Specific association of annexin 1 with plasma membrane-resident and internalized EGF receptors mediated through the protein core domain.
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 domain.
Radke
Susanne
S
Institute for Medical Biochemistry, Centre for Molecular Biology of Inflammation, ZMBE, IZKF Münster, University of Münster, von-Esmarch-Str. 56, 48149 Münster, Germany.
Austermann
Judith
J
Russo-Marie
Francoise
F
Gerke
Volker
V
Rescher
Ursula
U
D017305:Annexin A1 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D004705:Endocytosis / Q000502:physiology; D066246:ErbB Receptors / Q000378:metabolism*; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D047468:Immunoprecipitation; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D017305:Annexin A1; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; D066246:ErbB Receptors; D002118:Calcium