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The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Phosphorylation and dephosphorylation regulate APC/C(Cdh1) substrate degradation.

Kobi J Simpson-Lavy1, Drora Zenvirth1, Michael Brandeis1

  • 1a The Department of Genetics ; The Alexander Silberman Institute of Life Sciences; The Hebrew University of Jerusalem ; Jerusalem , Israel.

Cell Cycle (Georgetown, Tex.)
|August 8, 2015
PubMed
Summary
This summary is machine-generated.

The Anaphase Promoting Complex/Cyclosome (APC/C) regulates cell cycle progression. Constitutively active APC/C(Cdh1) drives mitotic exit and DNA re-replication, revealing new substrate degradation requirements like phosphorylation or dephosphorylation.

Keywords:
APC/C, Cdc5, Cdc14, Cdh1, Clb5, Dbf4, DNA replication, exit from mitosis, Pds1, substrate phosphorylation, yeast

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The Anaphase Promoting Complex/Cyclosome (APC/C) is a crucial ubiquitin ligase regulating the cell cycle.
  • APC/C activity is controlled by adaptor proteins, including Cdh1, which targets it for G1-specific activity.
  • The precise kinetics and requirements for APC/C(Cdh1)-mediated substrate degradation remain largely uncharacterized.

Purpose of the Study:

  • To investigate the consequences of constitutive APC/C(Cdh1) activation on cell cycle progression.
  • To identify novel requirements for the degradation of APC/C(Cdh1) substrates.
  • To explore the role of phosphorylation and dephosphorylation in APC/C(Cdh1) substrate targeting.

Main Methods:

  • Overexpression of a constitutively active Cdh1 mutant (CDH1(m11)) that bypasses inhibitory phosphorylation.
  • Analysis of mitotic exit in the absence of key regulatory pathways (FEAR and MEN).
  • Assessment of DNA re-replication in the absence of specific kinases (Cdc7).

Main Results:

  • Constitutive APC/C(Cdh1) activation induced mitotic exit independently of FEAR and MEN pathways.
  • Overactive APC/C(Cdh1) promoted DNA re-replication even without Cdc7 activity.
  • Substrate degradation by APC/C(Cdh1) exhibited differential requirements, with some substrates needing dephosphorylation (e.g., Pds1, Clb5) and others needing phosphorylation (e.g., Cdc5).

Conclusions:

  • Constitutively active APC/C(Cdh1) can override normal cell cycle checkpoints, leading to premature mitotic exit and re-replication.
  • APC/C(Cdh1) substrate degradation is a complex process influenced by the phosphorylation status of the substrates.
  • This study uncovers new regulatory mechanisms governing APC/C(Cdh1) function and substrate turnover essential for cell cycle control.