title: 'Putting the squeeze' on the tight junction: understanding cytoskeletal regulation.
abstract: The apical perijunctional actomyosin ring of epithelia is structurally associated with the tight junction. The functional association between the tight junction and the perijunctional actomyosin ring was initially described in studies using pharmacological agents that disrupt microfilaments. More recently, this interaction has been studied in physiological, pathophysiological, and molecular models of tight junction regulation. These studies have demonstrated the central role of actomyosin contraction in tight junction regulation. With the identification of novel tight junction proteins and characterization of their protein:protein interactions comes the promise of detailed understanding of the molecular interactions that mediate tight junction regulation.
authors.affiliation: Department of Pathology, Wayne State University School of Medicine, USA. jturner@med.wayne.edu
authors.forename: J R
authors.initials: JR
authors.lastname: Turner
mesh_terms: D000205:Actomyosin / Q000502:physiology; D000818:Animals; D015638:Cytochalasin D / Q000494:pharmacology; D003599:Cytoskeleton / Q000502:physiology*; D020895:Enterocytes / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D009219:Myosin-Light-Chain Kinase / Q000502:physiology; D010539:Permeability; D019108:Tight Junctions / Q000187:drug effects / Q000502:physiology*
chemical_list: D015638:Cytochalasin D; D000205:Actomyosin; D009219:Myosin-Light-Chain Kinase