Altered localization of H-Ras in caveolin-1-null cells is palmitoylation-independent

Baran, J., Mundy, D. I., Vasanji, A. and Parat, M-O. (2008) Altered localization of H-Ras in caveolin-1-null cells is palmitoylation-independent. Journal of Cell Communication and Signaling, 1 : 195-204.


Author Baran, J.
Mundy, D. I.
Vasanji, A.
Parat, M-O.
Title Altered localization of H-Ras in caveolin-1-null cells is palmitoylation-independent
Journal name Journal of Cell Communication and Signaling   Check publisher's open access policy
ISSN 1873-9601
Publication date 2008
Year available 2008
DOI 10.1007/s12079-008-0017-3
Volume 1
Start page 195
End page 204
Total pages 10
Editor perbal, B.
Place of publication Netherlands
Publisher Springer Netherlands
Collection year 2009
Language eng
Subject C1
060108 Protein Trafficking
060111 Signal Transduction
920102 Cancer and Related Disorders
Abstract Caveolin-1 is a palmitoylated protein involved in the formation of plasma membrane subdomains termed caveolae, intracellular cholesterol transport, and assembly and regulation of signaling molecules in caveolae. Caveolin-1 interacts via a consensus binding motif with several signaling proteins, including H-Ras. Ras oncogene products function as molecular switches in several signal transduction pathways regulating cell growth and differentiation. Post-translational modifications, including palmitoylation, are critical for the membrane targeting and function of H-Ras. Subcellular localization regulates the signaling pathways engaged by H-Ras activation. We show here that H-Ras is localized at the plasma membrane in caveolin-1-expressing cells but not in caveolin-1-deficient cells. Since palmitoylation is required for trafficking of H-Ras from the endomembrane system to the plasma membrane, we tested whether the altered localization of H-Ras in caveolin-1-null cells is due to decreased H-Ras palmitoylation. Although the palmitoylation profiles of cultured embryo fibroblasts isolated from wild type and caveolin-1 gene-disrupted mice differed, suggesting that caveolin-1, or caveolae, play a role in the palmitate incorporation of a subset of palmitoylated proteins, the palmitoylation of H-Ras was not decreased in caveolin-1-null cells. We conclude that the altered localization of H-Ras in caveolin-1-deficient cells is palmitoylation-independent. This article shows two important new mechanisms by which loss of caveolin-1 expression may perturb intracellular signaling, namely the mislocalization of signaling proteins and alterations in protein palmitoylation.
Q-Index Code C1
Q-Index Status Confirmed Code
Additional Notes Article clearly states: Received: 22 October 2007 Accepted: 31 January 2008 PUBLISHED ONLINE: 17 February 2008

 
Versions
Version Filter Type
Citation counts: Google Scholar Search Google Scholar
Access Statistics: 76 Abstract Views  -  Detailed Statistics
Created: Tue, 14 Apr 2009, 16:04:55 EST by Elizabeth Pyke on behalf of School of Pharmacy