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Yeast Protein Serine/Threonine Phosphatases: Multiple Roles and Diverse Regulation
Author(s) -
STARK MICHAEL J. R.
Publication year - 1996
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/(sici)1097-0061(199612)12:16<1647::aid-yea71>3.0.co;2-q
Subject(s) - biology , yeast , saccharomyces cerevisiae , phosphatase , protein phosphatase 2 , serine , gene , genetics , threonine , complement (music) , function (biology) , biochemistry , phosphorylation , phenotype , complementation
Since the isolation of the first yeast protein phosphatase genes in 1989, much progress has been made in understanding this important group of proteins. Yeast contain genes encoding all the major types of protein phosphatase found in higher eukaryotes and the ability to use powerful genetic approaches will complement the wealth of biochemical information available from other systems. This review will summarize recent progress in understanding the structure, function and regulation of the PPP family of protein serine‐threonine phosphatases, concentrating on the budding yeast Saccharomyces cerevisiae .