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Autophagy-related protein 8 (Autophagy-related ubiquitin-like modifier ATG8) (Cytoplasm to vacuole targeting protein 5)

 ATG8_YEAST              Reviewed;         117 AA.
P38182; D6VPS5;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
25-OCT-2017, entry version 163.
RecName: Full=Autophagy-related protein 8;
AltName: Full=Autophagy-related ubiquitin-like modifier ATG8;
AltName: Full=Cytoplasm to vacuole targeting protein 5;
Flags: Precursor;
Name=ATG8; Synonyms=APG8, AUT7, CVT5; OrderedLocusNames=YBL078C;
ORFNames=YBL0732;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7502586; DOI=10.1002/yea.320111112;
Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
"Sequence analysis of a 78.6 kb segment of the left end of
Saccharomyces cerevisiae chromosome II.";
Yeast 11:1103-1112(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
FUNCTION.
PubMed=8224160; DOI=10.1016/0014-5793(93)80398-E;
Tsukada M., Ohsumi Y.;
"Isolation and characterization of autophagy-defective mutants of
Saccharomyces cerevisiae.";
FEBS Lett. 333:169-174(1993).
[6]
FUNCTION.
PubMed=7593182; DOI=10.1083/jcb.131.3.591;
Harding T.M., Morano K.A., Scott S.V., Klionsky D.J.;
"Isolation and characterization of yeast mutants in the cytoplasm to
vacuole protein targeting pathway.";
J. Cell Biol. 131:591-602(1995).
[7]
FUNCTION, INTERACTION WITH ATG4, AND SUBCELLULAR LOCATION.
PubMed=9649430; DOI=10.1093/emboj/17.13.3597;
Lang T., Schaeffeler E., Bernreuther D., Bredschneider M., Wolf D.H.,
Thumm M.;
"Aut2p and Aut7p, two novel microtubule-associated proteins are
essential for delivery of autophagic vesicles to the vacuole.";
EMBO J. 17:3597-3607(1998).
[8]
FUNCTION.
PubMed=10525546; DOI=10.1083/jcb.147.2.435;
Kirisako T., Baba M., Ishihara N., Miyazawa K., Ohsumi M.,
Yoshimori T., Noda T., Ohsumi Y.;
"Formation process of autophagosome is traced with Apg8/Aut7p in
yeast.";
J. Cell Biol. 147:435-446(1999).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10681575; DOI=10.1074/jbc.275.8.5845;
Huang W.-P., Scott S.V., Kim J., Klionsky D.J.;
"The itinerary of a vesicle component, Aut7p/Cvt5p, terminates in the
yeast vacuole via the autophagy/Cvt pathways.";
J. Biol. Chem. 275:5845-5851(2000).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BET1 AND NYV1.
PubMed=10837468; DOI=10.1074/jbc.M000917200;
Legesse-Miller A., Sagiv Y., Glozman R., Elazar Z.;
"Aut7p, a soluble autophagic factor, participates in multiple membrane
trafficking processes.";
J. Biol. Chem. 275:32966-32973(2000).
[11]
FUNCTION, CLEAVAGE BY ATG4, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
GLY-116 AND ARG-117.
PubMed=11038174; DOI=10.1083/jcb.151.2.263;
Kirisako T., Ichimura Y., Okada H., Kabeya Y., Mizushima N.,
Yoshimori T., Ohsumi M., Takao T., Noda T., Ohsumi Y.;
"The reversible modification regulates the membrane-binding state of
Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole
targeting pathway.";
J. Cell Biol. 151:263-276(2000).
[12]
FUNCTION, INTERACTION WITH ATG3 AND ATG7, AND LIPIDATION AT GLY-116.
PubMed=11100732; DOI=10.1038/35044114;
Ichimura Y., Kirisako T., Takao T., Satomi Y., Shimonishi Y.,
Ishihara N., Mizushima N., Tanida I., Kominami E., Ohsumi M., Noda T.,
Ohsumi Y.;
"A ubiquitin-like system mediates protein lipidation.";
Nature 408:488-492(2000).
[13]
SUBCELLULAR LOCATION.
PubMed=11689437; DOI=10.1093/emboj/20.21.5971;
Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., Ohsumi Y.;
"The pre-autophagosomal structure organized by concerted functions of
APG genes is essential for autophagosome formation.";
EMBO J. 20:5971-5981(2001).
[14]
INTERACTION WITH ATG7.
PubMed=11139573; DOI=10.1074/jbc.M007737200;
Komatsu M., Tanida I., Ueno T., Ohsumi M., Ohsumi Y., Kominami E.;
"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).
[15]
FUNCTION, CLEAVAGE BY ATG4, AND SUBCELLULAR LOCATION.
