Journal
PROTEOMICS
Volume 6, Issue 1, Pages 143-152Publisher
WILEY
DOI: 10.1002/pmic.200500208
Keywords
cell signaling; endoplasmic reticulum; lipid raft; mass spectrometry; membrane proteins
Funding
- NCI NIH HHS [CA 107943] Funding Source: Medline
- NHLBI NIH HHS [HL 20948] Funding Source: Medline
- NIGMS NIH HHS [GM 52016] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R33CA107943, R21CA107943] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [P01HL020948] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM052016] Funding Source: NIH RePORTER
Ask authors/readers for more resources
Recent proteomic studies of detergent resistant membrane fractions have begun to characterize the protein composition of caveolae and lipid rafts. The methods used in most of these studies, however, are not able to distinguish between plasma membrane and internal membrane lipid domains. Here we used a non-detergent method for obtaining fractions enriched in caveolae derived from the plasma membrane of multiple cell types. Unexpectedly, the proteins in the caveolae proteome suggest these lipid domains may interact with elements of ER and mitochondria. A comparison of the partial proteome we obtained with other published reports identifies 26 proteins that are candidate marker proteins for identifying caveolae in multiple cell types.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available