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Related Experiment Video

Updated: May 18, 2026

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

Published on: April 14, 2023

FAM123A binds to microtubules and inhibits the guanine nucleotide exchange factor ARHGEF2 to decrease actomyosin

Priscila F Siesser¹, Marta Motolese, Matthew P Walker

¹Department of Cell and Developmental Biology, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill School of Medicine, Chapel Hill, NC 27599, USA.

Science Signaling

|September 6, 2012

Summary

FAM123A protein binds microtubules via a SKIP motif, regulating cell migration and contractility. This differs from WTX and FAM123C, highlighting distinct roles within the FAM123 gene family.

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Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

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Area of Science:

Cell Biology
Molecular Biology
Genetics

Background:

The FAM123 gene family includes FAM123A, WTX (FAM123B), and FAM123C, with WTX known for its role in development and disease via WNT signaling.
The functions of FAM123A and FAM123C in cellular processes and human diseases are not well understood.

Purpose of the Study:

To compare the protein-protein interaction networks and cellular roles of FAM123A, WTX, and FAM123C.
To investigate the specific mechanisms by which FAM123A influences cell behavior.

Main Methods:

Affinity purification coupled with mass spectrometry to define protein interaction networks.
Protein localization studies and functional assays.
Domain interaction experiments to identify key motifs and binding partners.

Main Results:

FAM123A, but not WTX or FAM123C, interacts with microtubule-associated proteins and localizes to dynamic microtubules.
A novel "SKIP" motif in FAM123A mediates binding to EB1 and EB3, enabling microtubule association.
FAM123A depletion disrupts microtubule dynamics, increases actomyosin contractility, and reduces cell migration by inhibiting ARHGEF2.

Conclusions:

FAM123A utilizes a SKIP motif for microtubule binding and regulation of cellular functions distinct from other FAM123 members.
FAM123A coordinates microtubule dynamics and actomyosin contractility through its interaction with EB proteins and ARHGEF2.
These findings reveal specialized roles for FAM123A in cell behavior and provide insights into potential disease mechanisms.