011) Mol. Cell , vol.44 , pp. 462-475
    • Noda, N.N.1
  • 8
    • 80555144189 scopus 로고    scopus 로고
    • Atg8 transfer from Atg7 to Atg3: A distinctive E1-E2 architecture and mechanism in the autophagy pathway
    • Taherbhoy, A.M. et al. Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and mechanism in the autophagy pathway. Mol. Cell 44, 451-461 (2011).
    • (2011) Mol. Cell , vol.44 , pp. 451-461
    • Taherbhoy, A.M.1
  • 9
    • 82955247613 scopus 로고    scopus 로고
    • Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8
    • Hong, S.B. et al. Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8. Nat. Struct. Mol. Biol. 18, 1323-1330 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1323-1330
    • Hong, S.B.1
  • 10
    • 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. et al. 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).
    • (2001) J. Biol. Chem. , vol.276 , pp. 9846-9854
    • Komatsu, M.1
  • 11
    • 84857472969 scopus 로고    scopus 로고
    • Trans mechanism for ubiquitin-like protein transfer in autophagy
    • Taherbhoy, A.M., Kaiser, S.E. & Schulman, B.A. Trans mechanism for ubiquitin-like protein transfer in autophagy. Cell Cycle 11, 635-636 (2012).
    • (2012) Cell Cycle , vol.11 , pp. 635-636
    • Taherbhoy, A.M.1    Kaiser, S.E.2    Schulman, B.A.3
  • 12
    • 34247237202 scopus 로고    scopus 로고
    • The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation
    • Yamada, Y. et al. The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation. J. Biol. Chem. 282, 8036-8043 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 8036-8043
    • Yamada, Y.1
  • 13
    • 84863519526 scopus 로고    scopus 로고
    • Structural insights into atg10-mediated formation of the autophagy-essential atg12-atg5 conjugate
    • Yamaguchi, M. et al. Structural insights into atg10-mediated formation of the autophagy-essential atg12-atg5 conjugate. Structure 20, 1244-1254 (2012).
    • (2012) Structure , vol.20 , pp. 1244-1254
    • Yamaguchi, M.1
  • 14
    • 13244249669 scopus 로고    scopus 로고
    • Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1
    • Huang, D.T. et al. Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1. Mol. Cell 17, 341-350 (2005).
    • (2005) Mol. Cell , vol.17 , pp. 341-350
    • Huang, D.T.1
  • 15
    • 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-to-vacuole targeting pathway
    • Yamaguchi, M. et al. Autophagy-related protein 8 (Atg8) family interacting motif in Atg3 mediates the Atg3-Atg8 interaction and is crucial for the cytoplasm-to-vacuole targeting pathway. J. Biol. Chem. 285, 29599-29607 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 29599-29607
    • Yamaguchi, M.1
  • 16
    • 38349152489 scopus 로고    scopus 로고
    • In vitro reconstitution of plant Atg8 and Atg12 conjugation systems essential for autophagy
    • Fujioka, Y. et al. In vitro reconstitution of plant Atg8 and Atg12 conjugation systems essential for autophagy. J. Biol. Chem. 283, 1921-1928 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 1921-1928
    • Fujioka, Y.1
  • 17
    • 77955637249 scopus 로고    scopus 로고
    • ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death
    • Radoshevich, L. et al. ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death. Cell 142, 590-600 (2010).
    • (2010) Cell , vol.142 , pp. 590-600
    • Radoshevich, L.1
  • 18
    • 77950484269 scopus 로고    scopus 로고
    • Atg8-family interacting motif crucial for selective autophagy
    • Noda, N.N., Ohsumi, Y. & Inagaki, F. Atg8-family interacting motif crucial for selective autophagy. FEBS Lett. 584, 1379-1385 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 1379-1385
    • Noda, N.N.1    Ohsumi, Y.2    Inagaki, F.3
  • 19
    • 47549092694 scopus 로고    scopus 로고
    • Atg8 controls phagophore expansion during autophagosome formation
    • Xie, Z., Nair, U. & Klionsky, D.J. Atg8 controls phagophore expansion during autophagosome formation. Mol. Biol. Cell 19, 3290-3298 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3290-3298
    • Xie, Z.1    Nair, U.2    Klionsky, D.J.3
  • 20
    • 34447099450 scopus 로고    scopus 로고
    • Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion
    • Nakatogawa, H., Ichimura, Y. & Ohsumi, Y. Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion. Cell 130, 165-178 (2007).
    • (2007) Cell , vol.130 , pp. 165-178
    • Nakatogawa, H.1    Ichimura, Y.2    Ohsumi, Y.3
  • 21
    • 33646204392 scopus 로고    scopus 로고
    • Generation of cell lines with tetracycline-regulated autophagy and a role for autophagy in controlling cell size
    • Hosokawa, N., Hara, Y. & Mizushima, N. Generation of cell lines with tetracycline-regulated autophagy and a role for autophagy in controlling cell size. FEBS Lett. 580, 2623-2629 (2006).
    • (2006) FEBS Lett. , vol.580 , pp. 2623-2629
    • Hosokawa, N.1    Hara, Y.2    Mizushima, N.3
  • 22
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • Hanada, T. et al. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J. Biol. Chem. 282, 37298-37302 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 37298-37302
    • Hanada, T.1
  • 23
    • 61549135769 scopus 로고    scopus 로고
    • Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method
    • Kobashigawa, Y., Kumeta, H., Ogura, K. & Inagaki, F. Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method. J. Biomol. NMR 43, 145-150 (2009).
    • (2009) J. Biomol. NMR , vol.43 , pp. 145-150
    • Kobashigawa, Y.1    Kumeta, H.2    Ogura, K.3    Inagaki, F.4
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. & Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025 (1997).
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 26
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M.D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D Biol. Crystallogr. 67, 235-242 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 27
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 29
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 31
  • 33
    • 0032701984 scopus 로고    scopus 로고
    • Formation process of autophagosome is traced with Apg8/Aut7p in yeast
    • Kirisako, T. et al. Formation process of autophagosome is traced with Apg8/Aut7p in yeast. J. Cell Biol. 147, 435-446 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 435-446
    • Kirisako, T.1
  • 34
    • 14744268915 scopus 로고    scopus 로고
    • Processing of ATG8s, ubiquitin-like proteins, and their deconjugation by ATG4s are essential for plant autophagy
    • Yoshimoto, K. et al. Processing of ATG8s, ubiquitin-like proteins, and their deconjugation by ATG4s are essential for plant autophagy. Plant Cell 16, 2967-2983 (2004).
    • (2004) Plant Cell , vol.16 , pp. 2967-2983
    • Yoshimoto, K.1
  • 35
    • 33644590635 scopus 로고    scopus 로고
    • The crystal structure of plant ATG12 and its biological implication in autophagy
    • Suzuki, N.N., Yoshimoto, K., Fujioka, Y., Ohsumi, Y. & Inagaki, F. The crystal structure of plant ATG12 and its biological implication in autophagy. Autophagy 1, 119-126 (2005).
    • (2005) Autophagy , vol.1 , pp. 119-126
    • Suzuki, N.N.1    Yoshimoto, K.2    Fujioka, Y.3    Ohsumi, Y.4    Inagaki, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.