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

Artikel i vetenskaplig tidskrift
Författare Ingrid Wadskog
Annabelle Forsmark
Guendalina Rossi
Catherine Konopka
Mattias Oyen
Mattias Goksör
Hans Ronne
Patrick Brennwald
Lennart Adler
Publicerad i Molecular biology of the cell
Volym 17
Nummer/häfte 12
Sidor 4988-5003
ISSN 1059-1524
Publiceringsår 2006
Publicerad vid Institutionen för cell- och molekylärbiologi
Institutionen för fysik (GU)
Sidor 4988-5003
Språk en
Länkar dx.doi.org/10.1091/mbc.E05-08-0798
Ämnesord Adenosine Triphosphatases, metabolism, Carrier Proteins, metabolism, Cation Transport Proteins, metabolism, Cell Membrane, drug effects, metabolism, Gene Expression, drug effects, Genes, Fungal, Golgi Apparatus, drug effects, Mutation, genetics, Protein Transport, drug effects, Recombinant Fusion Proteins, metabolism, Saccharomyces cerevisiae, cytology, drug effects, growth & development, ultrastructure, Saccharomyces cerevisiae Proteins, metabolism, Secretory Vesicles, drug effects, Sequence Homology, Sodium Chloride, pharmacology, Thermodynamics, Tumor Suppressor Proteins, metabolism, Vacuoles, metabolism
Ämneskategorier Biologiska vetenskaper

Sammanfattning

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 sro7Delta mutant is due to defective sorting of Ena1p, the main sodium pump in yeast. On exposure of sro7Delta mutants to NaCl stress, Ena1p 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, Ena1p 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 sro7Delta mutants by retargeting Ena1p to the plasma membrane. We propose a model in which blocked exocytic sorting in sro7Delta mutants, gives rise to quality control-mediated routing of Ena1p to the vacuole.

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