About: Lipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein

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About: Lipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Lipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein
Creator	Du, Li-Lin Nakatogawa, Hitoshi Coffman, Valerie Du, Xiao-Min Liu, Xiao-Man Noda, Nobuo Ohsumi, Yoshinori Wu, Jian-Qiu Yamasaki, Akinori
topic	covid:3c70b15cfe076cdbf34d0b8ad6b316df91897454#this
source	PMC
abstract	The ubiquitin-like protein Atg8, in its lipidated form, plays central roles in autophagy. Yet, remarkably, Atg8 also carries out lipidation-independent functions in non-autophagic processes. How Atg8 performs its moonlighting roles is unclear. Here we report that in the fission yeast Schizosaccharomyces pombe and the budding yeast Saccharomyces cerevisiae, the lipidation-independent roles of Atg8 in maintaining normal morphology and functions of the vacuole require its interaction with a vacuole membrane protein Hfl1 (homolog of human TMEM184 proteins). Crystal structures revealed that the Atg8-Hfl1 interaction is not mediated by the typical Atg8-family-interacting motif (AIM) that forms an intermolecular β-sheet with Atg8. Instead, the Atg8-binding regions in Hfl1 proteins adopt a helical conformation, thus representing a new type of AIMs (termed helical AIMs here). These results deepen our understanding of both the functional versatility of Atg8 and the mechanistic diversity of Atg8 binding.
has issue date	2018-11-19(xsd:dateTime)
bibo:doi	10.7554/elife.41237
bibo:pmid	30451685
has license	cc-by
sha1sum (hex)	3c70b15cfe076cdbf34d0b8ad6b316df91897454
schema:url	https://doi.org/10.7554/elife.41237
resource representing a document's title	Lipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein
has PubMed Central identifier	PMC6279349
has PubMed identifier	30451685
resource representing a document's body	covid:3c70b15cfe076cdbf34d0b8ad6b316df91897454#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/3c70b15cfe076cdbf34d0b8ad6b316df91897454
is schema:about of	named entity 'The' named entity 'AUTOPHAGY' named entity 'rely' named entity 'CBB' named entity 'sodium chloride' named entity 'lipid kinase' named entity 'binding surfaces' named entity 'NDP52' named entity 'phenotypes' named entity 'Phe' named entity 'vacuole membrane' named entity 'peptide' named entity 'Venus' named entity 'NaCl' named entity 'nitrogen' named entity 'PCR-based' named entity 'Y-site' named entity 'pH 8' named entity 'hydrophobic' named entity 'dithiothreitol' named entity 'vacuoles' named entity 'EcoRI' named entity 'protein expression' named entity 'human rhinovirus' named entity 'vacuole' named entity 'Atg8' named entity 'pH 8' named entity 'fission yeast' named entity 'Atg8' named entity 'glycerol' named entity 'helix' named entity 'Atg8' named entity 'HEPES' named entity 'acidic residues' named entity 'sequence alignment' named entity 'Atg8' named entity 'vacuole' named entity 'ubiquitin' named entity 'S. cerevisiae' named entity 'HEPES' named entity 'Macroautophagy' named entity 'binding affinity' named entity 'transporter proteins' named entity 'yeast' named entity 'vacuoles' named entity 'C-terminal' named entity 'wild type' named entity 'signal transduction' named entity 'gene' named entity 'peptides' named entity 'vacuole' named entity 'enzyme' named entity 'superfamily' named entity 'glutathione' named entity 'fission yeast' named entity 'beamline' named entity 'Alanine' named entity 'protease inhibitor' named entity 'pH 8' named entity 'coiled-coil region' named entity 'amino acids' named entity 'EDTA' named entity 'vacuolar' named entity 'MgSO' named entity 'hydrophobic residues' named entity 'protein family' named entity 'G418' named entity 'Bioneer' named entity 'Glu' named entity 'PMSF' named entity 'lipidation' named entity 'start codon'

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