ライフサイエンスコーパス: ATG12

1 ed lifespan phenocopying deletion of Atg7 or Atg12.

2 helix on a surface area that is exclusive to ATG12.

3 cape senescence express a high level of ATG5/ATG12.

4 Atg12, but NLRX1 did not associate with Atg5-Atg12.

5 aliana with a focus on the two loci encoding ATG12.

6 autophagy pathway genes LC3, Gabarapl1, and Atg12.

7 bind to promoter sequences of Gabarapl1 and Atg12.

8 We also found that the number of Atg12/16L1-positive puncta and recruitment of the Atg12-

9 ncta, and interacted with Atg5 and also with Atg12-5 conjugate.

10 -binding subclass responsible for localizing ATG12-5-16 L1 and driving ATG8 lipidation, whilst WIPI3

11 terface reduces or blocks the recruitment of ATG12-5-16 L1 and the conjugation of the ATG8 protein LC

12 The ATG12-5-16L1 complex is responsible for conjugating memb

13 Recruitment of the autophagy-associated Atg12-5-16L1 complex to Wipi2-positive phagophores is cr

14 some, by facilitating the recruitment of the Atg12-5-16L1 complex to Wipi2-positive phagophores.

15 /16L1-positive puncta and recruitment of the Atg12-5-16L1 complex to Wipi2-positive puncta are reduce

16 rane surrounding Salmonella and recruits the Atg12-5-16L1 complex, initiating LC3 conjugation, autoph

17 induced autophagy through recruitment of the Atg12-5-16L1 complex.

18 olic components requires the LC3-conjugating Atg12-5-16L1 complex.

19 ATG12-5-16L1 is recruited to the phagophore by a subset

20 The molecular mechanisms of Atg12-5-16L1 recruitment and significance of PtdIns(3)P

21 Of note, Optn was recruited to Atg12-5-16L1-positive puncta, and interacted with Atg5 a

22 tophagosome formation and recruitment to the Atg12-5-16L1-positive puncta.

23 Here we have purified the full-length human ATG12-5-ATG16L1 complex and show its essential role in L

24 knockdown of the autophagy-related gene 12 (Atg12) abolished the activation of autophagy and the inc

25 reduces acetylation of Atg5, Atg7, Atg8, and Atg12, although overexpressed p300 increases the acetyla

26 ment by ATG12 in higher eukaryotes and place ATG12 among the members of signaling ublps that bind lin

27 ATG12, an ubiquitin-like modifier required for macroauto

28 TUFM interacted with Atg5-Atg12 and Atg16L1 and has similar functions as NLRX1 by

29 tophagy by competing with ATG16 to bind ATG5/ATG12 and preventing ATG16/ATG5/ATG12 formation.

30 genes associated with tumorigenesis, such as ATG12 and XRCC4.

31 he role ubiquitin-like proteins (UBLs)-Atg5, Atg12, and Atg8-play in the formation of the double-memb

32 including MAFBx, MuRF1, p62, LC3B, Beclin1, Atg12, and Fn14.

33 agy activity and transcript levels of vps34, atg12, and gabarapl1 genes were reduced by insulin.

34 Levels of vps34, atg12, and gabarapl1 transcripts were elevated in the li

35 impaired LC3B-II conversion; reduced ATG14L, ATG12, and WIPI-1 puncta formation; and significantly de

36 ophagy-related (ATG)12 is a component of the ATG12 approximately ATG5-ATG16L1 E3 complex that promote

37 esidues whose side chains make contacts with ATG12 are important for E3 interaction as well as LC3 li

38 y proteins (i.e., Beclin-1, Atg4B, Atg5, and Atg12) are proviral factors required for translation of

39 eins including Vps34, autophagy gene (Atg)5, Atg12, Atg13, biochemical, and microscopy studies, we de

40 We found that depletion of Beclin-1, Atg12, Atg14, Atg16, or LC3 with specific small interfer

41 er with the LC3B conjugation complex of ATG5-ATG12-ATG15L1 are also critical for EBV envelope release

42 is co-localizes with autophagy factors ATG5, ATG12, ATG16L1, p62, NDP52, BECN1 and LC3, stimulation o

