Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Byeong-Won | - |
dc.contributor.author | Hong, Seung Beom | - |
dc.contributor.author | Kim, Jun Hoe | - |
dc.contributor.author | Kwon, Do Hoon | - |
dc.contributor.author | Song, Hyun Kyu | - |
dc.date.accessioned | 2021-09-06T03:58:09Z | - |
dc.date.available | 2021-09-06T03:58:09Z | - |
dc.date.created | 2021-06-14 | - |
dc.date.issued | 2013-03 | - |
dc.identifier.issn | 2041-1723 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/103861 | - |
dc.description.abstract | Infectious bacteria are cleared from mammalian cells by host autophagy in combination with other upstream cellular components, such as the autophagic receptor NDP52 and sugar receptor galectin-8. However, the detailed molecular basis of the interaction between these two receptors remains to be elucidated. Here, we report the biochemical characterization of both NDP52 and galectin-8 as well as the crystal structure of galectin-8 complexed with an NDP52 peptide. The unexpected observation of nicotinamide adenine dinucleotide located at the carbohydrate-binding site expands our knowledge of the sugar-binding specificity of galectin-8. The NDP52-galectin-8 complex structure explains the key determinants for recognition on both receptors and defines a special orientation of N- and C-terminal carbohydrate recognition domains of galectin-8. Dimeric NDP52 forms a ternary complex with two monomeric galectin-8 molecules as well as two LC3C molecules. These results lay the groundwork for understanding how host cells target bacterial pathogens for autophagy. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.subject | ANTIBACTERIAL AUTOPHAGY | - |
dc.subject | SELECTIVE AUTOPHAGY | - |
dc.subject | BACTERIA | - |
dc.subject | DEGRADATION | - |
dc.subject | SPECIFICITY | - |
dc.subject | INHIBITION | - |
dc.subject | RESTRICTS | - |
dc.subject | PROTEINS | - |
dc.subject | AFFINITY | - |
dc.subject | LIGANDS | - |
dc.title | Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8 | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Song, Hyun Kyu | - |
dc.identifier.doi | 10.1038/ncomms2606 | - |
dc.identifier.scopusid | 2-s2.0-84875908545 | - |
dc.identifier.wosid | 000318873900066 | - |
dc.identifier.bibliographicCitation | NATURE COMMUNICATIONS, v.4 | - |
dc.relation.isPartOf | NATURE COMMUNICATIONS | - |
dc.citation.title | NATURE COMMUNICATIONS | - |
dc.citation.volume | 4 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | ANTIBACTERIAL AUTOPHAGY | - |
dc.subject.keywordPlus | SELECTIVE AUTOPHAGY | - |
dc.subject.keywordPlus | BACTERIA | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | INHIBITION | - |
dc.subject.keywordPlus | RESTRICTS | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | AFFINITY | - |
dc.subject.keywordPlus | LIGANDS | - |
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