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PLoS One. 2012;7(9):e41408. doi: 10.1371/journal.pone.0041408. Epub 2012 Sep 26.

Mutational analysis of the yeast TRAPP subunit Trs20p identifies roles in endocytic recycling and sporulation.

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  • 1Consorzio Mario Negri Sud, Santa Maria Imbaro, Chieti, Italy.

Erratum in

  • PLoS One. 2013;8(5). doi:10.1371/annotation/118aea6f-8edc-4107-8012-29110a55a9b1.


Trs20p is a subunit of the evolutionarily conserved TRAPP (TRAnsport Protein Particle) complex that mediates various aspects of membrane trafficking. Three TRAPP complexes have been identified in yeast with roles in ER-to-Golgi trafficking, post-Golgi and endosomal-to-Golgi transport and in autophagy. The role of Trs20p, which is essential for viability and a component of all three complexes, and how it might function within each TRAPP complex, has not been clarified to date. To begin to address the role of Trs20p we generated different mutants by random mutagenesis but, surprisingly, no defects were observed in diverse anterograde transport pathways or general secretion in Trs20 temperature-sensitive mutants. Instead, mutation of Trs20 led to defects in endocytic recycling and a block in sporulation/meiosis. The phenotypes of different mutants appear to be separable suggesting that the mutations affect the function of Trs20 in different TRAPP complexes.

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