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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
41
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pubmed:dateCreated |
2003-10-6
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pubmed:abstractText |
Autophagy is a process for the bulk degradation of cytosolic compartments by lysosomes/vacuoles. The formation of autophagosomes involves a dynamic rearrangement of the membrane for which two ubiquitin-like modifications (the conjugation of Apg12p and the modification of a soluble form of MAP-LC3 to a membrane-bound form) are essential. In yeast, Apg10p is an E2-like enzyme essential for Apg12p conjugation. The isolated mouse APG10 gene product interacts with mammalian Apg12p dependent on mammalian Apg7p (E1-like enzyme), and facilitates Apg12p conjugation. The interaction of Apg10p with Apg12p is dependent on the carboxyl-terminal glycine of Apg12p. Mutational analysis of the predicted active site cysteine (Cys161) within mouse Apg10p shows that mutant Apg10pC161S, which can form a stable intermediate with Apg12p, inhibits Apg12p conjugation even in the presence of Apg7p, while overexpression of Apg7p facilitates formation of an Apg12p-Apg5p conjugate. Furthermore, the coexpression of Apg10p with Apg7p facilitates the modification of a soluble form of MAP-LC3 to a membrane-bound form, a second modification essential for autophagy. Mouse Apg10p interacts with MAP-LC3 in HEK293 cells, while no mutant Apg10pC161S forms any intermediate with MAP-LC3. Direct interaction between Apg10p and MAP-LC3 is also demonstrated by yeast two-hybrid analysis. The inability of mutant Apg10pC161S to form any intermediate with MAP-LC3 has ruled out the possibility that MAP-LC3 interacts with Apg10p as a substrate.
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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/ATG3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ATG7 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Apg12l protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/MAP1LC3A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MAP1LC3B protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MAP1LC3C protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Conjugating Enzymes
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39517-26
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12890687-Amino Acid Sequence,
pubmed-meshheading:12890687-Animals,
pubmed-meshheading:12890687-Autophagy,
pubmed-meshheading:12890687-Base Sequence,
pubmed-meshheading:12890687-Cell Line,
pubmed-meshheading:12890687-DNA, Complementary,
pubmed-meshheading:12890687-Humans,
pubmed-meshheading:12890687-Ligases,
pubmed-meshheading:12890687-Mice,
pubmed-meshheading:12890687-Microtubule-Associated Proteins,
pubmed-meshheading:12890687-Models, Biological,
pubmed-meshheading:12890687-Molecular Sequence Data,
pubmed-meshheading:12890687-Mutagenesis, Site-Directed,
pubmed-meshheading:12890687-Oxidoreductases,
pubmed-meshheading:12890687-Proteins,
pubmed-meshheading:12890687-Recombinant Proteins,
pubmed-meshheading:12890687-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12890687-Sequence Homology, Amino Acid,
pubmed-meshheading:12890687-Two-Hybrid System Techniques,
pubmed-meshheading:12890687-Ubiquitin-Conjugating Enzymes
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pubmed:year |
2003
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pubmed:articleTitle |
The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification.
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pubmed:affiliation |
Department of Biochemistry, Juntendo University, Medical School, Tokyo 113-8421, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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