I[gt@S\[̌`ɂ^pN̍\ƕq@\

<strong>cW<sup>1</sup>E_~F<sup>2</sup></strong>
i<sup>1</sup>ww q\͕C<sup>2</sup>kCww@[Ȋw@ |XgQmZ^[j
emailF<a href="mailto:nn@bikaken.or.jp">cW</a>C<a href="mailto:finagaki@pharm.hokudai.ac.jp">_~F</a>
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̈Zr[, <strong>3</strong>, e012 (2014)@<a href="http://dx.doi.org/10.7875/leading.author.3.e012">DOI: 10.7875/leading.author.3.e012</a>
Nobuo N. Noda & Fuyuhiko Inagaki: <strong>Structure and molecular function of autophagosome-forming factors.</strong>

<a href="http://leading.lifesciencedb.jp/wordpress/wp-content/uploads/2014/11/Inagaki-3.e012-PDF.pdf" target="_blank"><img class="size-full wp-image-112 alignright" title="Download PDF" src="/images/downloadPDF.png" alt="Download PDF" width="100" height="20" /></a>
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<h2>v </h2>
@I[gt@W[ɂő̃CxgłI[gt@S\[̌`18ނ̎vAtg^pNSĂĈ5ނ̌`̎nɂAtg1̂C8ނ̐LɂĎƂċ@\Atg8nAtg12n\ĂDߔNCvAtg^pNɊւ\wIȌIɐiWC̍\Ղѕq@\̈[炩ɂȂĂD̃r[ł́CAtg1̂Atg8nAtg12nɒڂC܂ł̌ɂ薾炩ɂꂽ\Ղѕq@\ɂčŐV̒mɂƂÂƂƂɁC̉ۑɂĂӂD

<h2>͂߂</h2>
@I[gt@W[͐^jɕۑꂽזEɂ{IȕnłCVp̕⃊TCNƂčזE̍P퐫̈ێɊ^Ă<a href="#R1"><sup>1)</sup></a>DI[gt@W[ɂƂIdvȃCxǵCdȂ\̂łI[gt@S\[̌`łDI[gt@W[UƁCˑRCזEɊuƂ΂閌\oCꂪLĕ邱ƂɂI[gt@S\[V邪C̉ߒŃ^pNIKlȂǂ̑̕ΏۂI[gt@S\[̓ɊuDÂāCI[gt@S\[̓\\[iyAł́CtEjƗZCe͉yf̂͂炫ɂԑŐsɕDI[gt@W[𐧌䂷Atg^pN͂܂łɏoypē肳C̐͌_38ނɒBĂ<a href="#R2"><sup>2,3)</sup></a>D̂vAtg^pNƂăI[gt@S\[̌`Ɋ֗^̂18ނłCȉ6̋@\O[vCȂ킿C1jAtg1́C2jAtg9C3jI[gt@W[ٓIPI3ḰiPI3KFphosphatidylinositol 3-kinaseCzXt@`WCmVg[3-Li[[jC4jAtg2-Atg18́C5jAtg12nC6jAtg8nCɕނ<a href="#R3"><sup>3)</sup></a>i<a href="#F1">}1</a>jD6̋@\O[vPASipre-autophagosomal structureCvI[gt@S\[\́jɋǍ݂Cċ@\邱ƂɂI[gt@S\[̌`ЂN<a href="#R4"><sup>4)</sup></a>D̎vAtg^pNы@\O[v͐iɂčLۑĂ邱ƂCI[gt@S\[̌`̊{Iȕq@\܂iɂĕۑĂƍlD̃r[ł́CI[gt@S\[̌`ɂvAtg^pN̂CߔNC\wIȌ邵iWAtg1̂Atg8nAtg12nɂāC̍\ƕq@\ɊւŐV̒m܂Ƃ߂D

<a name="F1"></a><div id="fig1-caption-text" style="display: none;"><strong>}1@I[gt@S\[̌`ɂvAtg^pN</strong>
Atg^pN̔ԍDE1FrL`yfl̍yfCE2FrL`yfl̍yfCE3FrL`]ڍyfl̍yfCPEFzXt@`WG^m[A~D
<a href="http://leading.lifesciencedb.jp/wordpress/wp-content/uploads/2014/11/Inagaki-3.e012-Fig.1.jpg" target="_blank">[Download]</a></div>[hs_figure id=1&amp;image=/wordpress/wp-content/uploads/2014/11/Inagaki-3.e012-Fig.1.png&amp;caption=fig1-caption-text]

@ȂCoyɂI[gt@W[̌ɂẮC<a href="http://leading.lifesciencedb.jp/1-e005/" target="_blank">rؕۍOEǓT, ̈Zr[, <strong>1</strong>, e005, 2012</a>CI[gt@W[ƎƂ̂ɂẮC<a href="http://leading.lifesciencedb.jp/3-e006/" target="_blank">R rE떾, ̈Zr[, <strong>3</strong>, e006, 2014</a> QƂꂽD

<h2>1DAtg1́FI[gt@S\[`̎nu</h2>
@I[gt@W[͋Qɂ苭U邪C̍ہC܂I[gt@S\[̌`̏łPAS\z<a href="#R4"><sup>4,5)</sup></a>DPASAtg^pNWςČ`\̂ł邪CPAŜƂjAtg1̂SƍlĂ<a href="#R5"><sup>5,6)</sup></a>DȂ킿CAtg1̂PAS̍\zƂăI[gt@S\[`̎nuƂċ@\DAtg1͎vAtg^pN̂ȂŗB̃Li[[łCQ̍ۂAtg13CAtg17CAtg29CAtg31Atg1̂`<a href="#R5"><sup>5,7)</sup></a>DAtg1̂Atg9уI[gt@W[ٓIPI3K̂N[gCɂ炪Atg2-Atg18́CAtg8nCAtg12nN[g邱ƂɂPAS<a href="#R6"><sup>6)</sup></a>i<a href="#F1">}1</a>jD

