Isolated endosomes from quiescent rat liver contain the signal transduction machinery
- 11 December 1998
- journal article
- Published by Wiley in FEBS Letters
- Vol. 441 (1), 34-38
- https://doi.org/10.1016/s0014-5793(98)01517-8
Abstract
In this study we identify the molecules involved in the MAPK signal transduction pathway (Ras, Raf-1, Mek, Mek-P and MAPK) in highly purified endosomal fractions isolated from rat liver. Biochemical analysis shows that only the early-sorting endocytic compartment contains activated Raf-1 and Mek. Finally, the exogenous administration of EGF led to redistribution of Raf-1 from the caveolin-enriched plasma membrane into the endosomes.Keywords
This publication has 26 references indexed in Scilit:
- THE CAVEOLAE MEMBRANE SYSTEMAnnual Review of Biochemistry, 1998
- Membrane transport in rat liver endocytic pathways: Preparation, biochemical properties and functional roles of hepatic endosomesElectrophoresis, 1997
- Src Tyrosine Kinases, Gα Subunits, and H-Ras Share a Common Membrane-anchored Scaffolding Protein, CaveolinPublished by Elsevier BV ,1996
- Receptor signalling and the regulation of endocytic membrane transportCurrent Opinion in Cell Biology, 1996
- Localization of Epidermal Growth Factor-stimulated Ras/Raf-1 Interaction to Caveolae MembranePublished by Elsevier BV ,1996
- Insulin stimulates the tyrosine phosphorylation of caveolin.The Journal of cell biology, 1995
- [31] Activation of Raf-1 by Ras in intact cellsMethods in Enzymology, 1995
- Structure/function relationship of proteins belonging to the family of receptors coupled to GTP‐binding proteinsJBIC Journal of Biological Inorganic Chemistry, 1991
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970