Publications by authors named "B L Nolen"
Article Synopsis
- The Arp2/3 complex is crucial for forming branched actin filaments that support cellular processes like endocytosis and cell movement.
- Researchers found that specific mutations in the budding yeast Arp2/3 complex affect how effectively a WASP family protein (Las17) binds to the complex, which is necessary for optimal activation of actin networks.
- While disrupted binding sites still allow for some actin formation, yeast cells exhibit impaired functions, like decreased membrane internalization, indicating that both binding sites are important for creating effective actin structures, despite some residual activity in the complex.
Actin-related protein 2/3 complex (Arp2/3 complex) catalyzes the nucleation of branched actin filaments that push against membranes in processes like cellular motility and endocytosis. During activation by WASP proteins, the complex must bind WASP and engage the side of a pre-existing (mother) filament before a branched filament is nucleated. Recent high-resolution structures of activated Arp2/3 complex revealed two major sets of activating conformational changes.
View Article and Find Full Text PDFDendrite morphogenesis is essential for neural circuit formation, yet the molecular mechanisms underlying complex dendrite branching remain elusive. Previous studies on the highly branched PVD sensory neuron identified a membrane co-receptor complex that links extracellular signals to intracellular actin remodeling machinery, promoting high-order dendrite branching. In this complex, the claudin-like transmembrane protein HPO-30 recruits the WAVE regulatory complex (WRC) to dendrite branching sites, stimulating the Arp2/3 complex to polymerize actin.
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- Fragmentation ion spectral analysis is a key technique in proteomics for studying protein interactions and structures, and Kojak version 2.0 is an updated tool designed for identifying cross-linked peptides from these analyses.
- The new version includes improved algorithms, better scoring metrics, support for cleavable cross-linkers, and the ability to identify cross-links in specific protein structures, making it more versatile in experimental setups.
- Kojak 2.0 integrates with the Trans-Proteomic Pipeline for additional analytical tools and remains open-source and compatible across multiple platforms.
Arp2/3 complex nucleates branched actin filaments that provide pushing forces to drive cellular processes such as lamellipodial protrusion and endocytosis. Arp2/3 complex is intrinsically inactive, and multiple classes of nucleation promoting factors (NPFs) stimulate its nucleation activity. When activated by WASP family NPFs, the complex must bind to the side of a preexisting (mother) filament of actin to complete the nucleation process, ensuring that WASP-mediated activation creates branched rather than linear actin filaments.
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