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Glucose and nitrogen rapidly activate a Ca 2+ ‐inhibitable, serine/threonine kinase activity toward microtubule‐associated protein 2 in Saccharomyces cerevisiae
Author(s) -
Hoshi Minako,
Nishida Eisuke,
Matsumoto Seiji,
Akiyama Tetsu,
Kawakami Minoru,
Yahara Ichiro,
Sakai Hikoichi
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81617-5
Subject(s) - protein kinase a , biochemistry , cyclin dependent kinase 9 , saccharomyces cerevisiae , kinase , mitogen activated protein kinase kinase , cyclin dependent kinase 2 , ask1 , c raf , threonine , map kinase kinase kinase , biology , map2k7 , chemistry , yeast , serine , microbiology and biotechnology , phosphorylation
Treatment of the glucose‐starved yeast cells ( Saccharomyces cerevisiae ) with 1% glucose or 2‐deoxyglucose induced a rapid increase in a protein kinase activity in cell extracts that phosphorylated microtubule‐associated protein 2 (MAP2) in vitro. Addition of 0.5% ammonium sulfate to the nitrogen‐starved yeast cells also stimulated the kinase activity toward MAP2. The stimulated MAP2 kinase activities had the following common properties: (i) Activation was rapid and transient in response to stimuli; (ii) The kinase activity was serine/threonine‐specific; and (iii) The kinase activity was inhibited by micromolar concentrations of free Ca 2+ . These properties are very similar to those of the mitogen‐activated, Ca 2+ ‐sensitive MAP2 kinase we have recently found in mammalian fibroblastic cells. The MAP2 kinase activation may be involved in initiation of proliferation of yeast cells.