Articles tagged with Actin Polymerization
Researchers at Aarhus University equip artificial cells with tiny motors mimicking the bacterium's actin polymerization mechanism, creating a functional internal skeleton and network of protein filaments. The study demonstrates how motion and structural organization can emerge in synthetic systems.
Dendritic cells assemble central actin structure to push obstacles away, generating space for migration. Mutations in Dock8 gene lead to severe immune disorder symptoms.
Researchers analyzed three distinct formins from fungi, mice, and humans, revealing a new paradigm in actin filament assembly. The structures show that formins encircle actin like an asymmetric ring, with one half stably bound and the other half loosely associated.
Researchers at Max Planck Institute of Molecular Physiology developed an innovative imaging technique to visualize the cardiac thick filament in its native environment. The resulting high-resolution image reveals new insights into the molecular organization and function of the sarcomere, a crucial component of heart muscle contraction.
The discovery sheds light on the mechanism of phosphate release from actin filaments, which is crucial for cell movement and disassembly. The researchers found that phosphate escapes through a molecular backdoor in the filament core, but the door remains closed for most of the time.
Researchers at City University of Hong Kong identified lysyl hydroxylase 1 (LH1) as a key factor in promoting confined migration of liver and pancreatic cancer cells. The study found that LH1 promotes metastasis by stabilizing Septin2, which enhances the actin network.
Researchers discovered that toxins produced by Vibrio bacteria hijack cell processes, redirecting key proteins into "roads to nowhere". This abnormal filament formation wastes cell resources and raises questions about its potential role or necessity.
A new study in Nature provides high-resolution structures showing how two key biochemical states of actin work jointly with bending forces to determine how actin can interact with other proteins. The research reveals a model of protein regulation that involves biochemical states and force working in concert.
Scientists have elucidated the regulatory functions of Pan1p, a key player in late-stage clathrin-mediated endocytosis. The protein drives actin assembly and disassembly, facilitating vesicle internalization.
Lillian Fritz-Laylin is a recipient of the Pew Scholars Program in Biomedical Sciences, which includes four years of funding to investigate complex mechanisms of biology. Her research focuses on understanding how cells deploy actin for various functions, with implications for disease prevention and progression.
Researchers have developed an assay that visualizes the formation of clathrin-coated vesicles at single clathrin-coated pits with high time resolution. This breakthrough sheds light on fundamental questions about clathrin-mediated endocytosis, including whether single coated pits give rise to multiple vesicles.