2016
DOI: 10.1038/cddis.2016.230
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TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death

Abstract: The formation of the autophagosome is controlled by an orderly action of ATG proteins. However, how these proteins are recruited to autophagic membranes remain poorly clarified. In this study, we have provided a line of evidence confirming that EVA1A (eva-1 homolog A)/TMEM166 (transmembrane protein 166) is associated with autophagosomal membrane development. This notion is based on dotted EVA1A structures that colocalize with ZFYVE1, ATG9, LC3B, ATG16L1, ATG5, STX17, RAB7 and LAMP1, which represent different s… Show more

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Cited by 50 publications
(54 citation statements)
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“…The requirement of the WD domain for LAP suggests that the scaffold provided by the WD domains of ATG16L1 has evolved a specialized role, independent of autophagy, to ensure the quality control of endocytic pathways by conjugating LC3 to phagosomes containing pathogens or apoptotic cells, or endocytic compartments showing signs of damage. This is supported by the observation that the WD domain of ATG16L1 binds NOD-like receptors [29], MEFV/TRIM20 [30], TMEM59 [31] and EVA1A/TMEM166 [32], which are important in pathogen recognition. Our observation that mice remain viable and maintain tissue homeostasis over long periods in the absence of the WD domain suggests that LAP does not play an essential role in preventing tissue damage in vivo.…”
Section: Discussionmentioning
confidence: 81%
“…The requirement of the WD domain for LAP suggests that the scaffold provided by the WD domains of ATG16L1 has evolved a specialized role, independent of autophagy, to ensure the quality control of endocytic pathways by conjugating LC3 to phagosomes containing pathogens or apoptotic cells, or endocytic compartments showing signs of damage. This is supported by the observation that the WD domain of ATG16L1 binds NOD-like receptors [29], MEFV/TRIM20 [30], TMEM59 [31] and EVA1A/TMEM166 [32], which are important in pathogen recognition. Our observation that mice remain viable and maintain tissue homeostasis over long periods in the absence of the WD domain suggests that LAP does not play an essential role in preventing tissue damage in vivo.…”
Section: Discussionmentioning
confidence: 81%
“…It would appear, however, that the sites identified here are important in all tested examples of non‐canonical autophagy. Interestingly, TMEM59 and TMEM166/EVA1 have been implicated in autophagy activation through the interaction with the WD40 CTD of ATG16L1 (Boada‐Romero et al , ; Hu et al , ). However, as yet, it is not clear whether these represent true non‐canonical autophagy pathways.…”
Section: Discussionmentioning
confidence: 99%
“…The loss of membrane recruitment of ATG16L1 correlated with a loss of LC3 lipidation. Individual residues in the WD40 domain were shown to be required for membrane localization of ATG16L1 and LC3 lipidation but the factors that mediate ATG16L1 recruitment remain to be identified, although TMEM59 and TMEM166/EVA1 could be involved (Boada‐Romero et al , ; Hu et al , ). Employing the truncated ATG16L1 lacking the WD40 domain, the authors went on to analyze the function of the ATG16L1 recruitment and LC3 lipidation in autophagy‐unrelated processes.…”
Section: Model For the Recruitment Of Atg16l1 To Membranesmentioning
confidence: 99%