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Positive Regulator Molecules

Positive Regulator Molecules

Mitotic cell division results in daughter cells that exactly resemble the parent cell. However, errors in the DNA replication or distribution of genetic material may lead to genetic mutations that may be passed down to every new cell formed from the resulting abnormal cell. Propagation of such mutant cells is restricted through checkpoint mechanisms present at different stages of the cell cycle. These checkpoints involve regulator molecules that either promote or demote cell cycle events.

Positive Regulator Molecules

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To consistently produce healthy cells, the cell cycle—the process that generates daughter cells—must be precisely regulated.

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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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The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...

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Related Experiment Video

Updated: Jul 4, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Cell cycle-dependent phosphorylation of human CDC5 regulates RNA processing.

Remo Gräub¹, Hope Lancero, Anissa Pedersen

¹Cardiovascular Research Institute, University of California, San Francisco, CA 94143-0130, USA.

Cell Cycle (Georgetown, Tex.)

|June 28, 2008

Summary

CDC5L phosphorylation is crucial for pre-mRNA splicing, with specific CDK-dependent sites regulating this process. Targeting these sites offers potential cancer treatment strategies.

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Published on: September 17, 2012

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

CDC5 proteins are vital spliceosome components regulating cell cycle progression.
Human CDC5L has numerous potential phosphorylation sites, but their roles and regulators were unknown.

Purpose of the Study:

To identify CDC5L phosphorylation sites and determine their role in regulating CDC5L activity and pre-mRNA splicing.
To investigate the kinases responsible for CDC5L phosphorylation and their potential therapeutic implications.

Main Methods:

Two-dimensional phosphopeptide mapping and nanoelectrospray mass spectrometry to identify phosphorylation sites.
In vitro splicing assays to assess the functional impact of phosphorylation.
In vitro kinase assays and in vivo radiolabeling experiments using CDK2 inhibitor CVT-313.

Main Results:

CDC5L is phosphorylated on at least nine sites in vivo.
Phosphorylation is not required for CDC5L homodimerization or nuclear localization.
Phosphorylation at threonines 411 and 438 is essential for CDC5L-mediated pre-mRNA splicing.
CDK2 inhibition blocks CDC5L phosphorylation.

Conclusions:

This study demonstrates the regulatory role of CDC5L phosphorylation in pre-mRNA splicing.
Specific CDK-dependent phosphorylation sites on CDC5L are critical for its function.
Targeting CDC5L phosphorylation sites or associated kinases may offer new therapeutic avenues for cancer treatment.