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Updated: Mar 6, 2026

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

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Tyr(less) kinase signaling during mitosis

Sabine Elowe1

  • 1a Department de Pédiatrie, Faculté de Medicine , Université Laval, Axe de Réproduction, Santé de la Mère et de l'enfant, Centre de Rechereche du CHU de Québec , Québec , QC , Canada.

Cell Cycle (Georgetown, Tex.)
|March 16, 2017
PubMed

Insights

Tyrosine phosphorylation, a rare cell modification, plays a key role in cell division. Recent studies reveal its significant involvement in mitotic progression and spindle formation, challenging previous assumptions.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Tyrosine phosphorylation constitutes a small fraction (0.5%) of cellular phosphorylations.
  • Mitogenic tyrosine kinase signaling is well-studied, but its role in the cell cycle, especially mitosis, remains unclear.

Purpose of the Study:

  • To investigate the role and extent of tyrosine phosphorylation during cell division (mitosis).
  • To identify regulators of mitotic progression and spindle formation involving phosphotyrosine signaling.

Main Methods:

  • Analysis of mitotic phosphoproteomics data sets.
  • Identification of protein tyrosine phosphatases involved in mitotic regulation.

Main Results:

  • Tyrosine phosphorylation is more extensive during mitosis than previously thought.
  • Protein tyrosine phosphatases are crucial regulators of mitotic progression and spindle formation.

Conclusions:

  • Tyrosine phosphorylation plays a more active and significant role in mitosis than previously appreciated.
  • These findings open new avenues for understanding cell cycle regulation and potential therapeutic targets.
Keywords:
kinetochoremitosisphosphotyrosineproteomicsspindle

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