The high osmolarity glycerol response (HOG) MAP kinase pathway controls localization of a yeast golgi glycosyltransferase.

Reynolds TB, Hopkins BD, Lyons MR, Graham TR
J Cell Biol. 1998 143 (4): 935-46

PMID: 9817752 · PMCID: PMC2132948 · DOI:10.1083/jcb.143.4.935

The yeast alpha-1,3-mannosyltransferase (Mnn1p) is localized to the Golgi by independent transmembrane and lumenal domain signals. The lumenal domain is localized to the Golgi complex when expressed as a soluble form (Mnn1-s) by exchange of its transmembrane domain for a cleavable signal sequence (Graham, T. R., and V. A. Krasnov. 1995. Mol. Biol. Cell. 6:809-824). Mutants that failed to retain the lumenal domain in the Golgi complex, called lumenal domain retention (ldr) mutants, were isolated by screening mutagenized yeast colonies for those that secreted Mnn1-s. Two genes were identified by this screen, HOG1, a gene encoding a mitogen-activated protein kinase (MAPK) that functions in the high osmolarity glycerol (HOG) pathway, and LDR1. We have found that basal signaling through the HOG pathway is required to localize Mnn1-s to the Golgi in standard osmotic conditions. Mutations in HOG1 and LDR1 also perturb localization of intact Mnn1p, resulting in its loss from early Golgi compartments and a concomitant increase of Mnn1p in later Golgi compartments.

MeSH Terms (22)

Calcium-Calmodulin-Dependent Protein Kinases Cell Wall Cloning, Molecular Fungal Proteins Gene Expression Regulation, Fungal Genetic Complementation Test Glycosyltransferases Golgi Apparatus Mannosyltransferases MAP Kinase Kinase Kinases Membrane Glycoproteins Mitogen-Activated Protein Kinases Mutagenesis Osmolar Concentration Phenotype Protein-Serine-Threonine Kinases Protein Kinase C Protein Structure, Tertiary Pyrophosphatases Saccharomyces cerevisiae Proteins Signal Transduction Yeasts

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