In molecular biology, autophagy related 3 (Atg3) is the E2 enzyme for the LC3 lipidation process.[1] It is essential for autophagy. The super protein complex, the Atg16L complex, consists of multiple Atg12-Atg5 conjugates. Atg16L has an E3-like role in the LC3 lipidation reaction. The activated intermediate, LC3-Atg3 (E2), is recruited to the site where the lipidation takes place.[2]
Atg3 catalyses the conjugation of Atg8 and phosphatidylethanolamine (PE). Atg3 has an alpha/beta-fold, and its core region is topologically similar to canonical E2 enzymes. Atg3 has two regions inserted in the core region and another with a long alpha-helicalstructure that protrudes from the core region as far as 30 A.[3] It interacts with atg8 through an intermediate thioesterbond between Cys-288 and the C-terminal Gly of atg8. It also interacts with the C-terminal region of the E1-like atg7 enzyme.
Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the lysosome/vacuole. Atg3 is a ubiquitin like modifier that is topologically similar to the canonical E2 enzyme.[4] It catalyses the conjugation of Atg8 and phosphatidylethanolamine.[5]
Atg3 consists of three domains, an N-terminal domain, a catalytic domain and a C-terminal domain. The catalytic domain contains a cysteine residue within an HPC motif, this is the putative active-site residue for recognition of the Apg5 subunit of the autophagosome complex.[6] The small C-terminal domain is likely to be a distinct binding region for the stability of the autophagosome complex.[7] It carries a highly characteristic conserved FLKF sequence motif.
Referencesedit
^Fujita N, Itoh T, Omori H, Fukuda M, Noda T, Yoshimori T (May 2008). "The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy". Mol. Biol. Cell. 19 (5): 2092–100. doi:10.1091/mbc.E07-12-1257. PMC2366860. PMID 18321988.
^Noda T, Fujita N, Yoshimori T (May 2008). "The Ubi brothers reunited". Autophagy. 4 (4): 540–1. doi:10.4161/auto.5973. PMID 18398292.
^Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F (March 2007). "The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation". J. Biol. Chem. 282 (11): 8036–43. doi:10.1074/jbc.M611473200. PMID 17227760.
^Tanida I, Tanida-Miyake E, Komatsu M, Ueno T, Kominami E (April 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 (16): 13739–44. doi:10.1074/jbc.M200385200. PMID 11825910.
^Schlumpberger M, Schaeffeler E, Straub M, Bredschneider M, Wolf DH, Thumm M (February 1997). "AUT1, a gene essential for autophagocytosis in the yeast Saccharomyces cerevisiae". J. Bacteriol. 179 (4): 1068–76. doi:10.1128/jb.179.4.1068-1076.1997. PMC178799. PMID 9023185.
^Mizushima N, Yoshimori T, Ohsumi Y (December 2002). "Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-mediated yeast two-hybrid method". FEBS Lett. 532 (3): 450–4. doi:10.1016/S0014-5793(02)03739-0. PMID 12482611. S2CID 37247321.
^Mizushima N, Yoshimori T, Ohsumi Y (May 2003). "Role of the Apg12 conjugation system in mammalian autophagy". Int. J. Biochem. Cell Biol. 35 (5): 553–61. doi:10.1016/S1357-2725(02)00343-6. PMID 12672448.