PubMed=11149920; DOI=10.1083/jcb.152.1.51;
Kim J., Huang W.-P., Klionsky D.J.;
"Membrane recruitment of Aut7p in the autophagy and cytoplasm to
vacuole targeting pathways requires Aut1p, Aut2p, and the autophagy
conjugation complex.";
J. Cell Biol. 152:51-64(2001).
[16]
INTERACTION WITH ATG19.
PubMed=12479808; DOI=10.1016/S1534-5807(02)00373-8;
Shintani T., Huang W.-P., Stromhaug P.E., Klionsky D.J.;
"Mechanism of cargo selection in the cytoplasm to vacuole targeting
pathway.";
Dev. Cell 3:825-837(2002).
[17]
SUBCELLULAR LOCATION, AND INTERACTION WITH ATG12 AND ATG19.
PubMed=11675395; DOI=10.1074/jbc.M109134200;
Kim J., Huang W.-P., Stromhaug P.E., Klionsky D.J.;
"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).
[18]
NOMENCLATURE.
PubMed=14536056; DOI=10.1016/S1534-5807(03)00296-X;
Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M.,
Ohsumi Y.;
"A unified nomenclature for yeast autophagy-related genes.";
Dev. Cell 5:539-545(2003).
[19]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[20]
CONJUGATION TO PHOSPHATIDYLETHANOLAMINE, AND SUBCELLULAR LOCATION.
PubMed=15194695; DOI=10.1074/jbc.M401066200;
Meiling-Wesse K., Barth H., Voss C., Eskelinen E.-L., Epple U.D.,
Thumm M.;
"Atg21 is required for effective recruitment of Atg8 to the
preautophagosomal structure during the Cvt pathway.";
J. Biol. Chem. 279:37741-37750(2004).
[21]
CONJUGATION TO PHOSPHATIDYLETHANOLAMINE.
PubMed=15277523; DOI=10.1074/jbc.M405860200;
Ichimura Y., Imamura Y., Emoto K., Umeda M., Noda T., Ohsumi Y.;
"In vivo and in vitro reconstitution of atg8 conjugation essential for
autophagy.";
J. Biol. Chem. 279:40584-40592(2004).
[22]
INTERACTION WITH ATG3, AND CONJUGATION TO PHOSPHATIDYLETHANOLAMINE.
PubMed=20615880; DOI=10.1074/jbc.M110.113670;
Yamaguchi M., Noda N.N., Nakatogawa H., Kumeta H., Ohsumi Y.,
Inagaki F.;
"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).
[23]
SUBCELLULAR LOCATION.
PubMed=15155809; DOI=10.1091/mbc.E04-02-0147;
Stromhaug P.E., Reggiori F., Guan J., Wang C.-W., Klionsky D.J.;
"Atg21 is a phosphoinositide binding protein required for efficient
lipidation and localization of Atg8 during uptake of aminopeptidase I
by selective autophagy.";
Mol. Biol. Cell 15:3553-3566(2004).
[24]
SUBCELLULAR LOCATION.
PubMed=15449304; DOI=10.1002/yea.1152;
Suzuki K., Noda T., Ohsumi Y.;
"Interrelationships among Atg proteins during autophagy in
Saccharomyces cerevisiae.";
Yeast 21:1057-1065(2004).
[25]
SUBCELLULAR LOCATION.
PubMed=16079147; DOI=10.1074/jbc.M501701200;
Meiling-Wesse K., Epple U.D., Krick R., Barth H., Appelles A.,
Voss C., Eskelinen E.L., Thumm M.;
"Trs85 (Gsg1), a component of the TRAPP complexes, is required for the
organization of the preautophagosomal structure during selective
autophagy via the Cvt pathway.";
J. Biol. Chem. 280:33669-33678(2005).
[26]
SUBCELLULAR LOCATION.
PubMed=15659643; DOI=10.1091/mbc.E04-11-1035;
Yorimitsu T., Klionsky D.J.;
"Atg11 links cargo to the vesicle-forming machinery in the cytoplasm
to vacuole targeting pathway.";
Mol. Biol. Cell 16:1593-1605(2005).
[27]
SUBCELLULAR LOCATION.
PubMed=16221887; DOI=10.1091/mbc.E05-07-0629;
Reggiori F., Monastyrska I., Shintani T., Klionsky D.J.;
"The actin cytoskeleton is required for selective types of autophagy,
but not nonspecific autophagy, in the yeast Saccharomyces
cerevisiae.";
Mol. Biol. Cell 16:5843-5856(2005).
[28]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG4, CLEAVAGE BY
ATG4, AND MUTAGENESIS OF TYR-49; LEU-50; PHE-77 AND PHE-79.
PubMed=16680092; DOI=10.1038/sj.embor.7400698;
Amar N., Lustig G., Ichimura Y., Ohsumi Y., Elazar Z.;
"Two newly identified sites in the ubiquitin-like protein Atg8 are
essential for autophagy.";
EMBO Rep. 7:635-642(2006).
[29]
FUNCTION.