43 Thus, the Atg5-Atg12/Atg16L1 complex performs a pivotal, nondegradative

44 We show that the Atg5-Atg12/Atg16L1 protein complex, whose prior known functio

45 IFNgamma, via Atg5-Atg12/Atg16L1, inhibited formation of the membranous cyt

46 Rather, the lack of ATG12-ATG3 complex formation produces an expansion in mi

47 ATG12-ATG3 complex formation requires ATG7 as the E1 enz

48 Overall, these results unveil a role for ATG12-ATG3 in mitochondrial homeostasis and implicate th

49 ation by an alternative conjugation complex, ATG12-ATG3, of ESCRT protein ALIX, which acts in membran

50 how the E3-like ligaseautophagy-related 12 (ATG12)-ATG5-ATG16L1 in complex with the E2-like conjugas

51 ether, we conclude that the formation of the ATG12-ATG5 adduct is essential for ATG8-mediated autopha

52 le but is not essential for synthesizing the ATG12-ATG5 and ATG8-phosphatidylethanolamine adducts tha

53 Synthesis of the ATG12-ATG5 and ATG8-phosphatidylethanolamine adducts, wh

54 Moreover, t-TUCB restored hepatic levels of Atg12-Atg5 and LC3-II conjugates and reduced p62 express

55 show here that the subpathway that forms the ATG12-ATG5 conjugate also has an essential role in plant

56 Here we report that TECPR1 binds to the Atg12-Atg5 conjugate and phosphatidylinositol 3-phosphat

57 essential for ATG12 conjugation and that the ATG12-ATG5 conjugate is necessary to form autophagic ves

58 gle atg12a and atg12b mutants on forming the ATG12-ATG5 conjugate reveal that the ATG12b locus is mor

59 ons of membranes and liposome-binding of the Atg12-Atg5 conjugate upon addition of Atg16.

60 6 form mutually exclusive complexes with the Atg12-Atg5 conjugate, and TECPR1 binds PtdIns(3)P upon a

61 as ATG16L1 in a noncovalent complex with the ATG12-ATG5 conjugate.

62 1 binds PtdIns(3)P upon association with the Atg12-Atg5 conjugate.

63 also show that ATG8 lipidation requires the ATG12-ATG5 conjugate.

64 plants missing ATG5 or ATG7, cannot form the ATG12-ATG5 conjugate.

65 We have shown previously that the Atg12-Atg5 conjugation system, required for autophagosom

66 hat the concerted interactions among TECPR1, Atg12-Atg5, and PtdIns(3)P provide the fusion specificit

67 zation of a second ubiquitin-like conjugate, Atg12-Atg5, suggests that Atg21 may be involved in the r

68 s on the presence of Atg16, a subunit of the Atg12-Atg5-Atg16 complex acting as the E3-like enzyme in

69 l 3-kinase (PI3K complex I), Atg2-Atg18, and Atg12-Atg5-Atg16 complexes.

70 ATG5 is a key component of an E3-like ATG12-ATG5-ATG16 protein complex that catalyzes conjugat

71 n of Atg3, the E1 Atg7, and the composite E3 Atg12-Atg5-Atg16 with pathologies including cancers, inf

72 /LC3 proteins to phagophore membranes by the ATG12-ATG5-ATG16L1 (E3) complex are two critical steps i

73 At high surface density, ATG12-ATG5-ATG16L1 binding increased the curvature of th

74 lethanolamine, including Atg7, Atg3, and the Atg12-Atg5-Atg16L1 complex play crucial roles in the con

75 ese observations show how the binding of the ATG12-ATG5-ATG16L1 complex to the early phagophore rim c

76 on reaction, the three-step targeting of the ATG12-ATG5-ATG16L1 machinery establishes a high level of

77 The Atg12-Atg5/Atg16L1 complex is recruited by WIPI2b to the

78 The interaction of the Atg12~Atg5-Atg16 complex and Atg8 with Atg19 is mutually

79 The interaction of Atg19 with the Atg12~Atg5-Atg16 complex is mediated by its Atg8-interac

80 o receptors interact with the E3-like enzyme Atg12~Atg5-Atg16, which stimulates Atg8 conjugation.

