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Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic.
- Source :
-
Cell [Cell] 2004 Sep 17; Vol. 118 (6), pp. 767-80. - Publication Year :
- 2004
-
Abstract
- Endocytosis comprises several routes of internalization. An outstanding question is whether the caveolar and endosomal pathways intersect. Following transport of the caveolar protein Caveolin-1 and two cargo complexes, Simian Virus 40 and Cholera toxin, in live cells, we uncovered a Rab5-dependent pathway in which caveolar vesicles are targeted to early endosomes and form distinct and stable membrane domains. In endosomes, the low pH selectively allowed the toxin to diffuse out of the caveolar domains into the surrounding membrane, while the virus remained trapped. Thus, we conclude that, unlike cyclic assembly and disassembly of coat proteins in vesicular transport, oligomeric complexes of caveolin-1 confer permanent structural stability to caveolar vesicles that transiently interact with endosomes to form subdomains and release cargo selectively by compartment-specific cues.
- Subjects :
- Caveolae ultrastructure
Caveolin 1
Cell Compartmentation physiology
Cell Membrane ultrastructure
Cholera Toxin metabolism
Endosomes metabolism
Endosomes ultrastructure
HeLa Cells
Humans
Hydrogen-Ion Concentration
Protein Transport physiology
Simian virus 40 metabolism
Transport Vesicles metabolism
rab5 GTP-Binding Proteins metabolism
Caveolae metabolism
Caveolins metabolism
Cell Membrane metabolism
Endocytosis physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0092-8674
- Volume :
- 118
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Cell
- Publication Type :
- Academic Journal
- Accession number :
- 15369675
- Full Text :
- https://doi.org/10.1016/j.cell.2004.09.003