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            <funder>Funding for this work was provided by grants from the National Institutes of Health (F32GM117793 to K.M.D., F32GM116370 and K99GM123221 to M.K.D., R33CA235254 to R.F., and R35GM136428 to G.D.). The content of the manuscript is solely the responsibility of the authors and does not represent the official views of the funding agencies. This research was supported in part by the computational resources provided by the BioHPC facility located in the Lyda Hill Department of Bioinformatics, UT Southwestern Medical Center, TX, and the UT Southwestern Quantitative Live Microscopy Core Facility, a Shared Resource of the Harold C. Simmons Cancer Center, supported in part by an NCI Cancer Center Support Grants, 1P30 CA142543-01.</funder>
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                  <idno type="halauthorid">1649784-0</idno>
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              <idno type="doi">10.1016/j.isci.2025.112623</idno>
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              <p>A critical step in cell morphogenesis is the extension of actin-dense pseudopods, controlled by actin-binding proteins (ABPs). While this process is well-understood on glass coverslips, it is less so in compliant threedimensional environments. Here, we knocked out a series of ABPs in osteosarcoma cells and evaluated their effect on pseudopod extension on glass surfaces (2D) and in collagen gels (3D). Cells lacking the longest Arp3 gene variant, or with attenuated Arp2/3 activity, had the strongest reduction in pseudopod formation between 2D and 3D. This was largely due to reduced activity of the hybrid Arp2/3-vinculin complex, which was dispensable on glass. Our data suggests that concurrent formation of actin branches and nascent adhesions, supported by Arp2/3-vinculin interactions, is essential to form mechanically stable links between fibrous extracellular matrix and actin in 3D. This highlights how experiments on stiff, planar substrates may conceal actin architectural features that are essential for morphogenesis in 3D.</p>
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