Abstract

The dynein adaptor Bicaudal D2 (BicD2) recognizes cargo for dynein-dependent transport and links them to the dynein motor complex. BicD2-dependent transport pathways are important for brain and muscle development, and mutations in BicD2 cause neuromuscular and neurodegenerative diseases, including spinal muscular atrophy, which is the most prevalent genetic cause of death in infants. However, the molecular mechanism for cargo selection by BicD2 is unknown. Here, in order to obtain mechanistic insights into how BicD2 selects cargo, we have characterized the interaction between cargo adaptor Nup358, which is a protein subunit of the nuclear pore complex and BicD2, by mutagenesis approaches.

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