title: Dystrophin and the membrane skeleton.
abstract: Recent studies have confirmed several predictions concerning the structure and possible function of dystrophin, including a direct interaction with F-actin and an indirect interaction with laminin via linkage through a transmembrane protein complex. The results of the past year support a role for dystrophin in linking the actin cytoskeleton with the extracellular matrix in striated muscle, but they have not explained its function in other tissues.
authors.affiliation: University of Wisconsin, Department of Physiology, Madison 53706.
authors.forename: J M
authors.initials: JM
authors.lastname: Ervasti
authors.forename: K P
authors.initials: KP
authors.lastname: Campbell
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D003599:Cytoskeleton / Q000648:ultrastructure*; D016189:Dystrophin / Q000502:physiology*; D006031:Glycosylation; D006801:Humans; D008840:Microfilament Proteins / Q000378:metabolism; D008958:Models, Molecular; D009136:Muscular Dystrophies / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D012508:Sarcolemma / Q000648:ultrastructure*; D014101:Torpedo / Q000378:metabolism
chemical_list: D000199:Actins; D016189:Dystrophin; D008840:Microfilament Proteins