Excited to see our fascin paper on the cover of the May issue of @natsmb.nature.com! Although we can claim zero credit for the charming carrot design.

This mediates the formation of cooperative cadherin-catenin complex clusters along individual actin filament strands, which are associated with filament curvature. It will be interesting to see if similar assemblies form in cell-cell adhesions where forces are large, e.g. tricellular junctions.

A couple key take homes: A segment of afadin’s coiled-coil domain bridges adjacent α-catenin actin binding domains along actin filaments, binding and stabilizing flexible parts of α-catenin implicated in mechanical regulation of adhesion.

After revision in response to very constructive reviewer comments, the paper features additional evidence that zyxin and other LIM proteins form force-dependent assemblies which lack underlying F-actin. Figuring out how these come together is the next frontier.

Congrats to all co-authors, and thanks again to the Bidone lab for a fantastic collaboration.

The main addition to our preprint is analyzing actin’s helical twist, which is not altered in our bundles. This suggests changing filament structure is not a primary mechanism for accommodating geometric mismatch between helical filaments and hexagonal bundles in our preparations. bit.ly/3uorbNn

Please also see this nice summary by @rockefelleruniv.bsky.social : bit.ly/3PKErmA . In addition to addressing the longstanding biophysical mystery of actin bundle assembly, we hope our work will be useful for developing optimized fascin inhibitors showing promise as cancer therapeutics.

Excited that the peer-reviewed version of our fascin structure paper is now out in NSMB. Thanks very much to the referees for their constructive feedback. rdcu.be/d6Tct