Myosin X and its motorless isoform differentially modulate dendritic spine development by regulating trafficking and retention of vasodilator-stimulated phosphoprotein.

Lin WH, Hurley JT, Raines AN, Cheney RE, Webb DJ
J Cell Sci. 2013 126 (Pt 20): 4756-68

PMID: 23943878 · PMCID: PMC3795341 · DOI:10.1242/jcs.132969

Myosin X (Myo10) is an unconventional myosin with two known isoforms: full-length (FL)-Myo10 that has motor activity, and a recently identified brain-expressed isoform, headless (Hdl)-Myo10, which lacks most of the motor domain. FL-Myo10 is involved in the regulation of filopodia formation in non-neuronal cells; however, the biological function of Hdl-Myo10 remains largely unknown. Here, we show that FL- and Hdl-Myo10 have important, but distinct, roles in the development of dendritic spines and synapses in hippocampal neurons. FL-Myo10 induces formation of dendritic filopodia and modulates filopodia dynamics by trafficking the actin-binding protein vasodilator-stimulated phosphoprotein (VASP) to the tips of filopodia. By contrast, Hdl-Myo10 acts on dendritic spines to enhance spine and synaptic density as well as spine head expansion by increasing the retention of VASP in spines. Thus, this study demonstrates a novel biological function for Hdl-Myo10 and an important new role for both Myo10 isoforms in the development of dendritic spines and synapses.

MeSH Terms (16)

Animals Cell Adhesion Molecules Cell Differentiation Dendritic Spines HEK293 Cells Hippocampus Humans Microfilament Proteins Myosins Phosphoproteins Protein Isoforms Protein Transport Pseudopodia Rats Synapses Transfection

Connections (1)

This publication is referenced by other Labnodes entities:

Links