4.5 Article

Detergent-free caveolae proteome suggests an interaction with ER and mitochondria

Journal

PROTEOMICS
Volume 6, Issue 1, Pages 143-152

Publisher

WILEY
DOI: 10.1002/pmic.200500208

Keywords

cell signaling; endoplasmic reticulum; lipid raft; mass spectrometry; membrane proteins

Funding

  1. NCI NIH HHS [CA 107943] Funding Source: Medline
  2. NHLBI NIH HHS [HL 20948] Funding Source: Medline
  3. NIGMS NIH HHS [GM 52016] Funding Source: Medline
  4. NATIONAL CANCER INSTITUTE [R33CA107943, R21CA107943] Funding Source: NIH RePORTER
  5. NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [P01HL020948] Funding Source: NIH RePORTER
  6. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM052016] Funding Source: NIH RePORTER

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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.

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