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M-Cdk Drives Transition Into Mitosis

M-Cdk Drives Transition Into Mitosis

Checkpoints throughout the cell cycle serve as safeguards and gatekeepers, allowing the cell cycle to progress in favorable conditions and slow or halt it in problematic ones. This regulation is known as the cell cycle control system.
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...

M-Cdk Drives Transition Into Mitosis

M-Cdk Drives Transition Into Mitosis

Checkpoints throughout the cell cycle serve as safeguards and gatekeepers, allowing the cell cycle to progress in favorable conditions and slow or halt it in problematic ones. This regulation is known as the cell cycle control system.
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...

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

Positive Regulator Molecules

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

Mitogens and the Cell Cycle

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...

Inhibition of Cdk Activity

Inhibition of Cdk Activity

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: Jun 26, 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 MAN1.

Yasuhiro Hirano¹, Yuka Iwase, Kohei Ishii

¹Graduate School of Biostudies, Kyoto University, Yoshida-konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan. hirano@lif.kyoto-u.ac.jp

|January 27, 2009

Summary

Mitotic phosphorylation of MAN1 proteins regulates their binding to BAF, a key factor in nuclear membrane targeting. This phosphorylation, particularly at Ser-402, is crucial for controlling MAN1-BAF interactions during the cell cycle.

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Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1

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Published on: February 25, 2016

Related Experiment Videos

Last Updated: Jun 26, 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

Studying Cell Cycle-regulated Gene Expression by Two Complementary Cell Synchronization Protocols

Studying Cell Cycle-regulated Gene Expression by Two Complementary Cell Synchronization Protocols

Published on: June 6, 2017

Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1

Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1

Published on: February 25, 2016

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

The LEM (LAP2beta, Emerin, and MAN1) protein family is vital for nuclear membrane association with chromatin.
This association is mediated by interactions with the barrier-to-autointegration factor (BAF).

Purpose of the Study:

To investigate the cell cycle-dependent phosphorylation of MAN1.
To elucidate the biological role of MAN1 phosphorylation, specifically its impact on BAF binding.

Main Methods:

Utilized a Xenopus egg cell-free system to study cell cycle-dependent phosphorylation.
Employed Titansphere column chromatography and MS/MS sequencing to identify phosphorylation sites.
Conducted in vitro BAF binding assays with MAN1 mutants.

Main Results:

MAN1 phosphorylation occurs in a cell cycle-dependent manner, particularly during M-phase.
Mitotic phosphorylation, especially at Ser-402 in the N-terminal region, inhibits MAN1 binding to BAF.
Identified M-phase-specific sites (Thr-209, Ser-351, Ser-402) and a cell cycle-independent site (Ser-463).

Conclusions:

MAN1 phosphorylation, particularly at Ser-402, is a critical regulatory mechanism for controlling MAN1-BAF interactions.
This regulation is essential for nuclear membrane targeting processes during the cell cycle.