<h2>2DAtg1̂̍\^pN̍\</h2>
@Atg1͍\I3̗̈CȂ킿CN[̃Li[[hCCC[̋̃hCCāC҂ȂVRϐ̈ɕi<a href="#F2">}2a</a>jDLi[[hC̗̍\͎Iɂ͂܂肳ĂȂCA~m_z̑veCLi[[X[p[t@~[ɂĕۑꂽ\Ɨ\zĂDCC[̋̃hC̍\́CAtg13Atg1̈Ƃ̂̕ƂX͂ɂ茈肳ꂽ<a href="#R8"><sup>8)</sup></a>i<a href="http://first.lifesciencedb.jp/archives/8761" target="_blank">V_r[</a> łfځjDAtg1̋̃hC23փbNXoh^fɂȂC҂݂ɖڂɑݍp邱ƂɂЂƂ̋\`ĂDꂼ3փbNXohMIThCƍ\ގ߁CN[MIT1MIT2ƖÂꂽ<a href="#R8"><sup>8)</sup></a>DMIThCMVBoHȂǖAɂ^pNɂ΂΂݂hCłC^pNǂȂW[Ƃċ@\DlɁCAtg1MIT1MIT2Atg13ёIII[gt@W[ɂAtg11Ƃ̌Ɋ֗^<a href="#R8"><sup>8,9)</sup></a>D܂CAtg1MIT1MIT2܂C[̗̈悪傫ȋȗ|\[ƌ邱Ƃ񍐂Ă<a href="#R10"><sup>10)</sup></a>DC̍\ɂ͖̋ȗF悤ȍ\Iȓ݂͂ꂸCƂ̌̋@\Ɋւڍׂ͕słDAtg1̓VRϐ͖̈300cȂCA~m_z񂩂̗̍\ƂȂƂ\DSerɕx݁Ĉ̓_邱Ƃ킩Ă邪C̈Ӌ`͕słDAtg1̓VRϐ̈ɂAtg8`[t܂܂CAtg8ƒړIɌ<a href="#R11"><sup>11,12)</sup></a>DAtg8`[tAtg1Atg8Ƃ̂̑ݍp͗҂PASւ̋Ǎ݂ɂ͕svł邪CAtg1uɋǍ݂邽߂ɕKvłDAtg1̊uւ̋Ǎ݂͌IȃI[gt@W[ɕKvł邱Ƃ킩Ă邪CAtg1uɂĒS̓Iȕq@\ɂĂ͂킩ĂȂD

<a name="F2"></a><div id="fig2-caption-text" style="display: none;"><strong>}2@Atg1̂\^pN̍\</strong>
iajAtg1̍\iPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=4p1n&PAGEID=Summary" target="_blank">4P1N</a>jDAIMFAtg8`[tD
ibjAtg13̍\iPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=4j2g&PAGEID=Summary" target="_blank">4J2G</a>jD
icjAtg17-Atg29-Atg31̂̍\iPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=4p1w&PAGEID=Summary" target="_blank">4P1W</a>jD
P̓_镔ʂD
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@Atg13͍\I2̗̈CȂ킿CN[̋̃hCC[̓VRϐ̈Ƃɕi<a href="#F2">}2b</a>jDAtg13̋hC̍\X͂ɂ茈肳ꂽ<a href="#R13"><sup>13)</sup></a>Di̕5{̃XghȂV[gƂ̕ЖʂɂȂ4{̃փbNXȂCC[3{̃XghȂV[gtꂽ\ƂDi̍̕\HORMAhCƓg|W[ƂCAtg13̋̃hCHORMAƖꂽ<a href="#R13"><sup>13)</sup></a>DAtg13HORMA̓I[gt@W[ٓIPI3K̂PASɋǍ݂邽ߕKvł邪C҂̂̒ړIȌ͊mFĂȂ<a href="#R13"><sup>13)</sup></a>DHORMAhCMad2̍\wIȌɂCMad2͊J\ƕ\2̎vȃRz[V̕tԂɂCKȟɂ肻̕t\ւƂ邱Ƃ킩Ă<a href="#R14"><sup>14)</sup></a>DAtg13HORMǍ\͕\ɗގ\Ƃ邪C܂ŁCJ\ɗގ\͕񍐂ĂȂDAtg13HORMAl̍\ω̂C܂Cڂ̌肪ł̂́CC炩ɂȂ΂ȂȂۑłDAtg13HORMAȊO̖470c͓VRϐ̈łƗ\ĂDAtg13̓VRϐ̈SerThrɕx݁C̑_邱Ƃ킩Ă<a href="#R8"><sup>8)</sup></a>D܂CVRϐ̖̈60c̗̈pAtg1ƁC13cȂZ̈pAtg17ƁCڂɌ<a href="#R8"><sup>8)</sup></a>D
@Atg17CAtg29CAtg31͉h{ɂ炸PIɈȕ̂`C<em>in vitro</em>ɂ2q̃XgCLIg[ł邱ƂĂ<a href="#R15"><sup>15)</sup></a>DAtg17-Atg29-Atg31̂̍\X͂ѓdqpPq͂ɂ茈肳ꂽ<a href="#R9"><sup>9,10,16)</sup></a>i<a href="#F2">}2c</a>jDAtg17̃vg}[4{̃փbNXȂIȎO̍\ƂCC[Ńzʑ̉邱ƂɂŜƂS̍\ƂDAtg318{̃XghȂThCb`\Ĉ1{Atg29ɗR邱ƂCAtg31̗̍\ێɂAtg29K{ƍlDThCb`\ɂ킦CAtg31C[1{̃փbNXCAtg173{̃փbNX4փbNXoh`邱ƂɂAtg17̉ʂɋłɌDAtg29N[Atg31̃ThCb`ɑgݍ܂XghCÂāC3փbNXoh\CɁCC[ɂ͓VRϐ̈DAtg29̓VRϐ̈܂SerThrɕx݁Ĉ͋QɈˑă_<a href="#R9"><sup>9)</sup></a>DAtg29̓VRϐ̈̓I[gt@W[̊ɂ͕svłCނCI[gt@W[}銈<a href="#R9"><sup>9)</sup></a>DVRϐ̈̃_ɂAtg29̑jQʂI[gt@W[iƂf񎦂Ă邪<a href="#R9"><sup>9)</sup></a>C̕q@\̏ڍׂ͕słD܂CAtg29̓VRϐ̈Atg11ƒړIɌ邪<a href="#R9"><sup>9)</sup></a>CC̈Ӌ`ɂĂ炩ɂĂKvD

<h2>3DAtg13Atg1̂̍\z̊</h2>
@Atg13̓VRϐ̈̂CAtg1Atg17Ƃ̌ɕKv\ȒZ̈ꂼp邱ƂɂCAtg1-Atg13̂Atg13-Atg17-Atg29-Atg31̂̌\肳ꂽ<a href="#R8"><sup>8)</sup></a>i<a href="#F3">}3 a,b</a>jDAtg13Atg1͓̈VRϐ̈ɑ݂CAtg1̔񑶍݉ɂĂ͓̗̍\Ȃ<a href="#R8"><sup>8)</sup></a>DAtg1Ƃ̌ɍۂCAtg1̈̓wbNX-[v-փbNX\ƂCN[̂փbNXpAtg1MIT2ƁCC[̂փbNXpAtg1MIT1ƌi<a href="#F3">}3a</a>jD̑ݍp͈ʓIMIThCMIT`[tiMIT-interacting motifFMIMjƂ̂ɂ݂鑊ݍpƗގĂƂCN[̂փbNẌMIM(N)CC[̂փbNẌMIM(C) Ɩꂽ<a href="#R8"><sup>8)</sup></a>DAtg1Atg13Ƃ̂̐ea͂MIM(N) MIT2Ƃ̂̑ݍpSCMIM(C) MIT1Ƃ̂̑ݍp͂⋭SDAtg13Atg17͓̈VRϐ̈13cɂ܂łڂĂC̒Z̈Atg17N[̕t߂ɂaƌi<a href="#F3">}3b</a>jDaIȑݍpɂ킦CAtg13Ser428Ser429Atg17Asp247Ɛf`ĂiȉCcԍ͊{Iɏoy̏ꍇjC̐fAtg13Atg17Ƃ̂̑ݍpɕK{ł<a href="#R8"><sup>8)</sup></a>D

<a name="F3"></a><div id="fig3-caption-text" style="display: none;"><strong>}3@Atg13Atg1̂̍\z̊</strong>
iajAtg1Atg13Ƃ̂̑ݍp̍\ՁiPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=4p1n&PAGEID=Summary" target="_blank">4P1N</a>jD
ibjAtg13Atg17Ƃ̂̑ݍp̍\ՁiPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=4p1w&PAGEID=Summary" target="_blank">4P1W</a>jD
icjAtg1̂̋QɈˑ`̃fDP̓_镔ʂD17BRFAtg17̈D
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<h2>4DAtg13̋QɈˑIȒE_Atg1̂̌`̋@\</h2>
@I[gt@W[͋Qɂ苭U邪C̐ɂ͉h{ZT[łTOR1Ă<a href="#R17"><sup>17)</sup></a>Dxh{ɂāCTOR1Atg13̓VRϐ̈Ɋ܂܂鑽SerThr𒼐ړIɃ_<a href="#R18"><sup>18)</sup></a>D_SerAtg1Ƃ̌ɂƂdvMIM(N) ɂ͊܂܂ꂸCݍp⋭MIM(C) ɕ݂ČʁC_Atg1Atg13Ƃ̂̐eax܂Ōコ<a href="#R8"><sup>8)</sup></a>DCAtg13Atg17̈ɂ́C_SerƂAtg17Asp247Ƃ̐fɂSer428Ser429܂܂D炪_邱Ƃɂ萅fj󂳂Cɕdׂ̔邱ƂɂCAtg13Atg17Ƃ̌͊SɎ<a href="#R8"><sup>8)</sup></a>DQɂȂTOR1̊ቺ邱ƂɂAtg13݂͂₩ɒE_CAtg1Atg17ɑ΂鍂eal邱ƂɂAtg1̂`I[gt@W[̎nɂ͂炭<a href="#R7"><sup>7,8)</sup></a>i<a href="#F3">}3c</a>jDxh{̂ƂAtg1Atg13Ƃ̂̑ݍpx܂ŕێ̂́CIII[gt@W[̈łCvtoH<a href="#R19"><sup>19)</sup></a> iނ߂ɏdvłƍlD

<h2>5DAtg8nAtg12nFI[gt@S\[`̎</h2>
@vAtg^pN18ނ̂C̔ɋ߂8ނrL`ľnłAtg8nAtg12n`<a href="#R20"><sup>20)</sup></a>i<a href="#F1">}1</a>jDrL`l^pNAtg12̓rL`yfl̍yfAtg7уrL`yfl̍yfAtg10̂͂炫ɂAtg5Lys149ƃC\yv`h`<a href="#R21"><sup>21)</sup></a>DAtg12n̓rL`]ڍyfl̍yfKvƂC܂CAtg12Atg5Ƃ̌ؒfyf݂ȂDAtg12-Atg5̂Atg16ƕ̂`C˂Atg12-Atg5-Atg16̂Ƃċ@\<a href="#R22"><sup>22)</sup></a>DЂƂ̃rL`l^pNAtg8̓rL`yfl̍yfAtg7уrL`yfl̍yfAtg3̂͂炫ɂ胊łzXt@`WG^m[A~ƃA~h`<a href="#R23"><sup>23)</sup></a>DAtg12-Atg5̂Ƃ͈قȂCAtg8-zXt@`WG^m[A~͓̂ٓIȃveA[[Atg4ɂE<a href="#R24"><sup>24)</sup></a>DAtg12-Atg5-Atg16̂Atg8ƃzXt@`WG^m[A~Ƃ̂̌𑣐i邱Ƃ<a href="#R25"><sup>25)</sup></a>CAtg8nɂ郆rL`]ڍyfl̍yfƍlĂDAtg8nAtg12nAtg^pNPASɋǍ݂ċ@\邪CAtg1̂PAS̒jƂċ@\̂ɑ΂CAtg8nAtg12nAtg^pN͎vAtg^pN̂ȂōŌPASɃN[g邱<a href="#R6"><sup>6)</sup></a>i<a href="#F1">}1</a>jCɁCL̓r̊uɂǍ݂邱Ƃ<a href="#R26"><sup>26)</sup></a>CI[gt@S\[`̎ƍlD

<h2>6DI[gt@W[ɓrL`l^pNAtg8Atg12</h2>
@Atg8͂܂܂ȎɗR̂̍\肳ĂCǂʂāCrL`iƂN[ɓI2̃փbNXȂ\ƂĂ<a href="#R27"><sup>27,28)</sup></a>i<a href="#F4">}4a</a>jDIȃփbNX݂̑́CAtg8ɌŗL2̋@\CȂ킿C̋ÏW\Atg8`[tɑ΂ٓIȔF\ĂD̋ÏW\̏ڍׂȕq@\͂܂킩ĂȂCقȂ閌ɑ݂Atg8-zXt@`WG^m[A~̂ǂݍp邱Ƃɂ薌ȂƂ߂Ƃf񎦂Ă<a href="#R29"><sup>29)</sup></a>DAtg8`[tɑ΂ٓIȔF\́CIȃփbNXƃrL`iƂ̂Ɍ`ꂽã|PbgłWʁCrL`iɌ`ꂽã|PbgłLʁC2Ԗڂ̃XghɂSĂCAtg8`[t̓T^IȔzłTrp-X-X-LeuziX͔Cӂ̃A~m_cjTrpWʂɂāCLeuLʂɂāC܂C卽2Ԗڂ̃XghqԃV[g`邱ƂɂF<a href="#R27"><sup>27,30,31)</sup></a>i<a href="#F4">}4a</a>jDAtg8`[t̓T^IȔẑCTrpTyr邢PheCLeuIle邢Valɂウ邱Ƃ킩ĂDAtg8`[t͚Mނ̃I[gt@W[֘A^pNɂĂoĂCLC3̈Ƃ΂Ă<a href="#R27"><sup>27,32)</sup></a>DAtg8`[t邢LC3̈͑III[gt@W[ɂĊ̔FS̎êɌoĂCAtg8-zXt@`WG^m[A~̂͊̔Fɂ閌ł̑Ƃċ@\<a href="#R27"><sup>27)</sup></a>DCAtg12ɂĂAtg8Ɣׂ̋@\̉𖾂͒xĂDAtg12ɂāCrL`i̍\͕ۑĂ邪<a href="#R33"><sup>33)</sup></a>CN[ɂ͎ɂ肳܂܂Ȓ̔z񂪕tC̖͂킩ĂȂDBCĂ@\̓rL`yfl̍yfAtg3̔FłCAtg12-Atg5-Atg16̂rL`]ڍyfl̍yfƂċ@\邽߂ɂ͂炭ƍlĂ<a href="#R34"><sup>34)</sup></a>DMނAtg12Atg3Ɋ܂܂̔zrL`iɂF邪<a href="#R35"><sup>35)</sup></a>i<a href="#F4">}4b</a>jC̑ݍp͍yɂĂ͕ۑĂ炸CȂ͂KvłD

