WebSpindly’s N-terminal coiled-coil uses distinct motifs to bind dynein light intermediate chain and the pointed-end complex of dynactin. Mutations in these motifs inhibit assembly of a dynein–dynactin–Spindly complex, and a null mutant of the dynactin pointed-end subunit p27 prevents kinetochore recruitment of dynein–dynactin without ... WebPhosphorylation and Pin1 binding to the LIC1 subunit selectively regulate mitotic dynein functions ... Dynein Light Intermediate Chains as …
Stork: The meiotic LINC complex component KASH5 is an …
WebNov 23, 2024 · In future work it will be important to demonstrate that autoinhibition and its subsequent reversal by multivalent dynein light chain binding is a conserved process of IC among species and determine how this autoinhibition affects dynein function. ... (heavy chain), LIC (dynein light intermediate chain), N-IC (N-terminal domain of IC), C-IC, … WebMay 20, 2024 · Adaptor binding is governed by the homologous dynein light intermediate chain subunits LIC1 (DYNC1LI1) and LIC2 (DYNC1LI2), which exist in mutually … dave harmon plumbing goshen ct
Structure of the dynein-2 complex and its assembly …
WebJun 5, 2024 · Cytoplasmic dynein plays crucial roles in the intracellular transport of organelles and other cargoes. Central to dynein function is the intrinsically disordered N-terminal domain of dynein intermediate chain (IC), which binds the three dimeric dynein light chains at multivalent sites, and dynactin p150 Glued and nuclear distribution … WebCytoplasmic dynein and dynactin are megadalton-sized multisubunit molecules that function together as a cytoskeletal motor. In the present study, we explore the mechanism of dynein-dynactin binding in vitro and then extend our findings to an in vivo context. Solution binding assays were used to define binding domains in the dynein intermediate chain (IC) and … WebOct 1, 2014 · Cytoplasmic dynein, a microtubule-based motor protein, transports many intracellular cargos by means of its light intermediate chain (LIC). In this study, we have determined the crystal structure of the conserved LIC domain, which binds the motor heavy chain, from a thermophilic fungus. We show that … dave harman facebook