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Monomeric myosin anchoring

Expression of a dominant-negative myosin-1A (green) results in loss of apical SI (red).

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.

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 proteins.

Thus, myosin-1A may serve as an anchor, with the clustering of SI in rafts helping to secure the link even if an individual myosin-1A lets go. The link appears to be specific as other raft proteins—which probably come and go between different rafts—are not affected by the dominant-negative constructs. Tyska is now determining whether the myosin-1A–SI link is regulated by signaling proteins or bacterial toxins.

William A. Wells

wellsw{at}rockefeller.edu

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This Article Full Text (PDF, 618K) PPT slides of all figures Alert me when this article is cited Services Email this article Similar articles in this journal Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Wells, W. A. Search for Related Content PubMed Articles by Wells, W. A. Social Bookmarking                            What's this?