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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2010-4-23
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pubmed:abstractText |
Accumulation of ubiquitinated proteins in cytoplasmic and/or nuclear inclusions is a hallmark of several diseases associated with premature cell death. SQSTM1/p62 is known to bind ubiquitinated substrates and aid their aggregation and degradation by macroautophagy. We show here that p62 is required to recruit the large phosphoinositide-binding protein ALFY to cytoplasmic p62 bodies generated upon amino acid starvation or puromycin-treatment. ALFY, as well as p62, is required for formation and autophagic degradation of cytoplasmic ubiquitin-positive inclusions. Moreover, both p62 and ALFY localize to nuclear promyleocytic leukemia (PML) bodies. The Drosophila p62 homologue Ref(2) P accumulates in ubiquitinated inclusions in the brain of flies carrying mutations in the ALFY homologue Blue cheese, demonstrating that ALFY is required for autophagic degradation of p62-associated ubiquitinated proteins in vivo. We conclude that p62 and ALFY interact to organize misfolded, ubiquitinated proteins into protein bodies that become degraded by autophagy.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Macrolides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SQSTM1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitinated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/WDFY3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/bafilomycin A1
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1554-8635
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pubmed:author |
pubmed-author:ØvervatnAudA,
pubmed-author:BjørkøyGeirG,
pubmed-author:BrechAndreasA,
pubmed-author:ClausenTerje HøyvardeTH,
pubmed-author:FinleyKimK,
pubmed-author:IsaksonPaulineP,
pubmed-author:JohansenTerjeT,
pubmed-author:LamarkTrondT,
pubmed-author:LarsenKenneth BowitzKB,
pubmed-author:SimonsenAnneA,
pubmed-author:StenmarkHaraldH
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pubmed:issnType |
Electronic
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
330-44
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pubmed:meshHeading |
pubmed-meshheading:20168092-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:20168092-Animals,
pubmed-meshheading:20168092-Autophagy,
pubmed-meshheading:20168092-Drosophila Proteins,
pubmed-meshheading:20168092-Drosophila melanogaster,
pubmed-meshheading:20168092-Enzyme Inhibitors,
pubmed-meshheading:20168092-HeLa Cells,
pubmed-meshheading:20168092-Humans,
pubmed-meshheading:20168092-Inclusion Bodies,
pubmed-meshheading:20168092-Macrolides,
pubmed-meshheading:20168092-Membrane Proteins,
pubmed-meshheading:20168092-Multiprotein Complexes,
pubmed-meshheading:20168092-Protein Folding,
pubmed-meshheading:20168092-RNA, Small Interfering,
pubmed-meshheading:20168092-Recombinant Fusion Proteins,
pubmed-meshheading:20168092-Transcription Factors,
pubmed-meshheading:20168092-Ubiquitinated Proteins
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pubmed:year |
2010
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pubmed:articleTitle |
p62/SQSTM1 and ALFY interact to facilitate the formation of p62 bodies/ALIS and their degradation by autophagy.
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pubmed:affiliation |
Molecular Cancer Research Group, Department of Medical Biology, University of Tromsø, Tromsø, Norway.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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