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Myristoylation and membrane binding regulate c-Src stability and kinase activity.

Parag Patwardhan¹, Marilyn D Resh

¹Cell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.

Molecular and Cellular Biology

|June 30, 2010

Summary

Myristoylation positively regulates c-Src kinase activity and affects its stability and degradation. This contrasts with c-Abl, revealing distinct myristoylation roles in tyrosine kinases.

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Area of Science:

Biochemistry
Molecular Biology
Cell Signaling

Background:

Myristoylation is essential for Src kinase membrane association.
The role of myristate in regulating other aspects of Src biology remains unexplored.
In c-Abl tyrosine kinase, myristate binding induces an autoinhibitory conformation.

Purpose of the Study:

To investigate the regulatory role of myristoylation on c-Src kinase activity and stability.
To compare the myristoylation mechanism in c-Src with that of c-Abl.
To explore the impact of myristoylation on c-Src ubiquitination and degradation.

Main Methods:

Biochemical assays to measure kinase activity.
Analysis of protein stability and degradation pathways.
Site-directed mutagenesis of predicted myristate-binding pocket residues in c-Src.
Assessment of membrane binding and localization.

Main Results:

Myristoylation positively impacts c-Src kinase activity.
Nonmyristoylated c-Src shows reduced kinase activity but enhanced stability.
Myristoylation and membrane binding regulate c-Src ubiquitination and degradation.
Mutations in the predicted myristate-binding pocket decrease kinase activity, with T456A causing partial membrane release.

Conclusions:

Myristoylation positively regulates c-Src kinase activity, unlike its inhibitory role in c-Abl.
Myristoylation and membrane binding influence c-Src ubiquitination and degradation.
Specific residues in the predicted myristate-binding pocket are crucial for c-Src regulation, albeit differently than in c-Abl.