Specific association of annexin 1 with plasma membrane‐resident and internalized EGF receptors mediated through the protein core domain
- 10 November 2004
- journal article
- Published by Wiley in FEBS Letters
- Vol. 578 (1-2) , 95-98
- https://doi.org/10.1016/j.febslet.2004.10.078
Abstract
Phosphorylation of the Ca2+ and membrane-binding protein annexin 1 by epidermal growth factor (EGF) receptor tyrosine kinase has been thought to be involved in regulation of the EGF receptor trafficking. To elucidate the interaction of annexin 1 during EGF receptor internalization, we followed the distribution of annexin 1-GFP fusion proteins at sites of internalizing EGF receptors. The observed association of annexin 1 with EGF receptors was confirmed by immunoprecipitation. We found that this interaction was independent of a functional phosphorylation site in the annexin 1 N-terminal domain but mediated through the Ca2+ binding core domainKeywords
This publication has 23 references indexed in Scilit:
- Glucocorticoids act within minutes to inhibit recruitment of signalling factors to activated EGF receptors through a receptor‐dependent, transcription‐independent mechanismBritish Journal of Pharmacology, 2000
- Annexin 1 expression and phosphorylation are upregulated during liver regeneration and transformation in antithrombin iii sv40 t large antigen transgenic miceHepatology, 2000
- Dynamin at the Neck of Caveolae Mediates Their Budding to Form Transport Vesicles by GTP-driven Fission from the Plasma Membrane of EndotheliumThe Journal of cell biology, 1998
- Control of EGF Receptor Signaling by Clathrin-Mediated EndocytosisScience, 1996
- The Hepatocyte Growth Factor Receptor Kinase-mediated Phosphorylation of Lipocortin-1 Transduces the Proliferating Signal of the Hepatocyte Growth FactorPublished by Elsevier ,1996
- Growth hormone induces tyrosine phosphorylation of annexin I in rat osteosarcoma cellsEndocrinology, 1996
- Induction of mutant dynamin specifically blocks endocytic coated vesicle formation.The Journal of cell biology, 1994
- Role of the amino-terminal domain in regulating interactions of annexin I with membranes: Effects of amino-terminal truncation and mutagenesis of the phosphorylation sitesBiochemistry, 1994
- Annexin I is phosphorylated in the multivesicular body during the processing of the epidermal growth factor receptor.The Journal of cell biology, 1993
- Epidermal growth factor-dependent phosphorylation of lipocortinNature, 1986