Dual regulation of the yeast CDC28-p40 protein kinase complex: Cell cycle, pheromone, and nutrient limitation effects

Michael D. Mendenhall; Christopher A. Jones; Steven I. Reed

doi:10.1016/0092-8674(87)90519-8

Dual regulation of the yeast CDC28-p40 protein kinase complex: Cell cycle, pheromone, and nutrient limitation effects

Michael D. Mendenhall, Christopher A. Jones, Steven I. Reed

Molecular and Cellular Biochemistry

Research output: Contribution to journal › Article › peer-review

99 Scopus citations

Abstract

A 40 kd polypeptide that coprecipitates with the CDC28 gene product in immune complexes is specifically phosphorylated by the CDC28 protein kinase. Using this reaction, we detect activity only in extracts from dividing G1 phase cells. Exit from G1 by entry into S phase or the preconjugatory state induced by mating pheromone correlates with loss of p40 phosphorylation activity. Inactive extracts from cdc28 mutants complement extracts from cells arrested in S or M phase, suggesting that non-G1 cells are deficient in an exchangeable activating factor. Stationary and pheromone-treated cultures are rich in this exchangeable factor, but possess an inactive kinase that is not activated by complementation. cAMP-deficient mutants resemble stationary cells.

Original language	English
Pages (from-to)	927-935
Number of pages	9
Journal	Cell
Volume	50
Issue number	6
DOIs	https://doi.org/10.1016/0092-8674(87)90519-8
State	Published - Sep 11 1987

Bibliographical note

Funding Information:
The authors would like to thank Dr. Cal S. McLaughlin for providing instructional and material assistance with the elutriator rotor, and Jeffrey A. Hadwiger, Jeong-Yau Ho, Dr. Curt Wittenberg, and Carolyn Keierle-ber for helpful discussion. We would also like to thank Dr. Ralph Arling-haus for providing laboratory space and synthetic peptides. M. D. M. is a Fellow of The Jane Coffin Childs Memorial Fund for Medical Research. This investigation has been aided by a grant from The Jane Coffin Childs Memorial Fund for Medical Research. C. A. J. was sup. ported by an EMBO postdoctoral fellowship. This work was supported by National Institutes of Health grants GM28005 and GM38328 to S. I. R., who also acknowledges the support provided by American Cancer Society Faculty Research Award FRA-246. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/0092-8674(87)90519-8

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title = "Dual regulation of the yeast CDC28-p40 protein kinase complex: Cell cycle, pheromone, and nutrient limitation effects",

abstract = "A 40 kd polypeptide that coprecipitates with the CDC28 gene product in immune complexes is specifically phosphorylated by the CDC28 protein kinase. Using this reaction, we detect activity only in extracts from dividing G1 phase cells. Exit from G1 by entry into S phase or the preconjugatory state induced by mating pheromone correlates with loss of p40 phosphorylation activity. Inactive extracts from cdc28 mutants complement extracts from cells arrested in S or M phase, suggesting that non-G1 cells are deficient in an exchangeable activating factor. Stationary and pheromone-treated cultures are rich in this exchangeable factor, but possess an inactive kinase that is not activated by complementation. cAMP-deficient mutants resemble stationary cells.",

author = "Mendenhall, {Michael D.} and Jones, {Christopher A.} and Reed, {Steven I.}",

note = "Funding Information: The authors would like to thank Dr. Cal S. McLaughlin for providing instructional and material assistance with the elutriator rotor, and Jeffrey A. Hadwiger, Jeong-Yau Ho, Dr. Curt Wittenberg, and Carolyn Keierle-ber for helpful discussion. We would also like to thank Dr. Ralph Arling-haus for providing laboratory space and synthetic peptides. M. D. M. is a Fellow of The Jane Coffin Childs Memorial Fund for Medical Research. This investigation has been aided by a grant from The Jane Coffin Childs Memorial Fund for Medical Research. C. A. J. was sup. ported by an EMBO postdoctoral fellowship. This work was supported by National Institutes of Health grants GM28005 and GM38328 to S. I. R., who also acknowledges the support provided by American Cancer Society Faculty Research Award FRA-246. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.",

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Dual regulation of the yeast CDC28-p40 protein kinase complex: Cell cycle, pheromone, and nutrient limitation effects

Abstract

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