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Research article2006Peer reviewedOpen access

The yeast tumor suppressor homologue Sro7p is required for targeting of the sodium pumping ATPase to the cell surface

Wadskog I, Forsmark A, Rossi G, Konopka C, Oyen M, Goksor M, Ronne H, Brennwald P, Adler L

Abstract

The SRO7/SOP1 encoded tumor suppressor homologue of Saccharomyces cerevisiae is required for maintenance of ion homeostasis in cells exposed to NaCl stress. Here we show that the NaCl sensitivity of the sro7 Delta mutant is due to defective sorting of Ena1p, the main sodium pump in yeast. On exposure of sro7 Delta mutants to NaCl stress, Enalp fails to be targeted to the cell surface, but is instead routed to the vacuole for degradation via the multivesicular endosome pathway. SRO7-deficient mutants accumulate post-Golgi vesicles at high salinity, in agreement with a previously described role for Sro7p in late exocytosis. However, Enalp is not sorted into these post-Golgi vesicles, in contrast to what is observed for the vesicles that accumulate when exocytosis is blocked in sec6-4 mutants at high salinity. These observations imply that Sro7p has a previously unrecognized role for sorting of specific proteins into the exocytic pathway. Screening for multicopy suppressors identified RSN1, encoding a transmembrane protein of unknown function. Overexpression of RSN1 restores NaCl tolerance of sro7 Delta mutants by retargeting Ena1p to the plasma membrane. We propose a model in which blocked exocytic sorting in sro7 Delta mutants, gives rise to quality control-mediated routing of Enalp to the vacuole

Published in

Molecular Biology of the Cell
2006, Volume: 17, number: 12, pages: 4988-5003
Publisher: AMER SOC CELL BIOLOGY