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Structural Insights into the Altering Function of CRMP2 by Phosphorylation.

Takuya Sumi¹, Tsuyoshi Imasaki^1,2,3, Mari Aoki²

¹Division of Structural Medicine and Anatomy, Kobe University Graduate School of Medicine.

Cell Structure and Function

|February 27, 2018

Summary

Collapsin response mediator protein 2 (CRMP2) phosphorylation prevents axonal microtubule formation by disrupting its interaction with GTP-tubulin. This structural change inhibits neurite outgrowth and promotes growth cone collapse.

Keywords:

CRMP2 axon crystal structure microtubule phosphorylation

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Area of Science:

Neuroscience
Molecular Biology
Structural Biology

Background:

Collapsin response mediator protein 2 (CRMP2) is crucial for neuronal polarity and microtubule dynamics.
CRMP2 activity is modulated by phosphorylation, particularly at its C-terminal tail, affecting axonal growth and growth cone collapse.
Unphosphorylated CRMP2 promotes axonal microtubule formation, while phosphorylated CRMP2 inhibits it.

Purpose of the Study:

To elucidate the molecular mechanisms by which CRMP2 phosphorylation alters its structure and function.
To investigate how phospho-mimic CRMP2 affects its interaction with GTP-tubulin and microtubule formation.

Main Methods:

Biochemical analyses
Structural analyses (e.g., crystal structure determination)
Phospho-mimic CRMP2 studies

Main Results:

Phosphorylation induces subtle conformational changes in CRMP2's C-terminal tail, altering its surface charge.
These changes disrupt CRMP2's interaction with GTP-tubulin, preventing hetero-trimer formation.
Phospho-mimic CRMP2 loses its ability to induce and maintain axonal microtubule formation.

Conclusions:

CRMP2 phosphorylation is a key regulatory mechanism controlling neuronal polarity and axon development.
Structural alterations upon phosphorylation directly impair CRMP2's function in microtubule assembly.
Understanding these mechanisms provides insights into neuronal development and potential therapeutic targets.