The requirement for the hydrophobic motif phosphorylation of Ypk1 in yeast differs depending on the downstream events, including endocytosis, cell growth, and resistance to a sphingolipid biosynthesis inhibitor, ISP-1.

doi:10.1016/j.abb.2005.02.030

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Article

The requirement for the hydrophobic motif phosphorylation of Ypk1 in yeast differs depending on the downstream events, including endocytosis, cell growth, and resistance to a sphingolipid biosynthesis inhibitor, ISP-1.

Archives of biochemistry and biophysics - 1 May 2005

Tanoue Daisuke, Kobayashi Takafumi, Sun Yidi, Fujita Tetsuro, Takematsu Hiromu, Kozutsumi Yasunori

Abstract excerpt

ISP-1 inhibits de novo sphingolipid biosynthesis and induces growth defects in both mammals and yeast (Saccharomyces cerevisiae). In our previous study, YPK1/SLI2 was identified as one of multicopy suppressor genes for ISP-1 in yeast. Ypk1 is proposed to be a downstream serine/threonine kinase of...

Topics

Amino Acid Motifs
Amino Acid Substitution
Antifungal Agents
Cell Enlargement
Drug Resistance, Fungal
Endocytosis
Fatty Acids, Monounsaturated
Glycogen Synthase Kinase 3
Phenotype
Point Mutation
Protein-Tyrosine Kinases
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins

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Identifiers

PMID: 15820214
DOI: 10.1016/j.abb.2005.02.030

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-15820214-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.