Multivalent endosome targeting by homodimeric EEA1.
Early endosome autoantigen localization to early endosomes is mediated by a C-terminal region, which includes a calmodulin binding motif, a Rab5 interaction site, and a FYVE domain that selectively binds phosphatidyl inositol 3-phosphate. The crystal structure of the C-terminal region bound to inositol 1,3-bisphosphate reveals an organized, quaternary assembly consisting ... of a parallel coiled coil and a dyad-symmetric FYVE domain homodimer. Structural and biochemical observations support a multivalent mechanism for endosomal localization in which domain organization, dimerization, and quaternary structure amplify the weak affinity and modest specificity of head group interactions with conserved residues. A unique mode of membrane engagement deduced from the quaternary structure of the C-terminal region provides insight into the structural basis of endosome tethering.
Mesh Terms:
Amino Acid Sequence, Autoantigens, Crystallography, X-Ray, Dimerization, Endosomes, Inositol Phosphates, Membrane Proteins, Models, Biological, Models, Molecular, Molecular Sequence Data, Phospholipids, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, Sequence Alignment, Vesicular Transport Proteins, Zinc Fingers, rab5 GTP-Binding Proteins
Amino Acid Sequence, Autoantigens, Crystallography, X-Ray, Dimerization, Endosomes, Inositol Phosphates, Membrane Proteins, Models, Biological, Models, Molecular, Molecular Sequence Data, Phospholipids, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, Sequence Alignment, Vesicular Transport Proteins, Zinc Fingers, rab5 GTP-Binding Proteins
Mol. Cell
Date: Nov. 01, 2001
PubMed ID: 11741531
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