PubMed=17132049; DOI=10.1371/journal.pbio.0040423;
Bernales S., McDonald K.L., Walter P.;
"Autophagy counterbalances endoplasmic reticulum expansion during the
unfolded protein response.";
PLoS Biol. 4:E423-E423(2006).
[30]
FUNCTION.
PubMed=17404498; DOI=10.4161/auto.4127;
Zhang Y., Qi H., Taylor R., Xu W., Liu L.F., Jin S.;
"The role of autophagy in mitochondria maintenance: characterization
of mitochondrial functions in autophagy-deficient S. cerevisiae
strains.";
Autophagy 3:337-346(2007).
[31]
FUNCTION.
PubMed=17700056; DOI=10.4161/auto.4784;
Ma J., Jin R., Dobry C.J., Lawson S.K., Kumar A.;
"Overexpression of autophagy-related genes inhibits yeast filamentous
growth.";
Autophagy 3:604-609(2007).
[32]
CONJUGATION TO PHOSPHATIDYLETHANOLAMINE, FUNCTION OF THE ATG8-PE
CONJUGATE, AND SUBUNIT.
PubMed=17632063; DOI=10.1016/j.cell.2007.05.021;
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).
[33]
SUBCELLULAR LOCATION.
PubMed=17295840; DOI=10.1111/j.1365-2443.2007.01050.x;
Suzuki K., Kubota Y., Sekito T., Ohsumi Y.;
"Hierarchy of Atg proteins in pre-autophagosomal structure
organization.";
Genes Cells 12:209-218(2007).
[34]
CONJUGATION TO PHOSPHATIDYLETHANOLAMINE.
PubMed=17699586; DOI=10.1091/mbc.E07-05-0485;
Yorimitsu T., Zaman S., Broach J.R., Klionsky D.J.;
"Protein kinase A and Sch9 cooperatively regulate induction of
autophagy in Saccharomyces cerevisiae.";
Mol. Biol. Cell 18:4180-4189(2007).
[35]
SUBCELLULAR LOCATION.
PubMed=18625846; DOI=10.1083/jcb.200711112;
Geng J., Baba M., Nair U., Klionsky D.J.;
"Quantitative analysis of autophagy-related protein stoichiometry by
fluorescence microscopy.";
J. Cell Biol. 182:129-140(2008).
[36]
CONJUGATION TO PHOSPHATIDYLETHANOLAMINE.
PubMed=18725539; DOI=10.1083/jcb.200801035;
Cao Y., Cheong H., Song H., Klionsky D.J.;
"In vivo reconstitution of autophagy in Saccharomyces cerevisiae.";
J. Cell Biol. 182:703-713(2008).
[37]
SUBCELLULAR LOCATION.
PubMed=18077553; DOI=10.1091/mbc.E07-08-0826;
Cheong H., Nair U., Geng J., Klionsky D.J.;
"The Atg1 kinase complex is involved in the regulation of protein
recruitment to initiate sequestering vesicle formation for nonspecific
autophagy in Saccharomyces cerevisiae.";
Mol. Biol. Cell 19:668-681(2008).
[38]
FUNCTION.
PubMed=18508918; DOI=10.1091/mbc.E07-12-1292;
Xie Z., Nair U., Klionsky D.J.;
"Atg8 controls phagophore expansion during autophagosome formation.";
Mol. Biol. Cell 19:3290-3298(2008).
[39]
SUBCELLULAR LOCATION.
PubMed=19088501; DOI=10.4161/auto.5.2.7201;
Xie Z., Nair U., Geng J., Szefler M.B., Rothman E.D., Klionsky D.J.;
"Indirect estimation of the area density of Atg8 on the phagophore.";
Autophagy 5:217-220(2009).
[40]
FUNCTION, INTERACTION WITH ATG19, AND MUTAGENESIS OF ARG-28; LYS-48;
TYR-49; LEU-50 AND LEU-55.
PubMed=19398890; DOI=10.4161/auto.5.4.7696;
Ho K.H., Chang H.E., Huang W.P.;
"Mutation at the cargo-receptor binding site of Atg8 also affects its
general autophagy regulation function.";
Autophagy 5:461-471(2009).
[41]
INTERACTION WITH ATG32.
PubMed=19619494; DOI=10.1016/j.devcel.2009.06.013;
Okamoto K., Kondo-Okamoto N., Ohsumi Y.;
"Mitochondria-anchored receptor Atg32 mediates degradation of
mitochondria via selective autophagy.";
Dev. Cell 17:87-97(2009).
[42]
INTERACTION WITH ATG3, AND CONJUGATION TO PHOSPHATIDYLETHANOLAMINE.
PubMed=19285500; DOI=10.1016/j.febslet.2009.03.009;
Hanada T., Satomi Y., Takao T., Ohsumi Y.;
"The amino-terminal region of Atg3 is essential for association with
phosphatidylethanolamine in Atg8 lipidation.";
FEBS Lett. 583:1078-1083(2009).
