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Polar gradients of the DYRK-family kinase Pom1 couple cell length with the cell cycle

Cells normally grow to a certain size before they enter mitosis and divide. Entry into mitosis depends on the activity of Cdk1, which is inhibited by the Wee1 kinase and activated by the Cdc25 phosphatase. However, how cells sense their size for mitotic commitment remains unknown. Here we show that... Full description

Journal Title: Nature 2009, Vol.459 (7248), p.852-856
Main Author: Martin, Sophie G
Other Authors: Berthelot-Grosjean, Martine
Format: Electronic Article Electronic Article
Language: English
Subjects:
ras
Publisher: London: Nature Publishing Group
ID: ISSN: 0028-0836
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recordid: cdi_hal_primary_oai_HAL_hal_00816838v1
title: Polar gradients of the DYRK-family kinase Pom1 couple cell length with the cell cycle
format: Article
creator:
  • Martin, Sophie G
  • Berthelot-Grosjean, Martine
subjects:
  • Arctic research
  • Biological and medical sciences
  • Cell Cycle
  • Cell Cycle - physiology
  • Cell Cycle Proteins
  • Cell Cycle Proteins - antagonists & inhibitors
  • Cell Cycle Proteins - metabolism
  • Cell cycle, cell proliferation
  • cell division
  • cell length
  • Cell physiology
  • Cell Polarity
  • Cellular Biology
  • enzyme inhibitors
  • Fundamental and applied biological sciences. Psychology
  • Fungal Proteins
  • Fungal Proteins - metabolism
  • G2 Phase
  • Genetic aspects
  • Life Sciences
  • Mitosis
  • Molecular and cellular biology
  • Nuclear Proteins
  • Nuclear Proteins - antagonists & inhibitors
  • Nuclear Proteins - metabolism
  • Phosphorylation
  • Physiological aspects
  • Protein
  • Protein Kinases
  • Protein Kinases - metabolism
  • protein phosphorylation
  • Protein Transport
  • Protein-Serine-Threonine Kinases
  • Protein-Serine-Threonine Kinases - antagonists & inhibitors
  • Protein-Serine-Threonine Kinases - metabolism
  • Protein-Tyrosine Kinases
  • Protein-Tyrosine Kinases - antagonists & inhibitors
  • Protein-Tyrosine Kinases - metabolism
  • ras
  • ras-GRF1
  • ras-GRF1 - metabolism
  • Schizosaccharomyces
  • Schizosaccharomyces - cytology
  • Schizosaccharomyces - metabolism
  • Schizosaccharomyces pombe
  • Schizosaccharomyces pombe Proteins
  • Schizosaccharomyces pombe Proteins - antagonists & inhibitors
  • Schizosaccharomyces pombe Proteins - metabolism
  • Serine
  • Threonine Kinases
  • tyrosine
  • Tyrosine Kinases
  • yeasts
ispartof: Nature, 2009, Vol.459 (7248), p.852-856
description: Cells normally grow to a certain size before they enter mitosis and divide. Entry into mitosis depends on the activity of Cdk1, which is inhibited by the Wee1 kinase and activated by the Cdc25 phosphatase. However, how cells sense their size for mitotic commitment remains unknown. Here we show that an intracellular gradient of the dual-specificity tyrosine-phosphorylation regulated kinase (DYRK) Pom1, which emanates from the ends of rod-shaped Schizosaccharomyces pombe cells, serves to measure cell length and control mitotic entry. Pom1 provides positional information both for polarized growth and to inhibit cell division at cell ends. We discovered that Pom1 is also a dose-dependent G2-M inhibitor. Genetic analyses indicate that Pom1 negatively regulates Cdr1 and Cdr2, two previously described Wee1 inhibitors of the SAD kinase family. This inhibition may be direct, because in vivo and in vitro evidence suggest that Pom1 phosphorylates Cdr2. Whereas Cdr1 and Cdr2 localize to a medial cortical region, Pom1 forms concentration gradients from cell tips that overlap with Cdr1 and Cdr2 in short cells, but not in long cells. Disturbing these Pom1 gradients leads to Cdr2 phosphorylation and imposes a G2 delay. In short cells, Pom1 prevents precocious M-phase entry, suggesting that the higher medial Pom1 levels inhibit Cdr2 and promote a G2 delay. Thus, gradients of Pom1 from cell ends provide a measure of cell length to regulate M-phase entry.
language: eng
source:
identifier: ISSN: 0028-0836
fulltext: no_fulltext
issn:
  • 0028-0836
  • 1476-4687
url: Link


