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Details on Person Atg18 constitutively interacts with Atg2, and the resulting ...

Class:IdSummation:5683909
_displayNameAtg18 constitutively interacts with Atg2, and the resulting ...
_timestamp2015-03-17 16:28:57
created[InstanceEdit:5683921] Jupe, Steve, 2015-03-17
literatureReference[LiteratureReference:5671908] The Atg18-Atg2 complex is recruited to autophagic membranes via phosphatidylinositol 3-phosphate and exerts an essential function
[LiteratureReference:5671915] Apg2p functions in autophagosome formation on the perivacuolar structure
[LiteratureReference:5683919] An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
[LiteratureReference:5683899] Atg9 vesicles are an important membrane source during early steps of autophagosome formation
[LiteratureReference:5682381] Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase
modified[InstanceEdit:5683929] Jupe, Steve, 2015-03-17
textAtg18 constitutively interacts with Atg2, and the resulting complex interacts with Atg9 during autophagy (Obara et al. 2008, Shintani et al. 2001). In yeast, the induction of autophagy leads to Atg9-rich golgi-derived vesicles 30-60nm in diameter (Mari et al. 2010, Yamamoto et al. 2012). These vesicles accumulate at the PAS in an Atg1-dependent manner, where Atg1-mediated phosphorylation of Atg9 facilitates the recruitment of Atg8 and Atg18 and subsequent phagophore expansion (Papinski et al. 2014).
(summation)[Reaction:5683926] Atg18:Atg2 binds Atg9 [Saccharomyces cerevisiae]
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