Multivalent glycan-protein binding events participate in various physiological functions including cell signaling, immune response, and pathogen-host recognition, among others. The complexity of these processes has driven sustained interest in developing densely functionalized glycan nanoassemblies to probe and modulate these important interactions. While synthetic glyconanomaterials have demonstrated significant promise in nanomedicine and biotechnology applications, achieving precise control over their architecture remains challenging.
View Article and Find Full Text PDFMyTH-FERM (MF) myosins are essential for filopodia formation in both Metazoa and Amoebozoa ( DdMyo7; mammalian Myo10) but their roles in filopodia formation are not fully understood. Taking advantage of a mutation in the highly conserved actin binding interface of another MF myosin, the () mutation of Myo15A that reduces its function, the impact of altering the myosin-F-actin interaction on filopodia formation was investigated. The mutation, a D to G substitution (Gong et al, 2022, Sci Adv), was introduced into DdMyo7 or Myo10 and filopodia formation assessed by quantitative analysis of number, length and myosin tip enrichment.
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