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Autophagy. 2018;14(7):1155-1156. doi: 10.1080/15548627.2018.1445915. Epub 2018 May 25.

An atypical BAR domain protein in autophagy.

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a Life Sciences Institute , University of Michigan , Ann Arbor , MI USA.
b Department of Molecular , Cellular, and Developmental Biology , University of Michigan , Ann Arbor , MI USA.
c Department of Chemistry , Dartmouth College , Hanover , NH USA.


The sorting nexin Atg20 interacts with the selective macroautophagy/autophagy scaffolding protein Atg11, suggesting an important role for Atg20 in the initiation of selective autophagy. To explore this possibility, we recently investigated the structure and function of Atg20 using a variety of biophysical and yeast genetic approaches. Our data demonstrate that the BAR domain of Atg20 interacts with Snx4/Atg24 to form an asymmetric heterodimeric BAR domain complex. Atg20 also contains a long intrinsically disordered N terminus that facilitates binding to Atg11 and a large 89-amino acid insertion in its BAR domain, which we have termed the BAR-GAP. This BAR-GAP region is a unique feature of Atg20 and has not been observed in other BAR domains. Furthermore, the BAR-GAP of Atg20 contains an amphipathic helix which is required for membrane binding, tubulation and autophagy. Our findings demonstrate the important role of this novel region in autophagy.


SAXS; amphipathic helix; electron microscopy; structure; vacuole; yeast

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