<a name="F4"></a><div id="fig4-caption-text" style="display: none;"><strong>}4@Atg8Atg12̍\</strong>
iajAtg8Atg19ɗRAtg8`[tƂ̂̍̕\iPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=2zpn&PAGEID=Summary" target="_blank">2ZPN</a>jDIWF̐̍㑤N[ɓI2̃փbNXCErL`iɑD2F2Ԗڂ̃XghD
ibjqgAtg12Atg3ɗRyv`hƂ̂̍̕\iPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=4naw&PAGEID=Summary" target="_blank">4NAW</a>jD
<a href="http://leading.lifesciencedb.jp/wordpress/wp-content/uploads/2014/11/Inagaki-3.e012-Fig.4.jpg" target="_blank">[Download]</a></div>[hs_figure id=4&amp;image=/wordpress/wp-content/uploads/2014/11/Inagaki-3.e012-Fig.4.png&amp;caption=fig4-caption-text]


<h2>7DEyfAtg4̍\Ɗ̔̋@\</h2>
@Atg4Atg4-Atg8̂̍\wIȌ́CMނAtg4I[\OłAtg4BAtg8I[\OłLC3pčsꂽ<a href="#R36"><sup>36-38)</sup></a>DAtg4͖|̂̂Atg8̃vZVOAtg8-zXt@`WG^m[A~̂̒E̗SVXeCveA[[łCppCƗގ\DP̂Atg4͊ʂ𐧌䃋[vCTrpiqgAtg4B̏ꍇCTrp142jCN[eCɂ莩ȑjQ\ƂDAtg8ƂɑK͂ȍ\ωNCAtg8C[GlyAtg4̊Cys̋ߖTɌi<a href="#F5">}5</a>jDAtg8t@~[C[ɖFA~m_c-GlyzۑĂC̔zAtg4̎ȑjQ̍\邽߂ɕKvł<a href="#R36"><sup>36)</sup></a>DȂ킿CȑjQ̍\Atg4̊ِSۂ@\̂ЂƂƍlDAtg4̓I[gt@S\[̌`ɋ@\ĂAtg8-zXt@`WG^m[A~̂͐ؒfȂƂĂ邪C̊̐@\ɂĂ͂킩ĂȂD

<a name="F5"></a><div id="fig5-caption-text" style="display: none;"><strong>}5@Atg4̍\Atg8̔F̃f</strong>
Atg4P̂̍\iPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=2cy7&PAGEID=Summary" target="_blank">2CY7</a>jCAtg8Ƃ̂̍̕\iPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=2zzp&PAGEID=Summary" target="_blank">2ZZP</a>jD̂̌`ɂ\ω𐶂Atg4̗̈FŁCAtg4̊Cys󃂃fŎDI[gt@W[֘AƂẮCu₻̑ÔƂȂ閌CI[gt@S\[Ȃǂ܂܂DPEFzXt@`WG^m[A~D
<a href="http://leading.lifesciencedb.jp/wordpress/wp-content/uploads/2014/11/Inagaki-3.e012-Fig.5.jpg" target="_blank">[Download]</a></div>[hs_figure id=5&amp;image=/wordpress/wp-content/uploads/2014/11/Inagaki-3.e012-Fig.5.png&amp;caption=fig5-caption-text]


<h2>8DrL`ľnǂyf̍\</h2>
@Atg8Atg12ɋʂ郆rL`yfl̍yfAtg7́CATP̃GlM[gƂɂ藼҂C[GlyCAtg7̂̊CysƂ̂Ń`IGXe`̂CAtg8Ƃ̃rL`yfl̍yfłAtg3C邢́CAtg12Ƃ̃rL`yfl̍yfłAtg10Ƃ̂Ƀ`IGXe`锽SDAtg72̋hCłN[hCC[hCZJ[łȂꂽ\<a href="#R39"><sup>39-41)</sup></a>DC[hC͂ɃAfjhCэC[hCɕCAfjhCăzʑ̂`i<a href="#F6">}6a</a>jDāCAtg7ׂ͂ẴhCъʂ2DʓIȃrL`yf̓zʑ̂`Cʂ⓯̃hC1ێȂƂƂ͑ΏƓIłDAfjhCׂ͂ẴrL`yfɂĕۑĂ̂ɑ΂CN[hCэC[hCAtg7ɌŗL̃hCłDCʓIȃrL`yfɕۑꂽCyshCуrL`lhCAtg7ɂ݂͑ȂDAtg7̊Cys̓AfjhCɑ}ꂽ[vɑ݂D

<a name="F6"></a><div id="fig6-caption-text" style="display: none;"><strong>}6@Atg^pŇ̍\</strong>
iajAtg7̍\Atg8уrL`yfl̍yf̔F̊ՁiPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=4gsl&PAGEID=Summary" target="_blank">4GSL</a>C<a href="http://service.pdbj.org/mine/Detail2?PDBID=4gsk&PAGEID=Summary" target="_blank">4GSK</a>C<a href="http://service.pdbj.org/mine/Detail2?PDBID=3vh4&PAGEID=Summary" target="_blank">3VH4</a>C<a href="http://service.pdbj.org/mine/Detail2?PDBID=2li5&PAGEID=Summary" target="_blank">2LI5</a>jDATPXeBbNfŁCCys󃂃fŎDNTDFN[hCCADFAfjhCCECTDFC[hCC15F15Ԗڂ̃XghD
ibjAtg10̍\Atg5̔F̋@\iPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=2lpu&PAGEID=Summary" target="_blank">2LPU</a>C<a href="http://service.pdbj.org/mine/Detail2?PDBID=2dyo&PAGEID=Summary" target="_blank">2DYO</a>jDCys󃂃fŎD
icjAtg3̍\iPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=2dyt&PAGEID=Summary" target="_blank">2DYT</a>jDCys󃂃fŎDHRFnḧCFRFtLVüD
idjAtg12-Atg5-Atg16̂̍\iPDB IDF<a href="http://service.pdbj.org/mine/Detail2?PDBID=3w1s&PAGEID=Summary" target="_blank">3W1S</a>C<a href="http://service.pdbj.org/mine/Detail2?PDBID=3a7p&PAGEID=Summary" target="_blank">3A7P</a>jD
<a href="http://leading.lifesciencedb.jp/wordpress/wp-content/uploads/2014/11/Inagaki-3.e012-Fig.6.jpg" target="_blank">[Download]</a></div>[hs_figure id=6&amp;image=/wordpress/wp-content/uploads/2014/11/Inagaki-3.e012-Fig.6.png&amp;caption=fig6-caption-text]

