title: Caveolin-2 localizes to the golgi complex but redistributes to plasma membrane, caveolae, and rafts when co-expressed with caveolin-1.
abstract: We have characterized comparatively the subcellular distributions of caveolins-1 and -2, their interactions and their roles in caveolar formation in polarized epithelial cells. In Fischer rat thyroid (FRT) cells, which express low levels of caveolin-2 and no caveolin-1, caveolin-2 localizes exclusively to the Golgi complex but is partially redistributed to the plasma membrane upon co-expression of caveolin-1 by transfection or by adenovirus-mediated transduction. In Madin-Darby canine kidney (MDCK) cells, which constitutively express both caveolin-1 and -2, caveolin-2 localized to both the Golgi complex and to the plasma membrane, where it co-distributed with caveolin-1 in flat patches and in caveolae. In FRT cells, endogenous or overexpressed caveolin-2 did not associate with low density Triton insoluble membranes that floated in sucrose density gradients but was recruited to these membranes when co-expressed together with caveolin-1. In MDCK cells, both caveolin-1 and caveolin-2 associated with low density Triton-insoluble membranes. In FRT cells, transfection of caveolin-1 promoted the assembly of plasma membrane caveolae that localized preferentially (over 99%) to the basolateral surface, like constitutive caveolae of MDCK cells. In contrast, as expected from its intracellular distribution, endogenous or overexpressed caveolin-2 did not promote the assembly of caveolae; rather, it appeared to promote the assembly of intracellular vesicles in the peri-Golgi area. The data reported here demonstrate that caveolin-1 and -2 have different and complementary subcellular localizations and functional properties in polarized epithelial cells and suggest that the two proteins co-operate to carry out specific as yet unknown tasks between the Golgi complex and the cell surface.
authors.affiliation: Dyson Vision Research Institute, Department of Ophthalmology, and Department of Cell Biology, Weill Medical College of Cornell University, New York 10021, USA.
authors.forename: R
authors.initials: R
authors.lastname: Mora
authors.forename: V L
authors.initials: VL
authors.lastname: Bonilha
authors.forename: A
authors.initials: A
authors.lastname: Marmorstein
authors.forename: P E
authors.initials: PE
authors.lastname: Scherer
authors.forename: D
authors.initials: D
authors.lastname: Brown
authors.forename: M P
authors.initials: MP
authors.lastname: Lisanti
authors.forename: E
authors.initials: E
authors.lastname: Rodriguez-Boulan
mesh_terms: D000818:Animals; D001692:Biological Transport; D051242:Caveolin 1; D051243:Caveolin 2; D022461:Caveolins; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D003594:Cytoplasmic Granules / Q000378:metabolism; D004285:Dogs; D006056:Golgi Apparatus / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D008854:Microscopy, Electron; D051381:Rats; D011916:Rats, Inbred F344; D013961:Thyroid Gland / Q000378:metabolism / Q000648:ultrastructure
chemical_list: C495537:Cav1 protein, rat; D051242:Caveolin 1; D051243:Caveolin 2; D022461:Caveolins; D008565:Membrane Proteins