Related Experiment Video
Updated: May 28, 2026

06:29
Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells
Published on: July 30, 2020
Phosphorylation at serine 331 is required for Aurora B activation
Eleni Petsalaki1, Tonia Akoumianaki, Elizabeth J Black
1Department of Biology, University of Crete, Heraklion 71409, Greece.
The Journal of Cell Biology
|October 26, 2011
Summary
Checkpoint kinase 1 (Chk1) phosphorylates Aurora B kinase at Serine 331 (Ser331), fully activating its cell division function. This phosphorylation is crucial for accurate chromosome segregation and cell cycle progression.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Aurora B kinase is vital for successful cell division, regulating key mitotic events.
- Proper regulation of Aurora B kinase activity is essential to prevent errors in chromosome segregation.
Purpose of the Study:
- To investigate the role of Aurora B kinase phosphorylation at Serine 331 (Ser331) in regulating its activity.
- To identify the kinase responsible for Ser331 phosphorylation and its downstream effects on cell division.
Main Methods:
- Phosphorylation analysis of Aurora B at Ser331 during mitosis.
- Investigation of Chk1 kinase's role in Ser331 phosphorylation using taxol and nocodazole.
- Assessment of Aurora B(S331A) mutant effects on chromosome segregation, kinetochore-microtubule attachments, and mitotic delay.
Main Results:
- Aurora B is phosphorylated at Ser331 during mitosis, localizing to kinetochores.
- Chk1 kinase is essential for Ser331 phosphorylation, which is required for optimal INCENP phosphorylation, Survivin association, and full Aurora B activation.
- Mutating Ser331 to alanine (Aurora B(S331A)) causes chromosome missegregation, multinucleation, and impaired mitotic delay.
Conclusions:
- Chk1-mediated phosphorylation of Aurora B at Ser331 is a critical step for full Aurora B kinase activation.
- Ser331 phosphorylation is essential for accurate chromosome segregation and proper mitotic progression.
- This regulatory mechanism highlights a key pathway for controlling cell division fidelity.
Related Concept Videos
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...
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...
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...
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...
PI3K/mTOR/AKT Signaling Pathway
The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a rapamycin-insensitive companion...
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...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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...

