Open AccessGenetic analyses of yeast protein serine/threonine phosphatases
Author(s) -
Stark Michael J.R.,
Black Sheila,
Sneddon Alan A.,
Andrews Paul D.
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06753.x
Subject(s) - phosphatase , yeast , protein phosphorylation , saccharomyces cerevisiae , biology , serine , protein phosphatase 2 , gene , phosphorylation , biochemistry , threonine , autophagy related protein 13 , genetics , protein kinase a
Protein phosphorylation is an important regulatory phenomenon in yeasts just as in other eukaryotic cells and controls a wide variety of cellular processes. The importance of protein phosphatases as well as protein kinases as key elements in such control is becoming increasingly clear. Over the past four years since the first yeast protein phosphatase gene was isolated, many more such genes have been described and the number of genes encoding protein phosphatase catalytic subunits in Saccharomyces cerevisiae has comfortably entered double figures. Given the genetic approaches available, yeasts offer powerful systems for addressing the cellular roles of these enzymes. This review summarises the results of genetic studies aimed at determining the functions of protein serine/threoninc phosphatases in yeast.