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Assaying Protein Kinase Activity with Radiolabeled ATP
Published on: May 26, 2017
Single-molecule detection of phosphorylation-induced plasticity changes during ezrin activation
Dan Liu1, Ling Ge, Fengsong Wang
1Division of Cellular Dynamics, Hefei National Laboratory for Physical Sciences, Hefei 230027, China.
FEBS Letters
|July 14, 2007
Summary
Phosphorylation of ezrin at T567 causes its N- and C-terminal domains to unfold, favoring inter-molecular association. This reveals the molecular mechanism of ezrin-radixin-moesin protein activation.
Area of Science:
- Cell biology
- Biophysics
- Molecular and structural biology
Background:
- The ezrin-radixin-moesin (ERM) protein family links the actin cytoskeleton to the plasma membrane.
- Phosphorylation of ezrin is crucial for membrane dynamics, but the activation mechanism is unclear.
Purpose of the Study:
- To elucidate the molecular mechanism of ezrin activation by T567 phosphorylation using single-molecule force spectroscopy.
Main Methods:
- Generated and purified phospho-mimicking and non-phosphorylatable ezrin mutants.
- Utilized atomic force microscopy (AFM) to probe single ezrin molecules.
- Measured mechanical unfolding forces of ezrin mutants.
Main Results:
- AFM revealed unfolding of N- and C-terminal domains upon T567 phosphorylation.
- T567 phosphorylation promotes inter-molecular association of ezrin.
- Force measurements quantified the mechanical changes associated with ezrin activation.
Conclusions:
- T567 phosphorylation induces a conformational change in ezrin, leading to its activation.
- Stimulus-induced protein conformational changes serve as a signaling mechanism in cellular dynamics.
- Provides molecular insights into ERM protein activation and cellular signaling.
