title: Molecular shape and self-association of vinculin and metavinculin.
abstract: Vinculin, a 130,000-dalton protein localized to adhesion plaques, and metavinculin, a 150,-000 dalton protein closely related to vinculin, have been studied using rotary shadowing and electron microscopy. Both proteins have globular head regions attached to rod-shaped tail domains. Vinculin and metavinculin also both form complexes consisting of four to six individual molecules. These multimers are formed by head-to-head as well as tail-to-tail interactions. Talin, another protein which has been localized to adhesion plaques and binds to both vinculin and metavinculin, has also been investigated using shadowing techniques. Talin is an elongated, flexible molecule in high ionic strength buffers, as shown here by rotary shadowing and negative stain electron microscopy.
mesh_terms: D000818:Animals; D030161:Avian Proteins; D002448:Cell Adhesion; D002645:Chickens; D046911:Macromolecular Substances; D008840:Microfilament Proteins / Q000378:metabolism; D008854:Microscopy, Electron; D009124:Muscle Proteins / Q000378:metabolism; D011485:Protein Binding; D016608:Talin; D016596:Vinculin
chemical_list: D030161:Avian Proteins; D046911:Macromolecular Substances; D008840:Microfilament Proteins; D009124:Muscle Proteins; D016608:Talin; C035689:VCL protein, Gallus gallus; D016596:Vinculin