Molecular Characterization of Caveolin Association with the Golgi Complex: Identification of a Cis-Golgi Targeting Domain in the Caveolin Molecule

Caveolins are integral membrane proteins which are a major component of caveolae. In addition, caveolins have been proposed to cycle between intracellular compartments and the cell surface but the exact trafficking route and targeting information in the caveolin molecule have not been defined. We sh...

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Bibliographic Details
Published in:The Journal of cell biology 1999-06, Vol.145 (7), p.1443-1459
Main Authors: Luetterforst, Robert, Stang, Espen, Zorzi, Natasha, Carozzi, Amanda, Way, Michael, Parton, Robert G.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Antibodies
Caveolae
Caveolin 1
Caveolin 3
Caveolins
Cell Line
Cell lines
Cell Membrane - chemistry
Cell Membrane - drug effects
Cell Membrane - metabolism
Cell Membrane - ultrastructure
Cell membranes
Cells
Cells, Cultured
Cellular biology
Cholesterols
Conserved Sequence - genetics
Epithelial cells
Fibroblasts
Fluorescent Antibody Technique
Golgi apparatus
Golgi Apparatus - chemistry
Golgi Apparatus - drug effects
Golgi Apparatus - metabolism
Golgi Apparatus - ultrastructure
Humans
Intracellular Membranes - chemistry
Intracellular Membranes - drug effects
Intracellular Membranes - metabolism
Intracellular Membranes - ultrastructure
Membrane Proteins - analysis
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membranes
Microscopy, Immunoelectron
Molecular Sequence Data
Molecules
Nocodazole - pharmacology
Palmitic Acid - metabolism
Protein Binding
Protein Sorting Signals
Proteins
Recombinant Fusion Proteins - analysis
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - immunology
Regular
Sequence Deletion
Transfection
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Summary:Caveolins are integral membrane proteins which are a major component of caveolae. In addition, caveolins have been proposed to cycle between intracellular compartments and the cell surface but the exact trafficking route and targeting information in the caveolin molecule have not been defined. We show that antibodies against the caveolin scaffolding domain or against the COOH terminus of caveolin-1 show a striking specificity for the Golgi pool of caveolin and do not recognize surface caveolin by immunofluorescence. To analyze the Golgi targeting of caveolin in more detail, caveolin mutants were expressed in fibroblasts. Specific mutants lacking the NH2 terminus were targeted to the cis Golgi but were not detectable in surface caveolae. Moreover, a 32-amino acid segment of the putative COOH-terminal cytoplasmic domain of caveolin-3 was targeted specifically and exclusively to the Golgi complex and could target a soluble heterologous protein, green fluorescent protein, to this compartment. Palmitoylation-deficient COOH-terminal mutants showed negligible association with the Golgi complex. This study defines unique Golgi targeting information in the caveolin molecule and identifies the cis Golgi complex as an intermediate compartment on the caveolin cycling pathway.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.145.7.1443