| pubmed-article:19270696 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19270696 | lifeskim:mentions | umls-concept:C0004391 | lld:lifeskim |
| pubmed-article:19270696 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:19270696 | lifeskim:mentions | umls-concept:C1306673 | lld:lifeskim |
| pubmed-article:19270696 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:19270696 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:19270696 | pubmed:dateCreated | 2009-4-1 | lld:pubmed |
| pubmed-article:19270696 | pubmed:abstractText | Beclin 1, a protein essential for autophagy, binds to hVps34/Class III phosphatidylinositol-3-kinase and UVRAG. Here, we have identified two Beclin 1 associated proteins, Atg14L and Rubicon. Atg14L and UVRAG bind to Beclin 1 in a mutually exclusive manner, whereas Rubicon binds only to a subpopulation of UVRAG complexes; thus, three different Beclin 1 complexes exist. GFP-Atg14L localized to the isolation membrane and autophagosome, as well as to the ER and unknown puncta. Knockout of Atg14L in mouse ES cells caused a defect in autophagosome formation. GFP-Rubicon was localized at the endosome/lysosome. Knockdown of Rubicon caused enhancement of autophagy, especially at the maturation step, as well as enhancement of endocytic trafficking. These data suggest that the Beclin 1-hVps34 complex functions in two different steps of autophagy by altering the subunit composition. | lld:pubmed |
| pubmed-article:19270696 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19270696 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19270696 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19270696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19270696 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19270696 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:19270696 | pubmed:issn | 1476-4679 | lld:pubmed |
| pubmed-article:19270696 | pubmed:author | pubmed-author:AkiraShizuoS | lld:pubmed |
| pubmed-article:19270696 | pubmed:author | pubmed-author:IsobeToshiaki... | lld:pubmed |
| pubmed-article:19270696 | pubmed:author | pubmed-author:SatohTakashiT | lld:pubmed |
| pubmed-article:19270696 | pubmed:author | pubmed-author:YoshimoriTamo... | lld:pubmed |
| pubmed-article:19270696 | pubmed:author | pubmed-author:NodaTakeshiT | lld:pubmed |
| pubmed-article:19270696 | pubmed:author | pubmed-author:IchimuraTohru... | lld:pubmed |
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| pubmed-article:19270696 | pubmed:author | pubmed-author:Shirahama-Nod... | lld:pubmed |
| pubmed-article:19270696 | pubmed:author | pubmed-author:OmoriHirokoH | lld:pubmed |
| pubmed-article:19270696 | pubmed:author | pubmed-author:KurotoriNaoki... | lld:pubmed |
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| pubmed-article:19270696 | pubmed:author | pubmed-author:TabataKeisuke... | lld:pubmed |
| pubmed-article:19270696 | pubmed:author | pubmed-author:MaejimaIkukoI | lld:pubmed |
| pubmed-article:19270696 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19270696 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:19270696 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19270696 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19270696 | pubmed:pagination | 385-96 | lld:pubmed |
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| pubmed-article:19270696 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19270696 | pubmed:articleTitle | Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. | lld:pubmed |
| pubmed-article:19270696 | pubmed:affiliation | Department of Cellular Regulation, Research Institute for Microbial Diseases, Osaka University, Suita, Japan. | lld:pubmed |
| pubmed-article:19270696 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19270696 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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