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Related Experiment Video

Updated: Jun 4, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

GEFH1 binds ASAP1 and regulates podosome formation.

Yoko Shiba¹, Paul A Randazzo

¹Laboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health, Bldg 37 Room 2042, Bethesda, MD 20892, United States.

Biochemical and Biophysical Research Communications

|March 1, 2011

Summary

Guanyl nucleotide exchange factor H1 (GEFH1) negatively regulates podosome assembly by interacting with ASAP1, a protein crucial for invadopodia formation and tumor invasion.

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Area of Science:

Cell Biology
Molecular Biology
Cancer Research

Background:

Invadopodia are key cellular structures implicated in tumor cell invasion.
ASAP1, an Arf GTPase-activating protein (GAP), is essential for invadopodia and podosome assembly.
Podosomes are Src-induced structures related to invadopodia.

Purpose of the Study:

To identify proteins interacting with the ASAP1 BAR domain.
To elucidate the role of GEFH1 in podosome formation and function.

Main Methods:

Two-hybrid screening to identify ASAP1 binding partners.
Immunoprecipitation to validate endogenous GEFH1-ASAP1 interaction.
siRNA to reduce GEFH1 expression.
Microscopy to assess podosome assembly and colocalization.

Main Results:

GEFH1 was identified as a binding partner of the ASAP1 BAR domain.
GEFH1 colocalized with ASAP1 in podosomes.
Overexpression of GEFH1 inhibited podosome assembly and ASAP1 GAP activity.
Reduced GEFH1 expression increased podosome assembly rate but did not affect matrix degradation.

Conclusions:

GEFH1 acts as a negative regulator of podosome assembly.
The interaction between GEFH1 and ASAP1 is critical for regulating podosome dynamics.