ArticleProceedings of the National Academy of Sciences of the United States of America2026
Atg39-dependent nucleophagy and Atg40-dependent ER-phagy require the Apq12/Brr6/Brl1 complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Autophagic degradation of parts of the nucleus (nucleophagy) and endoplasmic reticulum (ER-phagy) utilizes the selective autophagy receptors, Atg39 and Atg40, that link their target structures to the autophagy machinery. Here, we show that a complex of three proteins, Apq12, Brr6, and Brl1, is needed for both Atg39-dependent nucleophagy and Atg40-dependent ER-phagy. Apq12, Brr6, and Brl1 each have two transmembrane domains flanking a luminal region that contains an amphipathic helix. The Apq12/Brr6/Brl1 complex has been implicated in membrane remodeling during nuclear pore formation. While autophagosomal flux is unaffected by the loss of Apq12, Brr6, or Brl1, vacuolar delivery of outer and inner nuclear membrane proteins (Hmg1, Nvj1, and Src1), pan-ER proteins (Sec63 and Per33), and an ER tubule junction protein (Lnp1) is blocked. In
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