[43]
INDUCTION.
PubMed=20952643; DOI=10.1128/AEM.01535-10;
Mendes-Ferreira A., Sampaio-Marques B., Barbosa C., Rodrigues F.,
Costa V., Mendes-Faia A., Ludovico P., Leao C.;
"Accumulation of non-superoxide anion reactive oxygen species mediates
nitrogen-limited alcoholic fermentation by Saccharomyces cerevisiae.";
Appl. Environ. Microbiol. 76:7918-7924(2010).
[44]
SUBCELLULAR LOCATION.
PubMed=20154084; DOI=10.1074/jbc.M109.080374;
Nair U., Cao Y., Xie Z., Klionsky D.J.;
"Roles of the lipid-binding motifs of Atg18 and Atg21 in the cytoplasm
to vacuole targeting pathway and autophagy.";
J. Biol. Chem. 285:11476-11488(2010).
[45]
INTERACTION WITH ATG34.
PubMed=20639194; DOI=10.1074/jbc.M110.143511;
Suzuki K., Kondo C., Morimoto M., Ohsumi Y.;
"Selective transport of alpha-mannosidase by autophagic pathways:
identification of a novel receptor, Atg34p.";
J. Biol. Chem. 285:30019-30025(2010).
[46]
SUBCELLULAR LOCATION.
PubMed=20065092; DOI=10.1083/jcb.200904075;
Yen W.L., Shintani T., Nair U., Cao Y., Richardson B.C., Li Z.,
Hughson F.M., Baba M., Klionsky D.J.;
"The conserved oligomeric Golgi complex is involved in double-membrane
vesicle formation during autophagy.";
J. Cell Biol. 188:101-114(2010).
[47]
FUNCTION, AND INTERACTION WITH SHP1.
PubMed=20855502; DOI=10.1083/jcb.201002075;
Krick R., Bremer S., Welter E., Schlotterhose P., Muehe Y.,
Eskelinen E.L., Thumm M.;
"Cdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert
with ubiquitin-like Atg8.";
J. Cell Biol. 190:965-973(2010).
[48]
SUBCELLULAR LOCATION.
PubMed=20855505; DOI=10.1083/jcb.200912089;
Mari M., Griffith J., Rieter E., Krishnappa L., Klionsky D.J.,
Reggiori F.;
"An Atg9-containing compartment that functions in the early steps of
autophagosome biogenesis.";
J. Cell Biol. 190:1005-1022(2010).
[49]
SUBCELLULAR LOCATION.
PubMed=22144692; DOI=10.1083/jcb.201106098;
Bruns C., McCaffery J.M., Curwin A.J., Duran J.M., Malhotra V.;
"Biogenesis of a novel compartment for autophagosome-mediated
unconventional protein secretion.";
J. Cell Biol. 195:979-992(2011).
[50]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21429936; DOI=10.1242/jcs.076406;
Mendl N., Occhipinti A., Muller M., Wild P., Dikic I., Reichert A.S.;
"Mitophagy in yeast is independent of mitochondrial fission and
requires the stress response gene WHI2.";
J. Cell Sci. 124:1339-1350(2011).
[51]
ATG8-PE DECONJUGATION.
PubMed=22240591; DOI=10.4161/auto.8.2.18373;
Nakatogawa H., Ishii J., Asai E., Ohsumi Y.;
"Atg4 recycles inappropriately lipidated Atg8 to promote autophagosome
biogenesis.";
Autophagy 8:177-186(2012).
[52]
FUNCTION OF ATG8-PE DECONJUGATION.
PubMed=22622160; DOI=10.4161/auto.19385;
Nair U., Yen W.L., Mari M., Cao Y., Xie Z., Baba M., Reggiori F.,
Klionsky D.J.;
"A role for Atg8-PE deconjugation in autophagosome biogenesis.";
Autophagy 8:780-793(2012).
[53]
ATG8-PE DECONJUGATION.
PubMed=22652539; DOI=10.4161/auto.19652;
Yu Z.Q., Ni T., Hong B., Wang H.Y., Jiang F.J., Zou S., Chen Y.,
Zheng X.L., Klionsky D.J., Liang Y., Xie Z.;
"Dual roles of Atg8-PE deconjugation by Atg4 in autophagy.";
Autophagy 8:883-892(2012).
[54]
INTERACTION WITH ATG1.
PubMed=22885598; DOI=10.1038/emboj.2012.225;
Kraft C., Kijanska M., Kalie E., Siergiejuk E., Lee S.S.,
Semplicio G., Stoffel I., Brezovich A., Verma M., Hansmann I.,
Ammerer G., Hofmann K., Tooze S., Peter M.;
"Binding of the Atg1/ULK1 kinase to the ubiquitin-like protein Atg8
regulates autophagy.";
EMBO J. 31:3691-3703(2012).
