Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts golgi retention and results in default transport to the vacuole

Celeste A. Wilcox, Kevin Edward Redding, Robin Wright, Robert S. Fuller

Research output: Contribution to journalArticle

155 Citations (Scopus)

Abstract

Kex2 protease processes pro-α-factor in a late Golgi compartment in Saccharomyces cerevisiae. The first ∼30 residues of the 115 amino acid CO2H-terminal cytosolic tail (C-tail) of the Kex2 protein (Kex2p) contain a Golgi retention signal that resembles coated-pit localization signals in mammalian cell surface receptors. Mutation of one (Tyr713) of two tyrosine residues in the C-tail or deletion of sequences adjacent to Tyr713 results in loss of normal Golgi localization. Surprisingly, loss of the Golgi retention signal resulted in transport of C-tail mutant Kex2p to the vacuole (yeast lysosome), as judged by kinetics of degradation and by indirect immunoflourescence. Analysis of the loss of Kex2 function in vivo after shutting off expression of wild-type or mutant forms proved that mutations that cause rapid vacuolar turnover do so by increasing the rate of exit of the enzyme fro the pro-α-factor processing compartment. The most likely explanation for these results is that mutation of the Golgi retention signal in the C-tail results in transport of Kex2p to the vacuole by default. Wild-type Kex2p also was transported to the vacuole at an increased rate when overproduced, although apparently not due to saturation of a Golgi-retention mechanism. Instead, the wild-type and C-tail mutant forms of Kex2p may follow distinct paths to the vacuole.

Original languageEnglish
Pages (from-to)1353-1371
Number of pages19
JournalMolecular Biology of the Cell
Volume3
Issue number12
Publication statusPublished - Dec 1992

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Vacuoles
Tyrosine
Peptide Hydrolases
Yeasts
Mutation
Proteins
Sequence Deletion
Cell Surface Receptors
Mutant Proteins
Lysosomes
Saccharomyces cerevisiae
Carrier Proteins
Amino Acids
Enzymes

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts golgi retention and results in default transport to the vacuole. / Wilcox, Celeste A.; Redding, Kevin Edward; Wright, Robin; Fuller, Robert S.

In: Molecular Biology of the Cell, Vol. 3, No. 12, 12.1992, p. 1353-1371.

Research output: Contribution to journalArticle

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