Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Anaphase Promoting Complex00:50

Anaphase Promoting Complex

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...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
M-Cdk Drives Transition Into Mitosis02:15

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...
The Mitotic Spindle02:27

The Mitotic Spindle

The mitotic spindle—or spindle apparatus—is a eukaryotic, cytoskeletal structure made up of long protein fibers called microtubules. Formed during cell division, the spindle separates sister chromatids and moves them to opposite ends of a parental cell, where the now individual chromosomes are distributed to two daughter cell nuclei.
The bipolar configuration of the mitotic spindle facilitates chromosomal segregation, preparing the cell for division. One mechanism that ensures bipolar mitotic...
Separation of Sister Chromatids02:17

Separation of Sister Chromatids

At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
At the onset of anaphase, separase, a proteolytic enzyme, is...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Stress Granule Sequestration of CCR4-NOT Promotes Poly(A) Lengthening of Stress-Survival Transcripts.

bioRxiv : the preprint server for biology·2026
Same author

A conserved motif tunes Sidekick condensate dynamics to control tricellular junction recruitment during epithelial remodeling.

Cell reports·2026
Same author

Biomolecular condensates mediate C-N bond formation.

Nature chemical biology·2026
Same author

Origins of the Intrinsic Redox Activity of Biomolecular Condensates.

Journal of the American Chemical Society·2026
Same author

Biomolecular condensates sustain pH gradients at equilibrium through charge neutralization.

Nature chemistry·2026
Same author

Fast, Bright, and Reversible Fluorescent Labeling of Rhodamine-Binding Proteins.

Journal of the American Chemical Society·2025

Related Experiment Video

Updated: May 27, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

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

Published on: May 3, 2018

Systematic phosphorylation analysis of human mitotic protein complexes.

Björn Hegemann1, James R A Hutchins, Otto Hudecz

  • 1Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.

Science Signaling
|November 10, 2011
PubMed
Summary

Researchers mapped 1818 phosphorylation sites within mitotic protein complexes, identifying key regulatory subunits and potential kinase targets. This provides crucial insights into cell division regulation and signaling pathways.

More Related Videos

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Related Experiment Videos

Last Updated: May 27, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

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

Published on: May 3, 2018

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mitotic progression relies on protein complexes regulating chromosome segregation.
  • Mitotic protein kinases control these processes via phosphorylation.
  • Existing studies lack detailed information on phosphorylation site distribution and kinase-substrate relationships within mitotic complexes.

Purpose of the Study:

  • To systematically identify and map phosphorylation sites within mitotic protein complexes.
  • To investigate the distribution of these sites and identify potential kinase regulators.
  • To determine kinase dependency for specific phosphorylation events in key mitotic complexes.

Main Methods:

  • Systematic protein-affinity purification coupled with mass spectrometry.
  • Bioinformatic analyses to predict kinase-substrate relationships.
  • In-depth analysis using Aurora kinase B (AURKB) and Polo-like kinase 1 (PLK1) inhibitors.

Main Results:

  • Identified 1818 phosphorylation sites across over 100 mitotic protein complexes.
  • Observed concentrated phosphorylation on specific subunits, acting as signaling switchboards.
  • Determined kinase dependency for 172 phosphorylation sites on 41 proteins.
  • Identified 14 direct candidate substrates for AURKB or PLK1.

Conclusions:

  • This study provides a comprehensive map of mitotic phosphorylation sites and their regulators.
  • Identified key regulatory subunits within complexes that relay kinase signals.
  • Pinpointed direct substrates for AURKB and PLK1, advancing understanding of mitotic kinase signaling.