@Atg8̃rL`yfl̍yfłAtg3Atg12̃rL`yfl̍yfłAtg10́C݂ɗގrL`yf̃RA\CʓIȃrL`yfƂ͂قȂC[̃փbNX2Ă<a href="#R42"><sup>42-44)</sup></a>i<a href="#F6">}6 b,c</a>jDɂ킦CAtg10̓RA\яoIȃwAs\CpAtg12̌łAtg5𒼐ړIɔF<a href="#R43"><sup>43)</sup></a>i<a href="#F6">}6b</a>jDCAtg32̃j[Nȑ}̈łnḧ您уtLVü<a href="#R42"><sup>42)</sup></a>i<a href="#F6">}6c</a>jDnḧ̓RA\яo1{̒փbNXу[v̈悩ȂC[v̈ɂAtg8`[tɂAtg8ƒړIɌ<a href="#R45"><sup>45)</sup></a>DtLVü͖80A~m_cȂĈقƂǂVRϐԂƂ邪CBCZփbNXƂ̈悪Atg7N[hCƌ<a href="#R40"><sup>40,42)</sup></a>DAtg3N[̖20c͌ɂēdqxϑȂCA~m_z񂩂痼e}փbNX\Ƃ邱Ƃ\ĂCȗ̑傫Ȗ̔FɊ֗^邱Ƃ񍐂Ă<a href="#R46"><sup>46,47)</sup></a>D
@Atg8̃rL`]ڍyfl̍yfłAtg12-Atg5-Atg16̂́CAtg16zʑ̂`邱Ƃɂ肨̂̂̃^pN2܂ލ\Ƃ<a href="#R48"><sup>48)</sup></a>DAtg52̃rL`lhCLys149܂ރwbNXɕxރhCȂC3̃hC݂ɑݍp邱Ƃɂ1̋̍\Ƃ<a href="#R49"><sup>49)</sup></a>i<a href="#F6">}6 b,d</a>jDAtg16͕szʑ̂`RChRChCƁCAtg5Ƃ̌ɂ郿փbNXƂCtLVuȃJ[ɂȂꂽ\Ƃ<a href="#R48"><sup>48)</sup></a>i<a href="#F6">}6d</a>jDAtg12͂ɏqׂƂ胆rL`iȂCAtg5ƃC\yv`hɂȂꂽ\ɂẮC񋤗L̑ݍp`邱ƂɂAtg5̍iɌŒ肳<a href="#R50"><sup>50,51)</sup></a>i<a href="#F4">}4b</a>C<a href="#F6">}6d</a>jĎʁCAtg12-Atg5-Atg16̂̑S̍\6̃rL`lhCRChRCʑ̂̈[ɏW܂\ƂȂCق̃rL`]ڍyf̍\Ƃ͂邵قȂi<a href="#F6">}6d</a>jD

<h2>9DAtg^pŇ̕q@\</h2>
@܂CAtg7C[hCɂtLVuȗ̈Atg8⑫̂CAtg8AfjhCւƔzu<a href="#R41"><sup>41)</sup></a>i<a href="#F6">}6a</a>C<a href="#F7">}7</a>jDɁCAtg8C[GlyAtg7ɌATPƔ邱ƂŃAfjCÂāCAtg7̊CysAtg8C[Glyƃ`IGXe`D̉ߒɂāCCys܂ރ[v̈悪\ωNƂ\z邪Cق̃rL`yfɂĂ݂悤ȃhCǂ̑K͂Ȕzu]͕KvƂȂDAtg7Atg12ގ̗lŔFƎv邪CAtg7-Atg12̂̍\wIȌ͂܂łȂĂȂDAtg7ƃ`IGXe`Atg8Atg12́CÂāCꂼ̃rL`yfl̍yfłAtg3Atg10ƃ`IGXe`D̍ہCǂ̃rL`yfl̍yfAtg7N[hC15Ԗڂ̃Xgh̕t߂ɗގ̗lŌ邪i<a href="#F6">}6a</a>jCrL`lhCpʓIȃrL`yfƃrL`yfƂ̂̑ݍpƂ͂܂قȂ<a href="#R52"><sup>52,53)</sup></a>DAtg7̓zʑ̂`邽߁C2q̃rL`yfl̍yf邱Ƃ\łDāCAtg7̊CysɂȂꂽAtg8Atg12́CAtg7qɌrL`yfl̍yfƁCzʑ̂`1qAtg7ɌrL`yfl̍yf́Cǂ̊Cysɂ]ڂ\邪Cۂɂ́C҂ɂ̂ݑIIɓ]ڂ<a href="#R40"><sup>40,41)</sup></a>DAtg7-1̊CysɂȂꂽAtg8́CAtg7-2ɌAtg3ւƓ]ڂi<a href="#F6">}6a</a>C<a href="#F7">}7</a>jD́Cق̃rL`yfɂ݂͂ȂAtg7ɌŗL̋@\łCAtg7zʑ̂`闝R̂ЂƂƍlD̂ɂẮCAtg8Atg3݂̂ƁCAtg12Atg10݂̂ƃ`IGXe`ƍlĂ邪C<em>in vitro</em>ł́CAtg3Atg12ƂCAtg10Atg8Ƃ`IGXe`<a href="#R52"><sup>52)</sup></a>Dِ̖̓́CC炩ɂȂ΂ȂȂۑłD

<a name="F7"></a><div id="fig7-caption-text" style="display: none;"><strong>}7@Atg8-zXt@`WG^m[A~̂̌`̃f</strong>
C͊CysDI[gt@W[֘AƂẮCu₻̑ÔƂȂ閌CI[gt@S\[Ȃǂ܂܂D
NTDFN[hCCADFAfjhCCECTDFC[hCCPEFzXt@`WG^m[A~D
<a href="http://leading.lifesciencedb.jp/wordpress/wp-content/uploads/2014/11/Inagaki-3.e012-Fig.7.jpg" target="_blank">[Download]</a></div>[hs_figure id=7&amp;image=/wordpress/wp-content/uploads/2014/11/Inagaki-3.e012-Fig.7.png&amp;caption=fig7-caption-text]