[55]
CONJUGATION TO PHOSPHATIDYLETHANOLAMINE.
PubMed=23064152; DOI=10.1038/emboj.2012.278;
Romanov J., Walczak M., Ibiricu I., Schuchner S., Ogris E., Kraft C.,
Martens S.;
"Mechanism and functions of membrane binding by the Atg5-Atg12/Atg16
complex during autophagosome formation.";
EMBO J. 31:4304-4317(2012).
[56]
FUNCTION.
PubMed=22768199; DOI=10.1371/journal.pone.0040013;
Mijaljica D., Prescott M., Devenish R.J.;
"A late form of nucleophagy in Saccharomyces cerevisiae.";
PLoS ONE 7:E40013-E40013(2012).
[57]
INTERACTION WITH ATG1.
PubMed=22778255; DOI=10.1074/jbc.C112.387514;
Nakatogawa H., Ohbayashi S., Sakoh-Nakatogawa M., Kakuta S.,
Suzuki S.W., Kirisako H., Kondo-Kakuta C., Noda N.N., Yamamoto H.,
Ohsumi Y.;
"The autophagy-related protein kinase Atg1 interacts with the
ubiquitin-like protein Atg8 via the Atg8 family interacting motif to
facilitate autophagosome formation.";
J. Biol. Chem. 287:28503-28507(2012).
[58]
INDUCTION.
PubMed=22733735; DOI=10.1073/pnas.1200313109;
Bartholomew C.R., Suzuki T., Du Z., Backues S.K., Jin M.,
Lynch-Day M.A., Umekawa M., Kamath A., Zhao M., Xie Z., Inoki K.,
Klionsky D.J.;
"Ume6 transcription factor is part of a signaling cascade that
regulates autophagy.";
Proc. Natl. Acad. Sci. U.S.A. 109:11206-11210(2012).
[59]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[60]
INTERACTION WITH ATG3, AND CONJUGATION TO PHOSPHATIDYLETHANOLAMINE.
PubMed=22539722; DOI=10.1126/science.1216990;
Yi C., Ma M., Ran L., Zheng J., Tong J., Zhu J., Ma C., Sun Y.,
Zhang S., Feng W., Zhu L., Le Y., Gong X., Yan X., Hong B.,
Jiang F.J., Xie Z., Miao D., Deng H., Yu L.;
"Function and molecular mechanism of acetylation in autophagy
regulation.";
Science 336:474-477(2012).
[61]
SUBCELLULAR LOCATION.
PubMed=23549786; DOI=10.1242/jcs.122960;
Suzuki K., Akioka M., Kondo-Kakuta C., Yamamoto H., Ohsumi Y.;
"Fine mapping of autophagy-related proteins during autophagosome
formation in Saccharomyces cerevisiae.";
J. Cell Sci. 126:2534-2544(2013).
[62]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), INTERACTION WITH ATG19, AND
MUTAGENESIS OF ARG-28; PRO-52 AND ARG-67.
PubMed=19021777; DOI=10.1111/j.1365-2443.2008.01238.x;
Noda N.N., Kumeta H., Nakatogawa H., Satoo K., Adachi W., Ishii J.,
Fujioka Y., Ohsumi Y., Inagaki F.;
"Structural basis of target recognition by Atg8/LC3 during selective
autophagy.";
Genes Cells 13:1211-1218(2008).
[63]
STRUCTURE BY NMR OF MUTANT PRO-26, MUTAGENESIS OF LYS-26, AND
CONJUGATION TO PHOSPHATIDYLETHANOLAMINE.
PubMed=20428927; DOI=10.1007/s10858-010-9420-1;
Kumeta H., Watanabe M., Nakatogawa H., Yamaguchi M., Ogura K.,
Adachi W., Fujioka Y., Noda N.N., Ohsumi Y., Inagaki F.;
"The NMR structure of the autophagy-related protein Atg8.";
J. Biomol. NMR 47:237-241(2010).
[64]
STRUCTURE BY NMR.
PubMed=20382112; DOI=10.1016/j.bbrc.2010.04.043;
Schwarten M., Stoldt M., Mohrluder J., Willbold D.;
"Solution structure of Atg8 reveals conformational polymorphism of the
N-terminal domain.";
Biochem. Biophys. Res. Commun. 395:426-431(2010).
[65]
STRUCTURE BY NMR, AND X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX
WITH ATG7.
PubMed=22055191; DOI=10.1016/j.molcel.2011.08.035;
Noda N.N., Satoo K., Fujioka Y., Kumeta H., Ogura K., Nakatogawa H.,
Ohsumi Y., Inagaki F.;
"Structural basis of Atg8 activation by a homodimeric E1, Atg7.";
Mol. Cell 44:462-475(2011).
[66]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH ATG7.
