Mechanistic insight into the nucleus-vacuole junction based on the Vac8p-Nvj1p crystal structure.

Proc. Natl. Acad. Sci. U.S.A.2017 Jun 06;114(23):E4539-E4548. Epub 2017 May 22

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Vac8p cationic triad (Arg276, Arg317, and Arg359) motifs interacting with Nvj1p are also critical to the recognition of Atg13p, a key component of the cytoplasm-to-vacuole targeting (CVT) pathway, indicating competitive binding to Vac8p. Indeed, mutation of the cationic triad abolishes CVT of Ape1p in vivo. Combined with biochemical data, the crystal structure reveals a Vac8p homodimer formed from ARM1, and this self-association, likely regulated by the flexible H1 helix and the C terminus of Nvj1p, is critical for Vac8p cellular functions.

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Mechanistic insight into the nucleus-vacuole junction based on the Vac8p-Nvj1p crystal structure.

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