@Atg10ƃ`IGXe`Atg12́CŌɁCAtg5Lys149ƌDAtg10͌ŗL̃wAs\pAtg5̃rL`lhCɂXghƑݍp邱ƂɂCrL`]ڍyfl̍yf̏ȂɌSƍl<a href="#R43"><sup>43)</sup></a>i<a href="#F6">}6b</a>jDCAtg3ƃ`IGXe`Atg8́CrL`]ڍyfl̍yfłAtg12-Atg5-Atg16̂̏؂邱ƂɂzXt@`WG^m[A~ƌi<a href="#F7">}7</a>jDAtg3̊ʂ̍\͒PƂł͒ኈ̏ԂłCAtg12-Atg5-Atg16̂Ƒݍp邱Ƃɂ荂̏Ԃɕϊ邱ƂwIȎ@ɂ苭Ă<a href="#R54"><sup>54)</sup></a>D܂CAtg12-Atg5-Atg16̂Atg3K؂ȖւƃN[g邱ƂɂCAtg8̌łzXt@`WG^m[A~Atg8Ƃo킹@\SƍlĂ<a href="#R34"><sup>34)</sup></a>DC̕q@\Ɋւ闝͕s\łCSẻ𖾂̂߂ɂ͂Ȃ\wIȌK{łD

<h2></h2>
@I[gt@S\[̌`ɂvAtg^pN̂CAtg1̂Atg8nAtg12nɂẮCߔNC\wIȌ}ɐiWC炪͂q@\ɂĂ̈[炩ɂꂽDȂCƂ΁CAtg17̂ƂS̍\͉Ă̂ȂǁC\킩邱Ƃɂ肳ȂƐĂD܂CAtg1̂Atg8nAtg12nƂnAtg^pN̍\wIȌ͂قƂǐiWĂȂ̂łD\wIȌƍ\p@\̌sĐi߂邱ƂCI[gt@W[ɂЂƂЂƂ𖾂Ă߂ɂ߂ďdvłD