PubMed=22056771; DOI=10.1038/nsmb.2165;
Hong S.B., Kim B.W., Lee K.E., Kim S.W., Jeon H., Kim J., Song H.K.;
"Insights into noncanonical E1 enzyme activation from the structure of
autophagic E1 Atg7 with Atg8.";
Nat. Struct. Mol. Biol. 18:1323-1330(2011).
[67]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=22308029; DOI=10.1074/jbc.M111.299917;
Kondo-Okamoto N., Noda N.N., Suzuki S.W., Nakatogawa H., Takahashi I.,
Matsunami M., Hashimoto A., Inagaki F., Ohsumi Y., Okamoto K.;
"Autophagy-related protein 32 acts as autophagic degron and directly
initiates mitophagy.";
J. Biol. Chem. 287:10631-10638(2012).
-!- FUNCTION: Ubiquitin-like modifier involved in cytoplasm to vacuole
transport (Cvt) vesicles and autophagosomes formation. With ATG4,
mediates the delivery of the vesicles and autophagosomes to the
vacuole via the microtubule cytoskeleton. Required for selective
autophagic degradation of the nucleus (nucleophagy) as well as for
mitophagy which contributes to regulate mitochondrial quantity and
quality by eliminating the mitochondria to a basal level to
fulfill cellular energy requirements and preventing excess ROS
production. Participates also in membrane fusion events that take
place in the early secretory pathway. Also involved in endoplasmic
reticulum-specific autophagic process and is essential for the
survival of cells subjected to severe ER stress. The ATG8-PE
conjugate mediates tethering between adjacent membranes and
stimulates membrane hemifusion, leading to expansion of the
autophagosomal membrane during autophagy. Moreover not only
conjugation, but also subsequent ATG8-PE deconjugation is an
important step required to facilitate multiple events during
macroautophagy, and especially for efficient autophagosome
biogenesis, the assembly of ATG9-containing tubulovesicular
clusters into phagophores/autophagosomes, and for the disassembly
of PAS-associated ATG components. Plays also a role in regulation
of filamentous growth. {ECO:0000269|PubMed:10525546,
ECO:0000269|PubMed:10681575, ECO:0000269|PubMed:10837468,
ECO:0000269|PubMed:11038174, ECO:0000269|PubMed:11100732,
ECO:0000269|PubMed:11149920, ECO:0000269|PubMed:16680092,
ECO:0000269|PubMed:17132049, ECO:0000269|PubMed:17404498,
ECO:0000269|PubMed:17632063, ECO:0000269|PubMed:17700056,
ECO:0000269|PubMed:18508918, ECO:0000269|PubMed:19398890,
ECO:0000269|PubMed:20855502, ECO:0000269|PubMed:21429936,
ECO:0000269|PubMed:22622160, ECO:0000269|PubMed:22768199,
ECO:0000269|PubMed:7593182, ECO:0000269|PubMed:8224160,
ECO:0000269|PubMed:9649430}.
-!- SUBUNIT: Conjugation to phosphatidylethanolamine (PE) leads to
homodimerization. Interacts with ATG1, ATG3, ATG4, ATG7, ATG12,
ATG32, ATG34 and the C-terminal 10 residues domain of ATG19.
Interacts also with the endoplasmic reticulum to Golgi v-SNARE
protein BET1 and the vacuolar v-SNARE protein NYV1. Interacts with
the UBX domain-containing protein SHP1.
{ECO:0000269|PubMed:10837468, ECO:0000269|PubMed:11100732,
ECO:0000269|PubMed:11139573, ECO:0000269|PubMed:11675395,
ECO:0000269|PubMed:12479808, ECO:0000269|PubMed:16680092,
ECO:0000269|PubMed:17632063, ECO:0000269|PubMed:19021777,
ECO:0000269|PubMed:19285500, ECO:0000269|PubMed:19398890,
ECO:0000269|PubMed:19619494, ECO:0000269|PubMed:20615880,
ECO:0000269|PubMed:20639194, ECO:0000269|PubMed:20855502,
ECO:0000269|PubMed:22055191, ECO:0000269|PubMed:22056771,
ECO:0000269|PubMed:22539722, ECO:0000269|PubMed:22778255,
ECO:0000269|PubMed:22885598, ECO:0000269|PubMed:9649430}.
