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Related Experiment Video

Updated: Jun 23, 2026

Skeletal Phenotype Analysis of a Conditional Stat3 Deletion Mouse Model

Skeletal Phenotype Analysis of a Conditional Stat3 Deletion Mouse Model

Published on: July 3, 2020

Dynamin reduces Pyk2 Y402 phosphorylation and SRC binding in osteoclasts.

Angela Bruzzaniti¹, Lynn Neff, Amanda Sandoval

¹Department of Oral Biology, Indiana University School of Dentistry, 1121 W. Michigan St., DS241, Indianapolis, IN 46202-5186, USA. abruzzan@iupui.edu

Molecular and Cellular Biology

|April 22, 2009

Summary

Dynamin regulates cell adhesion by modulating the Pyk2-Src signaling pathway. This interaction, independent of dynamin

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Last Updated: Jun 23, 2026

Skeletal Phenotype Analysis of a Conditional Stat3 Deletion Mouse Model

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Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis

Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis

Published on: April 1, 2022

Area of Science:

Cell Biology
Molecular Signaling
Biochemistry

Background:

Podosomes are dynamic adhesion complexes crucial for highly motile cells like osteoclasts.
The Pyk2-Src-Cbl complex, downstream of integrins, regulates podosome assembly and dynamics.
Dynamin, a GTPase, is known to associate with podosomes and influence actin dynamics.

Purpose of the Study:

To investigate the interaction between dynamin and the Pyk2-Src signaling pathway.
To elucidate dynamin's role in regulating Pyk2 phosphorylation and Src binding.
To understand the implications of this regulation in cellular adhesion and signaling.

Main Methods:

Co-immunoprecipitation assays to study protein-protein interactions.
Analysis of tyrosine phosphorylation levels of Pyk2 and dynamin.
Overexpression studies of dynamin in osteoclastlike cells.
Site-directed mutagenesis of dynamin to assess the role of phosphorylation.

Main Results:

Dynamin associates with Pyk2 independently of its GTPase activity.
Dynamin reduces Pyk2 Y402 phosphorylation in a GTPase-dependent manner, decreasing Src binding.
Src kinase activity promotes dynamin-Pyk2 association, and dynamin modulates Pyk2 phosphorylation.

Conclusions:

Dynamin acts as a negative regulator in the Pyk2-Src signaling pathway downstream of integrins.
Src activation of a negative-feedback loop involving dynamin leads to Pyk2 Y402 dephosphorylation and Src dissociation.
This mechanism is critical for regulating podosome dynamics and cellular adhesion in motile cells.