81 mma against MNV in macrophages required Atg5-Atg12, Atg7, and Atg16L1, but not induction of autophagy

82 ate NRF2 activity irrespective of cell type: ATG12, ATG7, GOSR1, IFT172, NRXN2, RAB6A, VPS37A, and th

83 negative regulator of NRF2, KEAP1 Of these, ATG12, ATG7, KEAP1, and VPS37A are known to be involved

84 ATG12(Autophagy-related 12)-ATG5-ATG16L1 was up to 100-f

85 hagy-related protein 7 (Atg7), Beclin-1, and Atg12, autophagy regulatory proteins, was analyzed by we

86 proapoptotic role for the autophagic protein Atg12, based on a BH3-like domain, which enables binding

87 icated by altered expression and activity of ATG12, beclin, p62, and LC3A II, hallmarks of autophagy,

88 enic mice show lower levels of Dock180, LC3, Atg12, Becn1, Rab5 and Rubicon in Sertoli cells.

89 Here we report the identification of the ATG12 binding sequence in the flexible region of human A

90 tions of the autophagy-related proteins Atg5-Atg12, but NLRX1 did not associate with Atg5-Atg12.

91 ant increase of pro-autophagic proteins ATG5-ATG12 COMPLEX and Beclin-1.

92 its casp8 through interaction with FADD:Atg5-Atg12 complexes.

93 Protein levels of Beclin-1, Atg5-Atg12 conjugate, and LC3-II were also significantly redu

94 results indicate that ATG10 is essential for ATG12 conjugation and that the ATG12-ATG5 conjugate is n

95 7 or Atg5 or blocking LC3 lipidation or ATG5-ATG12 conjugation decreases ERK phosphorylation.

96 To characterize the ATG12 conjugation pathway specifically, we characterized

97 mitochondrial homeostasis and implicate the ATG12 conjugation system in cellular functions distinct

98 Surprisingly, disrupting ATG12 conjugation to ATG3 does not affect starvation-ind

99 DFCP1 to autophagic precursors, reduced ATG5-ATG12 conjugation, and compromised autophagosome formati

100 Here, we identify ATG3 as a substrate for ATG12 conjugation.

101 son reveals that the ATG3 binding surface on ATG12 contains a hydrophobic pocket corresponding to the

102 Unlike ATG8, ATG12 does not associate with autophagic bodies, implyin

103 Specificity of the ATG5/ATG12-E3 ligase responsible for the conjugation of LC3 i

104 to bind ATG5/ATG12 and preventing ATG16/ATG5/ATG12 formation.

105 tablish the mechanism of ATG3 recruitment by ATG12 in higher eukaryotes and place ATG12 among the mem

106 A role of ATG12 in the E3 complex is to recruit the E2 enzyme ATG3

107 Proteomic analysis of ATG12(-/-) iNeurons revealed accumulation of endoplasmic

108 The conjugation of ATG5 with ATG12 is dispensable for this interaction.

109 on of key autophagy effectors (such as ATG5, ATG12, LC3B and LAMP1) and AMPK-dependent activation of

110 lly and characterized it genetically through atg12 mutants that block ATG8 modification.

111 the E2, resulting in the covalent linkage of ATG12 onto a single lysine on ATG3.

112 Phenotypic analyses showed that atg12 plants are phenotypically normal and fertile when

113 atg12 plants have compromised autophagic transport as de

114 revealed that remobilization is impaired in atg12 plants, which significantly decreases seed yield a

115 or by depletion of the autophagy-related-12 (Atg12) protein homolog.

116 hat couple the AUTOPHAGY-RELATED8 (ATG8) and ATG12 proteins to their respective targets, phosphatidyl

117 autophagy events represented by ATG16L1 and ATG12 puncta formation.

118 Atg7 is required for the conjugation of Atg12 to Atg5, and Atg8 to phosphatidylethanolamine (PE)

119 autophagy flux and defects in conjugation of ATG12 to ATG5.

120 the two ubiquitin-fold polypeptides ATG8 and ATG12 to phosphatidylethanolamine and the ATG5 protein,

121 of two ubiquitin-like protein tags, ATG8 and ATG12, to phosphatidylethanolamine and the ATG5 protein,

122 leaves missing the core autophagy component ATG12 under normal growth conditions (e.g., lipids and s

123 jugation machinery in the SUMO, NEDD8, ATG8, ATG12, URM1, UFM1, FAT10, and ISG15 pathways while refer

124 quired to initiate ligation of both ATG8 and ATG12, we previously showed that the ATG8/12 conjugation

125 -fold proteins Autophagy-related (ATG)-8 and ATG12, which become attached to the lipid phosphatidylet

126 A key component in ATG8 function is ATG12, which promotes lipidation upon its attachment to