-!- INTERACTION:
P53104:ATG1; NbExp=3; IntAct=EBI-2684, EBI-2657;
P35193:ATG19; NbExp=5; IntAct=EBI-2684, EBI-29291;
P40344:ATG3; NbExp=9; IntAct=EBI-2684, EBI-3381;
Q12292:ATG34; NbExp=4; IntAct=EBI-2684, EBI-36362;
Q06159:ATG39; NbExp=3; IntAct=EBI-2684, EBI-33888;
P53867:ATG4; NbExp=3; IntAct=EBI-2684, EBI-29160;
Q99325:ATG40; NbExp=3; IntAct=EBI-2684, EBI-3681992;
P38862:ATG7; NbExp=12; IntAct=EBI-2684, EBI-2677;
P22804:BET1; NbExp=2; IntAct=EBI-2684, EBI-3550;
Q08412:CUE5; NbExp=4; IntAct=EBI-2684, EBI-37580;
Q14596:NBR1 (xeno); NbExp=7; IntAct=EBI-2684, EBI-742698;
Q13501:SQSTM1 (xeno); NbExp=3; IntAct=EBI-2684, EBI-307104;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, cvt vesicle membrane;
Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane; Lipid-
anchor. Vacuole membrane; Lipid-anchor. Note=Membrane-associated
through a lipid anchor. This association needs the 2 ubiquitin-
like systems required for cytoplasm to vacuole transport and
autophagy. ATG18 and ATG21 facilitate the recruitment of ATG8-PE
to the site of autophagosome formation and protect it from
premature cleavage by ATG4. Localizes to both the isolation
membrane (IM) and the vacuole-isolation membrane contact site
(VICS) during IM expansion. The IM is a membrane sac generated
from the pre-autophagosomal structure that ultimately expands to
become a mature autophagosome. Upon starvation, is also recruited
to into unique membrane structures near SEC13-containing ER exit
sites which lack components of the Golgi apparatus and the
endosomes, and which were called a compartments for unconventional
protein secretion (CUPS).
-!- INDUCTION: Up-regulated upon starvation conditions. Expression is
under the control of UME6 which acts along with a histone
deacetylase complex including SIN3 and RPD3 to regulate negatively
ATG8 levels and subsequent autophagic activity.
{ECO:0000269|PubMed:20952643, ECO:0000269|PubMed:22733735}.
-!- PTM: The C-terminal Arg-117 residue of ATG8 is removed by ATG4 to
expose Gly-116 at the C-terminus. This Gly-116 forms then a
thioester bond with the 'Cys-507' of ATG7 (E1-like activating
enzyme) before being transferred to the 'Cys-234' of ATG3 (the
specific E2 conjugating enzyme), in order to be finally amidated
with phosphatidylethanolamine. This lipid modification anchors
ATG8 to membranes and can be reversed by ATG4, releasing soluble
ATG8. {ECO:0000269|PubMed:11100732}.
-!- MISCELLANEOUS: Present with 2010 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X79489; CAA56032.1; -; Genomic_DNA.
EMBL; Z35839; CAA84899.1; -; Genomic_DNA.
EMBL; AY692870; AAT92889.1; -; Genomic_DNA.
EMBL; BK006936; DAA07045.1; -; Genomic_DNA.
PIR; S45432; S45432.
RefSeq; NP_009475.1; NM_001178318.1.
PDB; 2KQ7; NMR; -; A=1-117.
PDB; 2KWC; NMR; -; A=1-116.
PDB; 2LI5; NMR; -; A=1-116.
PDB; 2ZPN; X-ray; 2.70 A; A/B/C/D=1-116.
PDB; 3RUI; X-ray; 1.91 A; B=1-116.
PDB; 3VH3; X-ray; 2.00 A; B=1-116.
PDB; 3VH4; X-ray; 2.65 A; B=1-116.
PDB; 3VXW; X-ray; 3.00 A; A=1-116.
PDBsum; 2KQ7; -.
PDBsum; 2KWC; -.
PDBsum; 2LI5; -.
PDBsum; 2ZPN; -.
PDBsum; 3RUI; -.
PDBsum; 3VH3; -.
PDBsum; 3VH4; -.
PDBsum; 3VXW; -.
ProteinModelPortal; P38182; -.
SMR; P38182; -.
BioGrid; 32625; 279.
DIP; DIP-1197N; -.
ELM; P38182; -.
IntAct; P38182; 23.
MINT; MINT-391771; -.
STRING; 4932.YBL078C; -.
MaxQB; P38182; -.
PRIDE; P38182; -.
EnsemblFungi; YBL078C; YBL078C; YBL078C.
GeneID; 852200; -.
KEGG; sce:YBL078C; -.
EuPathDB; FungiDB:YBL078C; -.
SGD; S000000174; ATG8.
GeneTree; ENSGT00390000012937; -.
HOGENOM; HOG000232034; -.
InParanoid; P38182; -.
KO; K08341; -.
OMA; RVPVICE; -.
OrthoDB; EOG092C5HB8; -.
BioCyc; YEAST:G3O-28969-MONOMER; -.
Reactome; R-SCE-1632852; Macroautophagy.
Reactome; R-SCE-8854214; TBC/RABGAPs.
EvolutionaryTrace; P38182; -.
PMAP-CutDB; P38182; -.
PRO; PR:P38182; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0033110; C:Cvt vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0000407; C:pre-autophagosomal structure; IDA:SGD.
GO; GO:0008429; F:phosphatidylethanolamine binding; IMP:SGD.
