Geometry of actin-membrane attachments in the smooth muscle cell: the localisations of vinculin and alpha-actinin.
Antibodies to vinculin, a component of actin-membrane attachment sites, revealed by immunofluorescence microscopy a parallel co-axial array of continuous rib-like bands on the surface of isolated vertebrate smooth muscle cells. Images of extended and shortened cells showed that these ribs remain co-axially organised on contraction. Reference to earlier studies and labelling of thin sections indicates that the ribs correspond in position to the adhesion plaques previously described in electron microscope studies. Alpha-actinin showed a punctate distribution consistent with its presence in the cytoplasmic dense bodies, but did not show a constant association with the vinculin-containing ribs. It is suggested that alpha-actinin is an intracellular actin linker and not membrane associated, as earlier supposed, and that vinculin is, as deduced by others, a mediator of actin membrane attachment. The apparent co-association of these two proteins, noted previously, is concluded to arise from the inevitable geometrical apposition of peripheral and pre-terminal parts of the contractile machinery with the cell membrane.
D000185:Actinin / Q000378:metabolism*; D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D002645:Chickens; D006168:Guinea Pigs; D006651:Histocytochemistry; D008297:Male; D009119:Muscle Contraction; D009124:Muscle Proteins / Q000378:metabolism*; D009130:Muscle, Smooth / Q000378:metabolism*; D016596:Vinculin
D000199:Actins; D009124:Muscle Proteins; D000185:Actinin; D016596:Vinculin