Matches in SemOpenAlex for { <https://semopenalex.org/work/W3009647594> ?p ?o ?g. }
- W3009647594 endingPage "35" @default.
- W3009647594 startingPage "15" @default.
- W3009647594 abstract "Autophagy is a crucial cellular degradation and recycling pathway. During autophagy double-membrane vesicles, called autophagosomes, encapsulate cellular components and deliver their cargo to the lytic compartment for degradation. Formation of autophagosomes is regulated by the Atg1 kinase complex in yeast and the homologous ULK1 kinase complex in mammals. While research on Atg1 and ULK1 has advanced our understanding of how these protein kinases function in autophagy, the other Atg1/ULK1 kinase complex members have received much less attention. Here, we focus on the functions of the Atg1 kinase complex members Atg11 and Atg17 as well as the ULK1 kinase complex member FIP200 in autophagy. These three proteins act as scaffolds in their respective complexes. Recent studies have made it evident that they have similar but also distinct functions. In this article, we review our current understanding of how these scaffold proteins function from autophagosome formation to fusion and also discuss their possible roles in diseases." @default.
- W3009647594 created "2020-03-13" @default.
- W3009647594 creator A5013116980 @default.
- W3009647594 creator A5022608936 @default.
- W3009647594 creator A5082156932 @default.
- W3009647594 date "2020-01-01" @default.
- W3009647594 modified "2023-10-18" @default.
- W3009647594 title "Scaffold proteins in bulk and selective autophagy" @default.
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