When two kinases go for a dance

Authors

DOI:

https://doi.org/10.25250/thescbr.brk788

Keywords:

chemistry, Molecular Movies, kinases, Molecular Dynamics, P38a

Abstract

Phosphorylation is a fundamental mechanism in eukaryotic cells that allows signals to propagate. Kinases orchestrate this process by phosphorylating proteins to modulate their activity. Our work reveals the architecture of the complex between two key players of the mitogen-activated protein kinase signaling pathway, p38α and MKK6, while also giving an idea of what happens when the two come together.

Author Biographies

Ioannis Galdadas, University of Geneva

Postdoctoral Research Fellow

Francesco Luigi Gervasio, University of Geneva

Professor

Pauline Juyoux, IBS Grenoble

Postdoctoral Research Fellow

Original article reference

Juyoux, P., Galdadas, I., Gobbo, D., von Velsen, J., Pelosse, M., Tully, M., Vadas, O., Gervasio, F. L., Pellegrini, E., & Bowler, M. W. (2023). Architecture of the MKK6-p38a complex defines the basis of MAPK specificity and activation. Science, 381(6663), 1217–1225. https://doi.org/10.1126/science.add7859

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Published

2024-08-29

Issue

Vol. 10 No. 3 (2024): TheScienceBreaker

Section

Health & Physiology

License

Some rights reserved 2024 Ioannis Galdadas, Francesco Luigi Gervasio, Pauline Juyoux

Creative Commons License

This work is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.