GTP-dependent segregation of H-ras from lipid rafts is required for biological activity

Nature Cell Biology

Volumn 3, Issue 4, 2001, Pages 368-375

  Prior, Ian A ^a   Harding, Angus ^a   Yan, Jun ^a   Sluimer, Judith ^a   Parton, Robert G ^a   Hancock, John F ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; LIPID; NUCLEOTIDE; RAF PROTEIN; RAS PROTEIN;

ANIMAL CELL; ARTICLE; CELL MEMBRANE; CONTROLLED STUDY; GENE ACTIVATION; GENE FUNCTION; GENE SEGREGATION; NONHUMAN; ONCOGENE H RAS; ONCOGENE K RAS; PALMITOYLATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN TARGETING;

ANIMALS; CELL LINE; CELL MEMBRANE; CRICETINAE; ENZYME ACTIVATION; GUANOSINE TRIPHOSPHATE; LIPID METABOLISM; MEMBRANE MICRODOMAINS; MICROSCOPY, IMMUNOELECTRON; PROTO-ONCOGENE PROTEINS C-RAF; PROTO-ONCOGENE PROTEINS P21(RAS); RECOMBINANT FUSION PROTEINS;

ANIMALIA;

EID: 0035067187     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/35070050     Document Type: Article

References (33)

1. K-ras is an essential gene in the mouse with partial functional overlap with N-ras
2. The murine N-ras gene is not essential for growth and development
3. Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase
4. Increasing complexity of Ras signaling
5. All ras proteins are polyisoprenylated but only some are palmitoylated
6. A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
7. H-ras but not K-ras traffics to the cell surface via the exocytic pathway
8. Endomembrane trafficking of Ras: The CAAX motif targets proteins to the ER and Golgi
9. Dominant-negative caveolin inhibits H-ras function by disrupting cholesterol-rich plasma membrane domains
10. A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins
11. Lipid domain structure of the plasma membrane revealed by patching of membrane compartments
12. Functionally different GPI proteins are organized in different domains on the neuronal surface
13. Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains
14. Reduction of caveolin and caveolae in oncogenically transformed cells
15. Transforming p21 ras protein: Flexibility in the major variable region linking the catalytic and membrane anchoring domains
16. Matrix adhesion and Ras transformation both activate a phosphoinisotide 3-OH kinase and protein kinase B/Akt cellular survival pathway
17. Stimulation of p21ras upon T-cell activation
18. Stimulation of nucleotide exchange on Ras- and Rho-related proteins by small GTP-binding protein GDP dissociation stimulator
19. The complexity of Raf-1 regulation
20. Activity of plasma membrane recruited Raf-1 is regulated by Ras via the Raf zinc finger
21. 14-3-3 potentiates Ras dependent Raf-1 activation in vitro and in vivo
22. Serine and tyrosine phosphorylations cooperate in Raf-1, but not B-Raf activation
23. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
24. Activation of Raf as a result of recruitment to the plasma membrane
25. Membrane interactions of constitutively active GFP-Ki-Ras4B and their role in signaling
26. Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts
27. Lipid-dependent targeting of G-proteins into rafts
28. Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
29. Properties of lipid microdomains visualized by single molecule microscopy
30. Regulated migration of epidermal growth factor receptor from caveolae
31. Involvement of caveolin-1 in meiotic cell-cycle progression in Caenorhabditis elegans
32. 2+ on the guanine nucleotide exchange rate of p21N-ras
33. Determination of structural requirements for the interaction of Rab6 with RabGDI and Rab geranylgeranyltransferase