<h2> </h2>
<ol>
<li id="R1"><span class='au'>Mizushima, N. & Komatsu, M.</span>: <span class="ti">Autophagy: renovation of cells and tissues.</span> <span class='so'>Cell, 147, 728-741 (2011)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/22078875" target="_blank">PubMed</a>]</span></li>
<li id="R2"><span class='au'>Araki, Y., Ku, W. C., Akioka, M. et al.</span>: <span class="ti">Atg38 is required for autophagy-specific phosphatidylinositol 3-kinase complex integrity.</span> <span class='so'>J. Cell Biol., 203, 299-313 (2013)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/24165940" target="_blank">PubMed</a>]</span></li>
<li id="R3"><span class='au'>Mizushima, N., Yoshimori, T. & Ohsumi, Y.</span>: <span class="ti">The role of Atg proteins in autophagosome formation.</span> <span class='so'>Annu. Rev. Cell Dev. Biol., 27, 107-132 (2011)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/21801009" target="_blank">PubMed</a>]</span></li>
<li id="R4"><span class='au'>Suzuki, K., Kirisako, T., Kamada, Y. et al.</span>: <span class="ti">The pre-autophagosomal structure organized by concerted functions of <em>APG</em> genes is essential for autophagosome formation.</span> <span class='so'>EMBO J., 20, 5971-5981 (2001)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/11689437" target="_blank">PubMed</a>]</span></li>
<li id="R5"><span class='au'>Kawamata, T., Kamada, Y., Kabeya, Y. et al.</span>: <span class="ti">Organization of the pre-autophagosomal structure responsible for autophagosome formation.</span> <span class='so'>Mol. Biol. Cell, 19, 2039-2050 (2008)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/18287526" target="_blank">PubMed</a>]</span></li>
<li id="R6"><span class='au'>Suzuki, K., Kubota, Y., Sekito, T. et al.</span>: <span class="ti">Hierarchy of Atg proteins in pre-autophagosomal structure organization.</span> <span class='so'>Genes Cells, 12, 209-218 (2007)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/17295840" target="_blank">PubMed</a>]</span></li>
<li id="R7"><span class='au'>Kamada, Y., Funakoshi, T., Shintani, T. et al.</span>: <span class="ti">Tor-mediated induction of autophagy via an Apg1 protein kinase complex.</span> <span class='so'>J. Cell Biol., 150, 1507-1513 (2000)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/10995454" target="_blank">PubMed</a>]</span></li>
<li id="R8"><span class='au'>Fujioka, Y., Suzuki, S. W., Yamamoto, H. et al.</span>: <span class="ti">Structural basis of starvation-induced assembly of the autophagy initiation complex.</span> <span class='so'>Nat. Struct. Mol. Biol., 21, 513-521 (2014)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/24793651" target="_blank">PubMed</a>] [<a href="http://first.lifesciencedb.jp/archives/8761" target="_blank">V_r[</a>]</span></li>
<li id="R9"><span class='au'>Mao, K., Chew, L. H., Inoue-Aono, Y. et al.</span>: <span class="ti">Atg29 phosphorylation regulates coordination of the Atg17-Atg31-Atg29 complex with the Atg11 scaffold during autophagy initiation.</span> <span class='so'>Proc. Natl. Acad. Sci. USA, 110, E2875-E2884 (2013)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/23858448" target="_blank">PubMed</a>]</span></li>
<li id="R10"><span class='au'>Ragusa, M. J., Stanley, R. E. & Hurley, J. H.</span>: <span class="ti">Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis.</span> <span class='so'>Cell, 151, 1501-1512 (2012)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/23219485" target="_blank">PubMed</a>]</span></li>
<li id="R11"><span class='au'>Kraft, C., Kijanska, M., Kalie, E. et al.</span>: <span class="ti">Binding of the Atg1/ULK1 kinase to the ubiquitin-like protein Atg8 regulates autophagy.</span> <span class='so'>EMBO J., 31, 3691-3703 (2012)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/22885598" target="_blank">PubMed</a>]</span></li>
<li id="R12"><span class='au'>Nakatogawa, H., Ohbayashi, S., Sakoh-Nakatogawa, M. et al.</span>: <span class="ti">The autophagy-related protein kinase Atg1 interacts with the ubiquitin-like protein Atg8 via the Atg8 family interacting motif to facilitate autophagosome formation.</span> <span class='so'>J. Biol. Chem., 287, 28503-28507 (2012)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/22778255" target="_blank">PubMed</a>]</span></li>
<li id="R13"><span class='au'>Jao, C. C., Ragusa, M. J., Stanley, R. E. et al.</span>: <span class="ti">A HORMA domain in Atg13 mediates PI 3-kinase recruitment in autophagy.</span> <span class='so'>Proc. Natl. Acad. Sci. USA, 110, 5486-5491 (2013)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/23509291" target="_blank">PubMed</a>]</span></li>
<li id="R14"><span class='au'>Luo, X. & Yu, H.</span>: <span class="ti">Protein metamorphosis: the two-state behavior of Mad2.</span> <span class='so'>Structure, 16, 1616-1625 (2008)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/19000814" target="_blank">PubMed</a>]</span></li>
<li id="R15"><span class='au'>Kabeya, Y., Noda, N. N., Fujioka, Y. et al.</span>: <span class="ti">Characterization of the Atg17-Atg29-Atg31 complex specifically required for starvation-induced autophagy in <em>Saccharomyces cerevisiae</em>.</span> <span class='so'>Biochem. Biophys. Res. Commun., 389, 612-615 (2009)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/19755117" target="_blank">PubMed</a>]</span></li>
<li id="R16"><span class='au'>Chew, L. H., Setiaputra, D., Klionsky, D. J. et al.</span>: <span class="ti">Structural characterization of the <em>Saccharomyces cerevisiae</em> autophagy regulatory complex Atg17-Atg31-Atg29.</span> <span class='so'>Autophagy, 9, 1467-1474 (2013)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/23939028" target="_blank">PubMed</a>]</span></li>
<li id="R17"><span class='au'>Noda, T. & Ohsumi, Y.</span>: <span class="ti">Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast.</span> <span class='so'>J. Biol. Chem., 273, 3963-3966 (1998)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/9461583" target="_blank">PubMed</a>]</span></li>
<li id="R18"><span class='au'>Kamada, Y., Yoshino, K., Kondo, C. et al.</span>: <span class="ti">Tor directly controls the Atg1 kinase complex to regulate autophagy.</span> <span class='so'>Mol. Cell. Biol., 30, 1049-1058 (2010)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/19995911" target="_blank">PubMed</a>]</span></li>
<li id="R19"><span class='au'>Lynch-Day, M. A. & Klionsky, D. J.</span>: <span class="ti">The Cvt pathway as a model for selective autophagy.</span> <span class='so'>FEBS Lett., 584, 1359-1366 (2010)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/20146925" target="_blank">PubMed</a>]</span></li>
<li id="R20"><span class='au'>Ohsumi, Y.</span>: <span class="ti">Molecular dissection of autophagy: two ubiquitin-like systems.</span> <span class='so'>Nat. Rev. Mol. Cell Biol., 2, 211-216 (2001)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/11265251" target="_blank">PubMed</a>]</span></li>
<li id="R21"><span class='au'>Mizushima, N., Noda, T., Yoshimori, T. et al.</span>: <span class="ti">A protein conjugation system essential for autophagy.</span> <span class='so'>Nature, 395, 395-398 (1998)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/9759731" target="_blank">PubMed</a>]</span></li>
<li id="R22"><span class='au'>Mizushima, N., Noda, T. & Ohsumi, Y.</span>: <span class="ti">Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.</span> <span class='so'>EMBO J., 18, 3888-3896 (1999)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/10406794" target="_blank">PubMed</a>]</span></li>
<li id="R23"><span class='au'>Ichimura, Y., Kirisako, T., Takao, T. et al.</span>: <span class="ti">A ubiquitin-like system mediates protein lipidation.</span> <span class='so'>Nature, 408, 488-492 (2000)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/11100732" target="_blank">PubMed</a>]</span></li>
<li id="R24"><span class='au'>Kirisako, T., Ichimura, Y., Okada, H. et al.</span>: <span class="ti">The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway.</span> <span class='so'>J. Cell Biol., 151, 263-276 (2000)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/11038174" target="_blank">PubMed</a>]</span></li>
<li id="R25"><span class='au'>Hanada, T., Noda, N. N., Satomi, Y. et al.</span>: <span class="ti">The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy.</span> <span class='so'>J. Biol. Chem., 282, 37298-37302 (2007)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/17986448" target="_blank">PubMed</a>]</span></li>
<li id="R26"><span class='au'>Suzuki, K., Akioka, M., Kondo-Kakuta, C. et al.</span>: <span class="ti">Fine mapping of autophagy-related proteins during autophagosome formation in <em>Saccharomyces cerevisiae</em>.</span> <span class='so'>J. Cell Sci., 126, 2534-2544 (2013)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/23549786" target="_blank">PubMed</a>]</span></li>
<li id="R27"><span class='au'>Noda, N. N., Ohsumi, Y. & Inagaki, F.</span>: <span class="ti">Atg8-family interacting motif crucial for selective autophagy.</span> <span class='so'>FEBS Lett., 584, 1379-1385 (2010)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/20083108" target="_blank">PubMed</a>]</span></li>