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descriptionCells normally grow to a certain size before they enter mitosis and divide. Entry into mitosis depends on the activity of Cdk1, which is inhibited by the Wee1 kinase and activated by the Cdc25 phosphatase. However, how cells sense their size for mitotic commitment remains unknown. Here we show that an intracellular gradient of the dual-specificity tyrosine-phosphorylation regulated kinase (DYRK) Pom1, which emanates from the ends of rod-shaped Schizosaccharomyces pombe cells, serves to measure cell length and control mitotic entry. Pom1 provides positional information both for polarized growth and to inhibit cell division at cell ends. We discovered that Pom1 is also a dose-dependent G2-M inhibitor. Genetic analyses indicate that Pom1 negatively regulates Cdr1 and Cdr2, two previously described Wee1 inhibitors of the SAD kinase family. This inhibition may be direct, because in vivo and in vitro evidence suggest that Pom1 phosphorylates Cdr2. Whereas Cdr1 and Cdr2 localize to a medial cortical region, Pom1 forms concentration gradients from cell tips that overlap with Cdr1 and Cdr2 in short cells, but not in long cells. Disturbing these Pom1 gradients leads to Cdr2 phosphorylation and imposes a G2 delay. In short cells, Pom1 prevents precocious M-phase entry, suggesting that the higher medial Pom1 levels inhibit Cdr2 and promote a G2 delay. Thus, gradients of Pom1 from cell ends provide a measure of cell length to regulate M-phase entry.
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subjectArctic research ; Biological and medical sciences ; Cell Cycle ; Cell Cycle - physiology ; Cell Cycle Proteins ; Cell Cycle Proteins - antagonists & inhibitors ; Cell Cycle Proteins - metabolism ; Cell cycle, cell proliferation ; cell division ; cell length ; Cell physiology ; Cell Polarity ; Cellular Biology ; enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins ; Fungal Proteins - metabolism ; G2 Phase ; Genetic aspects ; Life Sciences ; Mitosis ; Molecular and cellular biology ; Nuclear Proteins ; Nuclear Proteins - antagonists & inhibitors ; Nuclear Proteins - metabolism ; Phosphorylation ; Physiological aspects ; Protein ; Protein Kinases ; Protein Kinases - metabolism ; protein phosphorylation ; Protein Transport ; Protein-Serine-Threonine Kinases ; Protein-Serine-Threonine Kinases - antagonists & inhibitors ; Protein-Serine-Threonine Kinases - metabolism ; Protein-Tyrosine Kinases ; Protein-Tyrosine Kinases - antagonists & inhibitors ; Protein-Tyrosine Kinases - metabolism ; ras ; ras-GRF1 ; ras-GRF1 - metabolism ; Schizosaccharomyces ; Schizosaccharomyces - cytology ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe ; Schizosaccharomyces pombe Proteins ; Schizosaccharomyces pombe Proteins - antagonists & inhibitors ; Schizosaccharomyces pombe Proteins - metabolism ; Serine ; Threonine Kinases ; tyrosine ; Tyrosine Kinases ; yeasts
ispartofNature, 2009, Vol.459 (7248), p.852-856
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descriptionCells normally grow to a certain size before they enter mitosis and divide. Entry into mitosis depends on the activity of Cdk1, which is inhibited by the Wee1 kinase and activated by the Cdc25 phosphatase. However, how cells sense their size for mitotic commitment remains unknown. Here we show that an intracellular gradient of the dual-specificity tyrosine-phosphorylation regulated kinase (DYRK) Pom1, which emanates from the ends of rod-shaped Schizosaccharomyces pombe cells, serves to measure cell length and control mitotic entry. Pom1 provides positional information both for polarized growth and to inhibit cell division at cell ends. We discovered that Pom1 is also a dose-dependent G2-M inhibitor. Genetic analyses indicate that Pom1 negatively regulates Cdr1 and Cdr2, two previously described Wee1 inhibitors of the SAD kinase family. This inhibition may be direct, because in vivo and in vitro evidence suggest that Pom1 phosphorylates Cdr2. Whereas Cdr1 and Cdr2 localize to a medial cortical region, Pom1 forms concentration gradients from cell tips that overlap with Cdr1 and Cdr2 in short cells, but not in long cells. Disturbing these Pom1 gradients leads to Cdr2 phosphorylation and imposes a G2 delay. In short cells, Pom1 prevents precocious M-phase entry, suggesting that the higher medial Pom1 levels inhibit Cdr2 and promote a G2 delay. Thus, gradients of Pom1 from cell ends provide a measure of cell length to regulate M-phase entry.
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abstractCells normally grow to a certain size before they enter mitosis and divide. Entry into mitosis depends on the activity of Cdk1, which is inhibited by the Wee1 kinase and activated by the Cdc25 phosphatase. However, how cells sense their size for mitotic commitment remains unknown. Here we show that an intracellular gradient of the dual-specificity tyrosine-phosphorylation regulated kinase (DYRK) Pom1, which emanates from the ends of rod-shaped Schizosaccharomyces pombe cells, serves to measure cell length and control mitotic entry. Pom1 provides positional information both for polarized growth and to inhibit cell division at cell ends. We discovered that Pom1 is also a dose-dependent G2-M inhibitor. Genetic analyses indicate that Pom1 negatively regulates Cdr1 and Cdr2, two previously described Wee1 inhibitors of the SAD kinase family. This inhibition may be direct, because in vivo and in vitro evidence suggest that Pom1 phosphorylates Cdr2. Whereas Cdr1 and Cdr2 localize to a medial cortical region, Pom1 forms concentration gradients from cell tips that overlap with Cdr1 and Cdr2 in short cells, but not in long cells. Disturbing these Pom1 gradients leads to Cdr2 phosphorylation and imposes a G2 delay. In short cells, Pom1 prevents precocious M-phase entry, suggesting that the higher medial Pom1 levels inhibit Cdr2 and promote a G2 delay. Thus, gradients of Pom1 from cell ends provide a measure of cell length to regulate M-phase entry.
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