This article incorporates text from the public domain Pfam and InterPro: IPR007134
This article incorporates text from the public domain Pfam and InterPro: IPR007135
This article incorporates text from the public domain Pfam and InterPro: IPR019461
April 13, 2024
atg3, molecular, biology, autophagy, related, atg3, enzyme, lipidation, process, essential, autophagy, super, protein, complex, atg16l, complex, consists, multiple, atg12, atg5, conjugates, atg16l, like, role, lipidation, reaction, activated, intermediate, atg. In molecular biology autophagy related 3 Atg3 is the E2 enzyme for the LC3 lipidation process 1 It is essential for autophagy The super protein complex the Atg16L complex consists of multiple Atg12 Atg5 conjugates Atg16L has an E3 like role in the LC3 lipidation reaction The activated intermediate LC3 Atg3 E2 is recruited to the site where the lipidation takes place 2 Autophagocytosis associated protein N terminalIdentifiersSymbolAutophagy NPfamPF03986InterProIPR007134Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryAutophagocytosis associated protein active site domainIdentifiersSymbolAutophagy act CPfamPF03987InterProIPR007135Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryAutophagocytosis associated protein C terminalIdentifiersSymbolAutophagy CtermPfamPF10381InterProIPR019461Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryAtg3 catalyses the conjugation of Atg8 and phosphatidylethanolamine PE Atg3 has an alpha beta fold and its core region is topologically similar to canonical E2 enzymes Atg3 has two regions inserted in the core region and another with a long alpha helical structure that protrudes from the core region as far as 30 A 3 It interacts with atg8 through an intermediate thioester bond between Cys 288 and the C terminal Gly of atg8 It also interacts with the C terminal region of the E1 like atg7 enzyme Autophagocytosis is a starvation induced process responsible for transport of cytoplasmic proteins to the lysosome vacuole Atg3 is a ubiquitin like modifier that is topologically similar to the canonical E2 enzyme 4 It catalyses the conjugation of Atg8 and phosphatidylethanolamine 5 Atg3 consists of three domains an N terminal domain a catalytic domain and a C terminal domain The catalytic domain contains a cysteine residue within an HPC motif this is the putative active site residue for recognition of the Apg5 subunit of the autophagosome complex 6 The small C terminal domain is likely to be a distinct binding region for the stability of the autophagosome complex 7 It carries a highly characteristic conserved FLKF sequence motif References edit Fujita N Itoh T Omori H Fukuda M Noda T Yoshimori T May 2008 The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy Mol Biol Cell 19 5 2092 100 doi 10 1091 mbc E07 12 1257 PMC 2366860 PMID 18321988 Noda T Fujita N Yoshimori T May 2008 The Ubi brothers reunited Autophagy 4 4 540 1 doi 10 4161 auto 5973 PMID 18398292 Yamada Y Suzuki NN Hanada T Ichimura Y Kumeta H Fujioka Y Ohsumi Y Inagaki F March 2007 The crystal structure of Atg3 an autophagy related ubiquitin carrier protein E2 enzyme that mediates Atg8 lipidation J Biol Chem 282 11 8036 43 doi 10 1074 jbc M611473200 PMID 17227760 Tanida I Tanida Miyake E Komatsu M Ueno T Kominami E April 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 16 13739 44 doi 10 1074 jbc M200385200 PMID 11825910 Schlumpberger M Schaeffeler E Straub M Bredschneider M Wolf DH Thumm M February 1997 AUT1 a gene essential for autophagocytosis in the yeast Saccharomyces cerevisiae J Bacteriol 179 4 1068 76 doi 10 1128 jb 179 4 1068 1076 1997 PMC 178799 PMID 9023185 Mizushima N Yoshimori T Ohsumi Y December 2002 Mouse Apg10 as an Apg12 conjugating enzyme analysis by the conjugation mediated yeast two hybrid method FEBS Lett 532 3 450 4 doi 10 1016 S0014 5793 02 03739 0 PMID 12482611 S2CID 37247321 Mizushima N Yoshimori T Ohsumi Y May 2003 Role of the Apg12 conjugation system in mammalian autophagy Int J Biochem Cell Biol 35 5 553 61 doi 10 1016 S1357 2725 02 00343 6 PMID 12672448 This article incorporates text from the public domain Pfam and InterPro IPR007134 This article incorporates text from the public domain Pfam and InterPro IPR007135 This article incorporates text from the public domain Pfam and InterPro IPR019461 Retrieved from https en wikipedia org w index php title ATG3 amp oldid 1187755630, wikipedia, wiki, book, books, library,
