Competition between two high- and low-affinity protein-binding sites in myosin VI controls its cellular function.

ABSTRACT: Myosin VI is involved in many cellular processes ranging from endocytosis to transcription. This multifunctional potential is achieved through alternative isoform splicing and through interactions of myosin VI with a diverse network of binding partners. However, the interplay between these two modes of regulation remains unexplored. To this end, we compared two different binding partners and their interactions with myosin VI by exploring the kinetic properties of recombinant proteins and their distribution in mammalian cells using fluorescence imaging. We found that selectivity for these binding partners is achieved through a high-affinity motif and a low-affinity motif within myosin VI. These two motifs allow competition among partners for myosin VI. Exploring how this competition affects

SUBMITTER: Fili N 

PROVIDER: S-EPMC6956527 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature