Compartmentalization of Ras proteins

DOI PDF 被引用文献2件
  • Ian A. Prior
    University of Queensland Medical School, Herston Road Laboratory of Experimental Oncology, Department of Pathology , , Brisbane, Australia
  • John F. Hancock
    University of Queensland Medical School, Herston Road Laboratory of Experimental Oncology, Department of Pathology , , Brisbane, Australia

書誌事項

公開日
2001-05-01
権利情報
  • http://www.biologists.com/user-licence-1-1/
DOI
  • 10.1242/jcs.114.9.1603
公開者
The Company of Biologists

この論文をさがす

説明

<jats:title>ABSTRACT</jats:title> <jats:p>The Ras GTPases operate as molecular switches that link extracellular stimuli with a diverse range of biological outcomes. Although many studies have concentrated on the protein-protein interactions within the complex signaling cascades regulated by Ras, it is becoming clear that the spatial orientation of different Ras isoforms within the plasma membrane is also critical for their function. H-Ras, N-Ras and K-Ras use different membrane anchors to attach to the plasma membrane. Recently it has been shown that these anchors also act as trafficking signals that direct palmitoylated H-Ras and N-Ras through the exocytic pathway to the cell surface but divert polybasic K-Ras around the Golgi to the plasma membrane via an as yet-unidentified-route. Once at the plasma membrane, H-Ras and K-Ras operate in different microdomains. K-Ras is localized predominantly to the disordered plasma membrane, whereas H-Ras exists in a GTP-regulated equilibrium between disordered plasma membrane and cholesterol-rich lipid rafts. These observations provide a likely explanation for the increasing number of biological differences being identified between the otherwise highly homologous Ras isoforms and raise interesting questions about the role membrane microlocalization plays in determining the interactions of Ras with its effectors and exchange factors.</jats:p>

収録刊行物

被引用文献 (2)*注記

もっと見る

詳細情報 詳細情報について

問題の指摘

ページトップへ