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Related Experiment Video

Updated: Jun 6, 2025

Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases

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Published on: September 6, 2024

Making PI3K superfamily enzymes run faster.

Grace Q Gong¹, Madhangopal Anandapadamanaban², Md Saiful Islam²

¹MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK; University College London Cancer Institute, University College London, London, UK.

Advances in Biological Regulation

|November 26, 2024

Summary

The phosphoinositide 3-kinase (PI3K) superfamily

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Area of Science:

Biochemistry and Structural Biology
Molecular and Cellular Biology

Background:

The phosphoinositide 3-kinase (PI3K) superfamily encompasses lipid and protein kinases with low basal activity.
These kinases share a conserved C-terminal kinase domain and are regulated by various factors.

Purpose of the Study:

To review common structural features of the PI3K superfamily.
To explore how these features facilitate activation and potential therapeutic applications.

Main Methods:

Structural analysis of PI3K superfamily members.
Review of recent findings on PI3K activators and their mechanisms.

Main Results:

Activators reconfigure the kinase active site through subtle lobe realignment and PIKK regulatory domain (PRD) conformational changes.
A helical region transmits regulatory interactions, leading to active site realignment for enhanced catalysis.

Conclusions:

The PI3K superfamily's structural flexibility allows for activation by diverse factors.
Exploiting this flexibility could lead to specific activators for therapeutic uses in nerve regeneration, wound healing, and neurodegenerative diseases.