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Actin filament- and Wiskott-Aldrich syndrome protein-binding sites on fructose-1,6-bisphosphate aldolase are functionally distinct from the active site

Cytoskeleton (Hoboken). 2020-11; 
Maggie H Hui, Kevin Rhine, Dean R Tolan
Products/Services Used Details Operation
PCR Cloning and Subcloning … Primers for site-directed mutagenesis, cloning, and sequencing were synthesized by Eurofins MWG Operon (Louisville, KY) and are listed in Supplemental Table 1. Peptides were synthesized by Genscript (Piscataway, NJ) and are listed in Supplemental Table 2. Q5 High … Get A Quote

摘要

The glycolytic enzyme fructose 1,6-(bis)phosphate aldolase (aldolase) is not only required for efficient utilization of glucose and fructose, but also for cytoskeletal functions like cytokinesis and cell motility. These differing roles are mediated by distinct and discrete binding interactions with aldolase's many binding partners, including actin filaments, Wiskott-Aldrich Syndrome protein (WASP), and Sorting Nexin 9 (SNX9). How these interactions are coordinated on the aldolase homotetramer of 160 kDa is unclear. In this study, the catalytic activity of wild-type aldolase is measured in the presence of actin filaments, and a WASP-derived peptide that binds to aldolase, or both. No appreciable changes in k o... More

关键词

Aldolase, WASP protein, actin, fluorescence anisotropy, glycolysis, kinetics, sorting Nexin