Junctional plasma membrane domains isolated from aggregating Dictyostelium discoideum amebae.

HM Ingalls, CM Goodloe-Holland… - Proceedings of the …, 1986 - National Acad Sciences
HM Ingalls, CM Goodloe-Holland, EJ Luna
Proceedings of the National Academy of Sciences, 1986National Acad Sciences
Regions of plasma membrane involved in Dictyostelium discoideum intercellular adhesion
resist solubilization with the nonionic detergent Triton X-100. Electron microscopy shows
that these regions of the plasma membrane adhere to each other, forming many bi-and
multilamellar structures. NaDodSO4/polyacrylamide gels of these regions contain major
polypeptides at 225 kDa (residual myosin), 105 kDa, 88 kDa, 84 kDa, 47 kDa (residual
actin), and 34 kDa. These membranes contain a subset of the total plasma membrane …
Regions of plasma membrane involved in Dictyostelium discoideum intercellular adhesion resist solubilization with the nonionic detergent Triton X-100. Electron microscopy shows that these regions of the plasma membrane adhere to each other, forming many bi- and multilamellar structures. NaDodSO4/polyacrylamide gels of these regions contain major polypeptides at 225 kDa (residual myosin), 105 kDa, 88 kDa, 84 kDa, 47 kDa (residual actin), and 34 kDa. These membranes contain a subset of the total plasma membrane proteins, as analyzed by labeling of electrophoretically fractionated and blotted membrane proteins with radioiodinated Con A and by electrophoresis of membrane proteins from surface-labeled cells. Antibodies specific for gp80, a glycoprotein implicated in intercellular adhesion, intensely stain the 88-kDa and 84-kDa bands. Since these membrane regions resist Triton extraction, they appear to be stabilized by protein-protein interactions. Such stabilizing interactions may involve multivalent linkages with adjacent cells, or associations with intracellular actin and myosin, or both. Since these membranes appear to represent regions of intercellular contact, we call them "contact regions."
National Acad Sciences