GO; GO:0031386; F:protein tag; IMP:SGD.
GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
GO; GO:0006914; P:autophagy; IMP:UniProtKB.
GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
GO; GO:0034629; P:cellular protein complex localization; IMP:SGD.
GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:SGD.
GO; GO:0044805; P:late nucleophagy; IMP:SGD.
GO; GO:0061025; P:membrane fusion; IDA:SGD.
GO; GO:0034727; P:piecemeal microautophagy of nucleus; IMP:SGD.
GO; GO:0032258; P:protein localization by the Cvt pathway; IMP:SGD.
GO; GO:0071211; P:protein targeting to vacuole involved in autophagy; IMP:SGD.
GO; GO:0016241; P:regulation of macroautophagy; IMP:SGD.
GO; GO:0061709; P:reticulophagy; IMP:SGD.
CDD; cd01611; GABARAP; 1.
InterPro; IPR004241; Atg8-like.
InterPro; IPR029071; Ubiquitin-rel_dom.
PANTHER; PTHR10969; PTHR10969; 1.
Pfam; PF02991; Atg8; 1.
SUPFAM; SSF54236; SSF54236; 1.
1: Evidence at protein level;
3D-structure; Autophagy; Complete proteome; Cytoplasmic vesicle;
Lipoprotein; Membrane; Protein transport; Reference proteome;
Transport; Ubl conjugation pathway; Vacuole.
CHAIN 1 116 Autophagy-related protein 8.
/FTId=PRO_0000017242.
PROPEP 117 117 Removed in mature form.
/FTId=PRO_0000017243.
SITE 116 117 Cleavage; by ATG4.
LIPID 116 116 Phosphatidylethanolamine amidated
glycine. {ECO:0000269|PubMed:11100732}.
MUTAGEN 26 26 K->P: No effect on autophagic activity.
{ECO:0000269|PubMed:20428927}.
MUTAGEN 28 28 R->D: Impairs ATG19-binding and
autophagic activity.
{ECO:0000269|PubMed:19021777,
ECO:0000269|PubMed:19398890}.
MUTAGEN 48 48 K->E: Impairs autophagic activity.
{ECO:0000269|PubMed:19398890}.
MUTAGEN 49 49 Y->A: Impairs ATG19-binding, PE-
conjugation, and autophagic activity.
{ECO:0000269|PubMed:16680092,
ECO:0000269|PubMed:19398890}.
MUTAGEN 50 50 L->A: Impairs ATG19-binding and
autophagic activity.
{ECO:0000269|PubMed:16680092,
ECO:0000269|PubMed:19398890}.
MUTAGEN 52 52 P->A: Significantly decreases ATG19-
binding and autophagic activity.
{ECO:0000269|PubMed:19021777}.
MUTAGEN 55 55 L->A: Impairs autophagic activity.
{ECO:0000269|PubMed:19398890}.
MUTAGEN 67 67 R->A: Significantly decreases ATG19-
binding and autophagic activity.
{ECO:0000269|PubMed:19021777}.
MUTAGEN 77 77 F->A: Impairs interaction with ATG4,
cleavage by ATG4, PAS localization, and
autophagic activity; when associated with
A-79. {ECO:0000269|PubMed:16680092}.
MUTAGEN 79 79 F->A: Impairs interaction with ATG4,
cleavage by ATG4, PAS localization, and
autophagic activity; when associated with
A-77. {ECO:0000269|PubMed:16680092}.
MUTAGEN 116 116 G->A: No cleaving of the C-terminal R-117
by ATG4. Defect in Cvt pathway and
autophagy. {ECO:0000269|PubMed:11038174}.
MUTAGEN 117 117 R->M: Normal processing after G-116 by
ATG4. {ECO:0000269|PubMed:11038174}.
HELIX 6 8 {ECO:0000244|PDB:3VH3}.
HELIX 11 24 {ECO:0000244|PDB:3RUI}.
STRAND 26 35 {ECO:0000244|PDB:3RUI}.
STRAND 37 39 {ECO:0000244|PDB:2KWC}.
STRAND 48 52 {ECO:0000244|PDB:3RUI}.
HELIX 57 67 {ECO:0000244|PDB:3RUI}.
STRAND 76 80 {ECO:0000244|PDB:3RUI}.
STRAND 87 90 {ECO:0000244|PDB:2KWC}.
HELIX 91 98 {ECO:0000244|PDB:3RUI}.
STRAND 105 111 {ECO:0000244|PDB:3RUI}.
SEQUENCE 117 AA; 13627 MW; 1246CEFF5A038819 CRC64;
MKSTFKSEYP FEKRKAESER IADRFKNRIP VICEKAEKSD IPEIDKRKYL VPADLTVGQF
VYVIRKRIML PPEKAIFIFV NDTLPPTAAL MSAIYQEHKD KDGFLYVTYS GENTFGR


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