Claude Prigent

Centre national de la recherche scientifique Morocco

Claude Prigent received his PhD degree in Biology at the University in Rennes 1, France, studying DNA ligases in the laboratory of Pr. Michel Philippe. He then worked on DNA repair mechanisms at the Imperial Cancer Research Fund laboratories at South Mimms, London, England, in the laboratory of Pr. Thomas Lindahl. He got a permanent position in the CNRS (French National Center for Scientific Research) just after his postdoc in 1993. He established his own research group in 1996 in Rennes with the main objective on studying the regulation of cell cycle progression by protein kinases with a particular focus on mitosis. His team is also deeply engaged in cancer research trying to understand how deregulated kinases participate in carcinogenesis.

1books edited

2chapters authored

Latest work with IntechOpen by Claude Prigent

Protein phosphorylation reactions are carried out in a cell by protein kinases, which predominantly use ATP as a phosphate donor that is transferred and covalently bound to an amino acid on a substrate protein. Protein phosphorylation was discovered in 1954 by Edmond Fischer who shared the Nobel Prize in Medicine or Physiology in 1992 with Edwin Krebs. There are so many kinases that one was called "Just Another Kinase" for JAK kinase. Their counterpart is protein phosphatases that remove phosphates from phosphorylated proteins. Kinases and phosphatases act as switches in the cell that activates or inactivates protein functions. These reactions are reversible; the cell can quickly react to a situation but can then go back to its initial state.

Go to the book

Protein Phosphorylation

Edited by Claude Prigent

Chapters authored

Sister Chromatid Cohesion and Aneuploidy

By Erwan Watrin and Claude Prigent

Part of the book: Aneuploidy in Health and Disease

Regulation of Aurora Kinases and Their Activity

By Lucie Vaufrey, Arun Prasath Damodaran, Olivia Gavard, Stéphanie Le Bras and Claude Prigent

The three mitotic protein kinases Aurora-A, B and C are complementary enzymes that regulate multiple mitotic events. To do so, the different kinases must be locally activated, and the control of their activity is tightly regulated in time and space during mitosis. For instance, Aurora-A is first active at the centrosomes, then on microtubules at the spindle pole, Aurora-B is active in the nucleus, then at chromosome kinetochores and later one at the midbody. Aurora kinase activity is regulated in space and time by locally binding to regulators. Aurora kinases must bind to protein partners to be activated. Aurora-A for instance binds to targeting protein for Xenopus kinesin-like protein 2 (TPX2) and is activated at the spindle pole, Aurora-B and Aurora-C to INner CENtromer Protein (INCENP) and is activated on the chromosomes. These activations go through an autophosphorylation of a threonine residue in the T-loop of the kinase. Other protein partners are using different mechanisms to activate Auroras. These allow activation of the kinase at different time and location in the cell. This review is an up-to-date list of regulators of Aurora kinases. The subcellular localization of these regulators explains the presence of an active Aurora kinase. It also explains the changes in the localizations of the Aurora kinases activity observed during cell cycle progression in mitosis. Aurora kinases have been recently reported to be involved in nonmitotic events, and the identity of their activators in these events must be searched.

Part of the book: Protein Phosphorylation

Claude Prigent

Latest work with IntechOpen by Claude Prigent

Protein Phosphorylation

Chapters authored

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