An atypical BAR domain protein in autophagy. Issue 7 (3rd July 2018)

• Record Type: Journal Article
• Authors: Popelka, Hana; Klionsky, Daniel J.; Ragusa, Michael J.
• Is Part Of: Autophagy. Volume 14:Issue 7(2018)
• Page Start: 1155
• Page End: 1156
• Publication Date: 2018-07-03
• Subjects: amphipathic helix -- electron microscopy -- SAXS -- structure -- vacuole -- yeast; Autophagic vacuoles -- Periodicals; Apoptosis -- Periodicals; Cell death -- Periodicals; Lysosomes -- Periodicals; Degeneration (Pathology) -- Periodicals; Autophagy -- Periodicals; Cell Death -- Periodicals; Lysosomes -- Periodicals; Periodicals; 571.936
• DOI: 10.1080/15548627.2018.1445915
• Languages: English
• ISSNs: 1554-8627

Abstract

ABSTRACT: 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.