About: Hidden Behind Autophagy: The Unconventional Roles of ATG Proteins

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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
has title	Hidden Behind Autophagy: The Unconventional Roles of ATG Proteins
Creator	Reggiori, Fulvio Mauthe, Mario V'kovski, Philip Bestebroer, Jovanka
Source	Medline; PMC
abstract	Macroautophagy (hereafter referred to as autophagy) is an evolutionarily conserved intracellular catabolic transport route that generally allows the lysosomal degradation of cytoplasmic components, including bulk cytosol, protein aggregates, damaged or superfluous organelles and invading microbes. Target structures are sequestered by double‐membrane vesicles called autophagosomes, which are formed through the concerted action of the autophagy (ATG)‐related proteins. Until recently it was assumed that ATG proteins were exclusively involved in autophagy. A growing number of studies, however, have attributed functions to some of them that are distinct from their classical role in autophagosome biogenesis. Autophagy‐independent roles of the ATG proteins include the maintenance of cellular homeostasis and resistance to pathogens. For example, they assist and enhance the turnover of dead cells and microbes upon their phagocytic engulfment, and inhibit murine norovirus replication. Moreover, bone resorption by osteoclasts, innate immune regulation triggered by cytoplasmic DNA and the ER‐associated degradation regulation all have in common the requirement of a subset of ATG proteins. Microorganisms such as coronaviruses, Chlamydia trachomatis or Brucella abortus have even evolved ways to manipulate autophagy‐independent functions of ATG proteins in order to ensure the completion of their intracellular life cycle. Taken together these novel mechanisms add to the repertoire of functions and extend the number of cellular processes involving the ATG proteins. [Image: see text]
has issue date	2013-07-30(xsd:dateTime)
bibo:doi	10.1111/tra.12091
bibo:pmid	23837619
has license	no-cc
sha1sum (hex)	8c4d11d0eba3961e79a2401f0ce117ccdd336e35
schema:url	https://doi.org/10.1111/tra.12091
resource representing a document's title	Hidden Behind Autophagy: The Unconventional Roles of ATG Proteins
has PubMed Central identifier	PMC7169877
has PubMed identifier	23837619
schema:publication	Traffic
resource representing a document's body	covid:8c4d11d0eba3961e79a2401f0ce117ccdd336e35#body_text
is schema:about of	named entity '80%' named entity 'equally' named entity 'Proteins' named entity 'ATG16L1' named entity 'toll-like receptors' named entity 'Escherichia coli' named entity 'autophagy' named entity 'cell division' named entity 'knockout mice' named entity 'virus' named entity 'ATG5' named entity 'TLR' named entity 'autophagy' named entity 'VPS34' named entity 'OS-9' named entity 'Murine norovirus' named entity 'LC3-I' named entity 'C. trachomatis' named entity 'virus' named entity 'autophagosome' named entity 'ATG12' named entity 'apoptosis' named entity 'BECLIN1' named entity 'organelle' named entity 'cytochrome' named entity 'ultrastructural' named entity 'TLR1' named entity 'conjugation' named entity 'gene' named entity 'ULK1' named entity 'autophagosomes' named entity 'phosphatidylethanolamine' named entity 'IRF3' named entity 'LC3' named entity 'transcription' named entity 'intracellular bacterium' named entity 'ATG12' named entity 'ZWINT-1' named entity 'Golgi' named entity 'cellular functions' named entity 'bone tissue' named entity 'RNA virus' named entity 'autophagy' named entity 'ATG7' named entity 'endosomes' named entity 'ERAD' named entity 'agonist' named entity 'mice' named entity 'autophagy' named entity 'RAB9' named entity 'vacuole' named entity 'bone resorption' named entity 'B. abortus' named entity 'biogenesis' named entity 'OS-9' named entity 'TLR9' named entity 'MHV' named entity 'secretion' named entity 'JAK-STAT' named entity 'C. trachomatis' named entity 'infection' named entity 'LC3' named entity 'ATG12' named entity 'anticancer drugs' named entity 'lipidation' named entity 'pathogens' named entity 'lysosome' named entity 'BECLIN1' named entity 'ATG5' named entity 'lipidated' named entity 'atg7' named entity 'SEL1L' named entity 'TLR4' named entity 'ATG9A' named entity 'lysosomes' named entity 'SEL1L' named entity 'biogenesis' named entity 'conjugation'

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