Open figure viewer
A monomeric myosin first spotted in electron micrographs almost 30 years ago has finally been united with a proposed function. Tyska and Mooseker (page 395) report that myosin-1A associates with and anchors a raft component in apical membranes.
Expression of a dominant-negative myosin-1A (green) results in loss of apical SI (red).
Myosin-1A was previously thought to shuttle Golgi-derived cargos to the plasma membrane (after most of the distance had been covered using microtubule-based motors). But the in vitro evidence for this came from undifferentiated cells, and in mature, polarized colon epithelial cells, Tyska and Mooseker see no evidence of shuttling by myosin-1A. What they did spot was cofractionation and cross-linking of myosin-1A with the transmembrane disaccharidase sucrase-isomaltase (SI). This raft protein is lost from the apical surface when a fragment of either myosin-1A or SI interferes with the link between the two full-length...
The Rockefeller University Press
2004
You do not currently have access to this content.
