Actin filaments are associated with the septate junctions of invertebrates.
Septate junctions are almost ubiquitous in the tissues of invertebrates but are never found in those of vertebrates. In spite of their widespread occurrence and hence obvious importance to the invertebrates, their precise function has remained elusive although they have been variously considered to be regions of cell-cell coupling, permeability barriers or adhesion sites. This report demonstrates that elements of the cytoskeletal system insert into the cytoplasmic face of septate junctions. Actin filaments, identified by virtue of their capacity to bind the S1 subfragment of rabbit myosin, are associated with the membranes of septate junctions. Cytochalasin D, an actin depolymerizer, leads to disorganization of the intramembrane components of these junctions. These data suggest that a primary role of septate junctions could be to maintain intercellular cohesion and hence tissue integrity. The assembly and localization of these junctions may be mediated, directly or indirectly, by the cytoplasmic actin filaments associated with their lateral membranes.
Lane
N J
NJ
AFRC Unit of Insect Neurophysiology and Pharmacology, Department of Zoology, Cambridge.
Flores
V
V
D000199:Actins / Q000032:analysis* / Q000378:metabolism; D000818:Animals; D002432:Cecum / Q000166:cytology*; D015638:Cytochalasin D; D003572:Cytochalasins / Q000494:pharmacology; D005260:Female; D005614:Freeze Fracturing; D047348:Hydrolyzable Tannins; D007365:Intercellular Junctions / Q000187:drug effects / Q000648:ultrastructure*; D007811:Lanthanum; D008854:Microscopy, Electron; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism; D010526:Periplaneta; D013194:Staining and Labeling
D000199:Actins; D003572:Cytochalasins; D047348:Hydrolyzable Tannins; D015879:Myosin Subfragments; D010446:Peptide Fragments; D015638:Cytochalasin D; D007811:Lanthanum; D009218:Myosins