Biology subjects

Boiero Sanders, M.

Publications and source records attributed to Boiero Sanders, M..

3 recordsLinked to original sources

bioRxiv2026

Molecular orchestration of global actin remodelling by INF2

The actin cytoskeleton rapidly reorganizes in response to intracellular calcium signals, driving cellular morphogenesis and wound healing. Among actin regulators, the formin INF2 uniquely mediates the "Calcium-mediated Actin Reset" (CaAR) reaction, orchestrating transient and global actin remodeling upon calcium influx. Excessive INF2 activity is linked to kidney and neuronal diseases, underscoring the need for its tight control. Combining live cell imaging with single molecule tracking, biochemistry and structural analysis we discover that INF2 activity is tightly controlled by two interlinked mechanisms: canonical intramolecular autoinhibition and binding of the INF2 N-terminus to the side of actin filaments. Side-binding limits actin elongation and supports re-establishment of autoinhibition. Disruption of this negative feedback prolongs INF2 activity, affecting plasma membrane organization and repair as well as transcriptional control. Our findings uncover a novel product-inhibition mechanism that limits INF2 function and offer important insight into disease mechanisms linked to actin dysregulation.

cell biology↗

bioRxiv2025

Streamlined Montage Cryo-Electron Tomography for Exploring the Ultrastructure of Cells and Tissues

Cryo-electron tomography reveals the architecture of biological specimens at molecular resolution, albeit with a limited field of view. Montage tomography overcomes this limitation, but existing strategies depend on complex dose distribution imaging schemes or hardware modifications which prevent widespread adoption of the method. To lower the barrier to entry, we developed a straightforward workflow that deviates minimally from conventional image acquisition and leverages our software MontageMaker to merge overlapping tilt series. The resulting montage tomograms are produced with high throughput, retain nanoscale detail despite the uneven accumulation of dose, and are easily acquired on a wide variety of biological samples. Most importantly, this approach can be implemented immediately by any lab with access to automated cryo-ET data collection.

cell biology↗

bioRxiv2021

Specialization of actin isoforms derived from the loss of key interactions with regulatory factors

A paradox of eukaryotic cells is that while some species assemble a complex actin cytoskeleton from a single ortholog, other species utilize a greater diversity of actin isoforms. The physiological consequences of using different actin isoforms, and the molecular mechanisms by which highly conserved actin isoforms are segregated into distinct networks, are poorly known. Here, we sought to understand how a simple biological system, composed of a unique actin and a limited set of actin-binding proteins, reacts to a switch to heterologous actin expression. Using yeast as a model system and biomimetic assays, we show that such perturbation causes drastic reorganization of the actin cytoskeleton. Our results indicate that defective interaction of a heterologous actin for important regulators of actin assembly limits certain actin assembly pathways while reinforcing others. Expression of two heterologous actin variants, each specialized in assembling a different network, rescues cytoskeletal organization and confers resistance to external perturbation. Hence, while species using a unique actin have homeostatic actin networks, actin assembly pathways in species using several actin isoforms may act more independently.

cell biology↗