M. J. Tyska

This study shows MISP binds preferentially to ADP-actin filaments near their pointed ends, forming parallel bundles and modulating microvilli structure.

This study shows that intermicrovillar adhesion complexes stabilize nascent microvilli at epithelial cell margins through transjunctional interactions, leading to their accumulation in medial regions.

This study shows that myosin-generated force can drive protrusion growth, independent of cargo delivery or barbed end elongation factors.

The paper identifies MISP as an actin bundler that stabilizes microvillus rootlets and reveals its interaction with ezrin to maintain bundle structure.

This study uses live imaging to visualize microvillus biogenesis in epithelial cells, identifying key temporal steps and factors involved in their formation and collapse.

The paper develops a heterologous in-cell assay to study intermicrovillar adhesion complex interactions and function, revealing a mechanism for length matching of surface protrusions.

The paper presents X-ray structures of PCDH24 and CDHR5 extracellular domains and identifies species-specific adhesive units for homophilic and heterophilic interactions.

This study identifies non-muscle myosin-2C as a key regulator of microvilli length by controlling actin turnover in the terminal web.

This study identifies SETD2 as an actin lysine methyltransferase that regulates actin polymerization and cell migration through methylation of the actin cytoskeleton.

This study shows that PACSIN2 regulates microvilli morphology via apical endocytosis, with loss of PACSIN2 causing structural defects in intestinal brush borders.

This study shows that microvilli move actively during brush border formation, driven by actin dynamics, leading to their clustering and organization.