Display Settings:

Format

Send to:

Choose Destination
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10517-21.

Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-transformed fibroblasts.

Author information

  • 1Lucille P. Markey Cancer Center, Lexington, KY.

Abstract

Caveolae are flask-shaped plasma membrane invaginations abundant in endothelium and muscle but may be present in all cells. They contain a filamentous coat material thought to be important in their structure and function. Recent studies have demonstrated that a 22-kDa protein (caveolin) phosphorylated on tyrosine in Rous sarcoma virus-transformed chicken fibroblasts is a component of the caveolae coat on the inner aspect of the membrane. We now report the deduced protein sequence of chicken caveolin derived from cDNA PCR products and genomic DNA clones. Caveolin is a unique protein of 178 amino acids and displays little sequence similarity to other proteins in the GenBank data base. Hydrophobicity predictions indicate an unusual 40-amino acid hydrophobic region near the C terminus that may be used to anchor the protein to the membrane. When chicken caveolin was expressed in mouse 3T3 cells and detected by immunofluorescence microscopy, the typical caveolae pattern was observed. This includes brightly fluorescent membrane patches in many cases concentrated at the margin of cells and in arrays. Caveolae may be distinct from other membrane domains due at least in part to caveolin.

PMID:
1279683
[PubMed - indexed for MEDLINE]
PMCID:
PMC50370
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk