PhD-trained scientists are essential contributors to the workforce in diverse employment sectors that include academia, industry, government, and nonprofit organizations. Hence, best practices for training the future biomedical workforce are of national concern. Complementing coursework and laboratory research training, many institutions now offer professional training that enables career exploration and develops a broad set of skills critical to various career paths.
View Article and Find Full Text PDFPalladin is a widely expressed protein found in stress fibers, focal adhesions, growth cones, Z-discs, and other actin-based subcellular structures. It belongs to a small gene family that includes the Z-disc proteins myopalladin and myotilin, all of which share similar Ig-like domains. Recent advances have shown that palladin shares with myotilin the ability to bind directly to F-actin, and to crosslink actin filaments into bundles, in vitro.
View Article and Find Full Text PDFPalladin is a widely expressed phosphoprotein that plays an important role in organizing the actin cytoskeleton. Palladin is concentrated in multiple actin-based structures involved in cell motility and adhesion, including stress fibers, focal adhesions, cell-cell junctions, growth cones and Z-discs. Here, we show that palladin also localizes to the dorsal, circular ruffles that form transiently in response to growth factor stimulation.
View Article and Find Full Text PDFThe dynamic remodeling of the actin cytoskeleton plays a critical role in cellular morphogenesis and cell motility. Actin-associated scaffolds are key to this process, as they recruit cohorts of actin-binding proteins and associated signaling complexes to subcellular sites where remodeling is required. This review is focused on a recently discovered family of three proteins, myotilin, palladin, and myopalladin, all of which function as scaffolds that regulate actin organization.
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