Key result
Overexpression of FMNL1ɣ enhances cell adhesion and rescues migration in depleted cells, facilitating filamentous actin bundling independent of the FH2 domain.
Why the study?
Does FMNL1ɣ modulate actin bundling and cell migration in breast adenocarcinoma models?
Does FMNL1ɣ modulate actin bundling and cell migration in breast adenocarcinoma models?
FMNL1ɣ facilitates actin bundling and promotes cell migration in breast adenocarcinoma models, highlighting a novel actin-modifying function.
No immediate clinical implications; leaves open FMNL1 as a migration target pending in vivo studies.
The formin family of proteins contributes to spatiotemporal control of actin cytoskeletal rearrangements during motile cell activities. The FMNL subfamily exhibits multiple mechanisms of linear actin filament formation and organization. Here we report novel actin-modifying functions of FMNL1 in breast adenocarcinoma migration models. FMNL1 is required for efficient cell migration and its three isoforms exhibit distinct localization. Suppression of FMNL1 protein expression results in a significant impairment of cell adhesion, migration, and invasion. Overexpression of FMNL1ɣ, but not FMNL1β or FMNL1α, enhances cell adhesion independent of the FH2 domain and FMNL1ɣ rescues migration in cells depleted of all three endogenous isoforms. While FMNL1ɣ inhibits actin assembly in vitro, it facilitates bundling of filamentous actin independent of the FH2 domain. The unique interactions of FMNL1ɣ with filamentous actin provide a new understanding of formin domain functions and its effect on motility of diverse cell types suggest a broader role than previously realized.
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Miller et al. (2019) studied Breast adenocarcinoma. FMNL1ɣ overexpression vs. FMNL1β, FMNL1α, or endogenous depletion was evaluated on Cell adhesion, migration, invasion, and actin bundling. Overexpression of FMNL1ɣ enhances cell adhesion and rescues migration in depleted cells, facilitating filamentous actin bundling independent of the FH2 domain.
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