Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating Atg8-PE conjugation
Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating Atg8-PE conjugation
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Publisher
Chichester, UK: John Wiley & Sons, Ltd
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Language
English
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Chichester, UK: John Wiley & Sons, Ltd
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Contents
Atg12 is conjugated to Atg5 through enzymatic reactions similar to ubiquitination. The Atg12–Atg5 conjugate functions as an E3‐like enzyme to promote lipidation of Atg8, whereas lipidated Atg8 has essential roles in both autophagosome formation and selective cargo recognition during autophagy. However, the molecular role of Atg12 modification in th...
Alternative Titles
Full title
Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating Atg8-PE conjugation
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3596133
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3596133
Other Identifiers
ISSN
1469-221X
E-ISSN
1469-3178
DOI
10.1038/embor.2012.208
