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

doi:10.1083/jcb.143.4.935

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Article

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

The Journal of cell biology - 16 Nov 1998

Reynolds T B, Hopkins B D, Lyons M R, Graham T R

Abstract excerpt

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...

Topics

Calcium-Calmodulin-Dependent Protein Kinases
Cell Wall
Cloning, Molecular
Fungal Proteins
Gene Expression Regulation, Fungal
Genetic Complementation Test
Glycosyltransferases
Golgi Apparatus
MAP Kinase Kinase Kinases
Mannosyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Membrane Glycoproteins

Mitogen-Activated Protein Kinases

Mutagenesis

Osmolar Concentration

Phenotype

Protein Kinase C

Protein Serine-Threonine Kinases

Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

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

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-9817752-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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