<li id="R28"><span class='au'>Sugawara, K., Suzuki, N. N., Fujioka, Y. et al.</span>: <span class="ti">The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of <em>Saccharomyces cerevisiae</em> Atg8.</span> <span class='so'>Genes Cells, 9, 611-618 (2004)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/15265004" target="_blank">PubMed</a>]</span></li>
<li id="R29"><span class='au'>Nakatogawa, H., Ichimura, Y. & Ohsumi, Y.</span>: <span class="ti">Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion.</span> <span class='so'>Cell, 130, 165-178 (2007)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/17632063" target="_blank">PubMed</a>]</span></li>
<li id="R30"><span class='au'>Noda, N. N., Kumeta, H., Nakatogawa, H. et al.</span>: <span class="ti">Structural basis of target recognition by Atg8/LC3 during selective autophagy.</span> <span class='so'>Genes Cells, 13, 1211-1218 (2008)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/19021777" target="_blank">PubMed</a>]</span></li>
<li id="R31"><span class='au'>Ichimura, Y., Kumanomidou, T., Sou, Y. S. et al.</span>: <span class="ti">Structural basis for sorting mechanism of p62 in selective autophagy.</span> <span class='so'>J. Biol. Chem., 283, 22847-22857 (2008)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/18524774" target="_blank">PubMed</a>]</span></li>
<li id="R32"><span class='au'>Pankiv, S., Clausen, T. H., Lamark, T. et al.</span>: <span class="ti">p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy.</span> <span class='so'>J. Biol. Chem., 282, 24131-24145 (2007)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/17580304" target="_blank">PubMed</a>]</span></li>
<li id="R33"><span class='au'>Suzuki, N. N., Yoshimoto, K., Fujioka, Y. et al.</span>: <span class="ti">The crystal structure of plant ATG12 and its biological implication in autophagy.</span> <span class='so'>Autophagy, 1, 119-126 (2005)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/16874047" target="_blank">PubMed</a>]</span></li>
<li id="R34"><span class='au'>Fujita, N., Itoh, T., Omori, H. et al.</span>: <span class="ti">The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy.</span> <span class='so'>Mol. Biol. Cell, 19, 2092-2100 (2008)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/18321988" target="_blank">PubMed</a>]</span></li>
<li id="R35"><span class='au'>Metlagel, Z., Otomo, C., Takaesu, G. et al.</span>: <span class="ti">Structural basis of ATG3 recognition by the autophagic ubiquitin-like protein ATG12.</span> <span class='so'>Proc. Natl. Acad. Sci. USA, 110, 18844-18849 (2013)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/24191030" target="_blank">PubMed</a>]</span></li>
<li id="R36"><span class='au'>Satoo, K., Noda, N. N., Kumeta, H. et al.</span>: <span class="ti">The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy.</span> <span class='so'>EMBO J., 28, 1341-1350 (2009)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/19322194" target="_blank">PubMed</a>]</span></li>
<li id="R37"><span class='au'>Kumanomidou, T., Mizushima, T., Komatsu, M. et al.</span>: <span class="ti">The crystal structure of human Atg4b, a processing and de-conjugating enzyme for autophagosome-forming modifiers.</span> <span class='so'>J. Mol. Biol., 355, 612-618 (2006)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/16325851" target="_blank">PubMed</a>]</span></li>
<li id="R38"><span class='au'>Sugawara, K., Suzuki, N. N., Fujioka, Y. et al.</span>: <span class="ti">Structural basis for the specificity and catalysis of human Atg4B responsible for mammalian autophagy.</span> <span class='so'>J. Biol. Chem., 280, 40058-40065 (2005)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/16183633" target="_blank">PubMed</a>]</span></li>
<li id="R39"><span class='au'>Hong, S. B., Kim, B. W., Lee, K. E. et al.</span>: <span class="ti">Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8.</span> <span class='so'>Nat. Struct. Mol. Biol., 18, 1323-1330 (2011)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/22056771" target="_blank">PubMed</a>]</span></li>
<li id="R40"><span class='au'>Taherbhoy, A. M., Tait, S. W., Kaiser, S. E. et al.</span>: <span class="ti">Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and mechanism in the autophagy pathway.</span> <span class='so'>Mol. Cell, 44, 451-461 (2011)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/22055190" target="_blank">PubMed</a>]</span></li>
<li id="R41"><span class='au'>Noda, N. N., Satoo, K., Fujioka, Y. et al.</span>: <span class="ti">Structural basis of Atg8 activation by a homodimeric E1, Atg7.</span> <span class='so'>Mol. Cell, 44, 462-475 (2011)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/22055191" target="_blank">PubMed</a>] [<a href="http://first.lifesciencedb.jp/archives/3954" target="_blank">V_r[</a>]</span></li>
<li id="R42"><span class='au'>Yamada, Y., Suzuki, N. N., Hanada, T. et al.</span>: <span class="ti">The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation.</span> <span class='so'>J. Biol. Chem., 282, 8036-8043 (2007)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/17227760" target="_blank">PubMed</a>]</span></li>
<li id="R43"><span class='au'>Yamaguchi, M., Noda, N. N., Yamamoto, H. et al.</span>: <span class="ti">Structural insights into Atg10-mediated formation of the autophagy-essential Atg12-Atg5 conjugate.</span> <span class='so'>Structure, 20, 1244-1254 (2012)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/22682742" target="_blank">PubMed</a>]</span></li>
<li id="R44"><span class='au'>Hong, S. B., Kim, B. W., Kim, J. H. et al.</span>: <span class="ti">Structure of the autophagic E2 enzyme Atg10.</span> <span class='so'>Acta Crystallogr. D. Biol. Crystallogr., 68, 1409-1417 (2012)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/22993095" target="_blank">PubMed</a>]</span></li>
<li id="R45"><span class='au'>Yamaguchi, M., Noda, N. N., Nakatogawa, H. et al.</span>: <span class="ti">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.</span> <span class='so'>J. Biol. Chem., 285, 29599-29607 (2010)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/20615880" target="_blank">PubMed</a>]</span></li>
<li id="R46"><span class='au'>Nath, S., Dancourt, J., Shteyn, V. et al.</span>: <span class="ti">Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3.</span> <span class='so'>Nat. Cell Biol., 16, 415-424 (2014)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/24747438" target="_blank">PubMed</a>]</span></li>
<li id="R47"><span class='au'>Hanada, T., Satomi, Y., Takao, T. et al.</span>: <span class="ti">The amino-terminal region of Atg3 is essential for association with phosphatidylethanolamine in Atg8 lipidation.</span> <span class='so'>FEBS Lett., 583, 1078-1083 (2009)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/19285500" target="_blank">PubMed</a>]</span></li>
<li id="R48"><span class='au'>Fujioka, Y., Noda, N. N., Nakatogawa, H. et al.</span>: <span class="ti">Dimeric coiled-coil structure of <em>Saccharomyces cerevisiae</em> Atg16 and its functional significance in autophagy.</span> <span class='so'>J. Biol. Chem., 285, 1508-1515 (2010)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/19889643" target="_blank">PubMed</a>]</span></li>
<li id="R49"><span class='au'>Matsushita, M., Suzuki, N. N., Obara, K. et al.</span>: <span class="ti">Structure of Atg5?Atg16, a complex essential for autophagy.</span> <span class='so'>J. Biol. Chem., 282, 6763-6772 (2007)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/17192262" target="_blank">PubMed</a>]</span></li>
<li id="R50"><span class='au'>Noda, N. N., Fujioka, Y., Hanada, T. et al.</span>: <span class="ti">Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating Atg8-PE conjugation.</span> <span class='so'>EMBO Rep., 14, 206-211 (2013)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/23238393" target="_blank">PubMed</a>]</span></li>
<li id="R51"><span class='au'>Otomo, C., Metlagel, Z., Takaesu, G. et al.</span>: <span class="ti">Structure of the human ATG12~ATG5 conjugate required for LC3 lipidation in autophagy.</span> <span class='so'>Nat. Struct. Mol. Biol., 20, 59-66 (2013)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/23202584" target="_blank">PubMed</a>]</span></li>
<li id="R52"><span class='au'>Yamaguchi, M., Matoba, K., Sawada, R. et al.</span>: <span class="ti">Noncanonical recognition and UBL loading of distinct E2s by autophagy-essential Atg7.</span> <span class='so'>Nat. Struct. Mol. Biol., 19, 1250-1256 (2012)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/23142983" target="_blank">PubMed</a>] [<a href="http://first.lifesciencedb.jp/archives/6186" target="_blank">V_r[</a>]</span></li>
<li id="R53"><span class='au'>Kaiser, S. E., Mao, K., Taherbhoy, A. M. et al.</span>: <span class="ti">Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and Atg7-Atg10 structures.</span> <span class='so'>Nat. Struct. Mol. Biol., 19, 1242-1249 (2012)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/23142976" target="_blank">PubMed</a>]</span></li>
<li id="R54"><span class='au'>Sakoh-Nakatogawa, M., Matoba, K., Asai, E. et al.</span>: <span class="ti">Atg12-Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site.</span> <span class='so'>Nat. Struct. Mol. Biol., 20, 433-439 (2013)[<a href="http://www.ncbi.nlm.nih.gov/pubmed/23503366" target="_blank">PubMed</a>] [<a href="http://first.lifesciencedb.jp/archives/6807" target="_blank">V_r[</a>]</span></li>
</ol>
<div class="au-profile">
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