Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases
Cheng, Aiyang ; Ross, Karen E. ; Kaldis, Philipp LU
and Solomon, Mark J.
(1999)
In Genes and Development
13(22).
p.2946-2957
- Abstract
Activating phosphorylation of cyclin-dependent protein kinases (CDKs) is necessary for their kinase activity and cell cycle progression. This phosphorylation is carried out by the Cdk-activating kinase (CAK); in contrast, little is known about the corresponding protein phosphatase. We show that type 2C protein phosphatases (PP2Cs) are responsible for this dephosphorylation of Cdc28p, the major budding yeast CDK. Two yeast PP2Cs, Ptc2p and Ptc3p, display Cdc28p phosphatase activity in vitro and in vivo, and account for ~90% of Cdc28p phosphatase activity in yeast extracts. Overexpression of PTC2 or PTC3 results in synthetic lethality in strains temperature-sensitive for yeast CAK1, and disruptions of PTC2 and PTC3 suppress the growth... (More)
Activating phosphorylation of cyclin-dependent protein kinases (CDKs) is necessary for their kinase activity and cell cycle progression. This phosphorylation is carried out by the Cdk-activating kinase (CAK); in contrast, little is known about the corresponding protein phosphatase. We show that type 2C protein phosphatases (PP2Cs) are responsible for this dephosphorylation of Cdc28p, the major budding yeast CDK. Two yeast PP2Cs, Ptc2p and Ptc3p, display Cdc28p phosphatase activity in vitro and in vivo, and account for ~90% of Cdc28p phosphatase activity in yeast extracts. Overexpression of PTC2 or PTC3 results in synthetic lethality in strains temperature-sensitive for yeast CAK1, and disruptions of PTC2 and PTC3 suppress the growth defect of a cak1 mutant. Furthermore, PP2C-like enzymes are the predominant phosphatases toward human Cdk2 in HeLa cell extracts, indicating that the substrate specificity of PP2Cs toward CDKs is evolutionarily conserved.
(Less)
- author
- Cheng, Aiyang
; Ross, Karen E.
; Kaldis, Philipp
LU
and Solomon, Mark J.
- publishing date
- 1999-12-17
- type
- Contribution to journal
- publication status
- published
- keywords
- Activating phosphorylation, Cdk-activating kinase (CAK), Cyclin-dependent kinase, Protein phosphatase type 2C
- in
- Genes and Development
- volume
- 13
- issue
- 22
- pages
- 2946 - 2957
- publisher
- Cold Spring Harbor Laboratory Press (CSHL)
- external identifiers
-
- pmid:10580002
- scopus:0032751695
- ISSN
- 0890-9369
- DOI
- 10.1101/gad.13.22.2946
- language
- English
- LU publication?
- no
- id
- b6414cdb-c979-4ca3-bfd9-3f3c0fab360f
- date added to LUP
- 2019-09-18 14:34:43
- date last changed
- 2024-04-16 20:46:13
@article{b6414cdb-c979-4ca3-bfd9-3f3c0fab360f,
abstract = {{<p>Activating phosphorylation of cyclin-dependent protein kinases (CDKs) is necessary for their kinase activity and cell cycle progression. This phosphorylation is carried out by the Cdk-activating kinase (CAK); in contrast, little is known about the corresponding protein phosphatase. We show that type 2C protein phosphatases (PP2Cs) are responsible for this dephosphorylation of Cdc28p, the major budding yeast CDK. Two yeast PP2Cs, Ptc2p and Ptc3p, display Cdc28p phosphatase activity in vitro and in vivo, and account for ~90% of Cdc28p phosphatase activity in yeast extracts. Overexpression of PTC2 or PTC3 results in synthetic lethality in strains temperature-sensitive for yeast CAK1, and disruptions of PTC2 and PTC3 suppress the growth defect of a cak1 mutant. Furthermore, PP2C-like enzymes are the predominant phosphatases toward human Cdk2 in HeLa cell extracts, indicating that the substrate specificity of PP2Cs toward CDKs is evolutionarily conserved.</p>}},
author = {{Cheng, Aiyang and Ross, Karen E. and Kaldis, Philipp and Solomon, Mark J.}},
issn = {{0890-9369}},
keywords = {{Activating phosphorylation; Cdk-activating kinase (CAK); Cyclin-dependent kinase; Protein phosphatase type 2C}},
language = {{eng}},
month = {{12}},
number = {{22}},
pages = {{2946--2957}},
publisher = {{Cold Spring Harbor Laboratory Press (CSHL)}},
series = {{Genes and Development}},
title = {{Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases}},
url = {{http://dx.doi.org/10.1101/gad.13.22.2946}},
doi = {{10.1101/gad.13.22.2946}},
volume = {{13}},
year = {{1999}},
}