@article{oai:ir.soken.ac.jp:00003274,
 author = {蟻川, 謙太郎 and WILLIAMS, David S and HALLETT, Mark A. and ARIKAWA, Kentaro},
 issue = {1},
 journal = {Journal of Cell Science, Journal of Cell Science},
 month = {Sep},
 note = {application/pdf, The cilium of a vertebrate photoreceptor cell connects the phototransductive outer segment of the cell to the inner segment. Previous studies have shown that, within the connecting cilium, there is a small cluster of actin filaments, which play a critical role in the formation of new disk membranes. Here, we have detected a polypeptide in rat rod outer segments that is recognized by myosin heavy chain antibodies and was found to possess other characteristics of conventional non-muscle myosin heavy chain: it comigrates in SDS-PAGE with non-muscle myosin heavy chain; it associates with the cytoskeleton of rod outer segments in an ATP-sensitive manner; and it binds to purified actin filaments in the absence of ATP. Myosin ATPase activity was also detected in isolated rod outer segments. Electron immunomicroscopy revealed that myosin is present in the small actin-containing domain within the connecting cilium at the site of disk membrane morphogenesis. These results pose the possibility that an actin-myosin contractile mechanism functions in the formation of new photoreceptor disk membranes.},
 pages = {183--190},
 title = {Association of myosin with the connecting cilium of rod photoreceptors},
 volume = {103},
 year = {1992}
}