Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol.

@article{Harder1997SpecificRO,
  title={Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol.},
  author={Tim Harder and Roland Kellner and Robert G. Parton and Jean Gruenberg},
  journal={Molecular biology of the cell},
  year={1997},
  volume={8 3},
  pages={533-45}
}
Annexin II is an abundant protein which is present in the cytosol and on the cytoplasmic face of plasma membrane and early endosomes. It is generally believed that this association occurs via Ca(2+)-dependent binding to lipids, a mechanism typical for the annexin protein family. Although previous studies have shown that annexin II is involved in early endosome dynamics and organization, the precise biological role of the protein is unknown. In this study, we found that approximately 50% of the… CONTINUE READING

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Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
CytoskeletonIs associated anatomy of gene productezrin
Among the released proteins , we identified , in addition to annexin II itself , the cortical cytoskeletal proteins alpha - actinin , ezrin and moesin , and membrane - associated actin .
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
MicrofilamentsConstitutional part ofCytoskeleton
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
MicrofilamentsAnatomic structure is physical part ofCytoskeleton
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
Since annexin II is tightly membrane - associated in a cholesterol - dependent manner , and since it seems to interact physically with elements of the cortical actin cytoskeleton , we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton .
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