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© The Rockefeller University Press, 0021-9525/1998//935 $5.00
The Journal of Cell Biology, Volume 143, Number 4, , 1998 935-946

Regular Articles

The High Osmolarity Glycerol Response (HOG) MAP Kinase Pathway Controls Localization of a Yeast Golgi Glycosyltransferase



Todd B. Reynolds, B. Diane Hopkins, Matthew R. Lyons, and Todd R. Graham

Department of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235

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.

Key Words: HOG1 • MAP kinase • Golgi localization • glycosyltransferase • MNN1

Abbreviations used in this paper: CPY, carboxypeptidase Y; ECL, enhanced chemiluminescent; EMS, ethylmethanesulfonate; HOG, high osmolarity glycerol response; ldr, lumenal domain retention; MAPK, mitogen-activated protein kinase; MAPKK, MAPK kinase; MAPKKK, MAPK kinase kinases; Mnn1p, {alpha}-1,3-mannosyltransferase; PGK, phosphoglycerate kinase; PKC, protein kinase C; SD, synthetic defined.

Address all correspondence to Todd R. Graham, Department of Molecular Biology, Vanderbilt University, Nashville, TN 37235. Tel.: (615) 343-1835. Fax: (615) 343-6707. E-mail: tr.graham{at}vanderbilt.edu


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