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  • Title: Modulation of band 3-ankyrin interaction by protein 4.1. Functional implications in regulation of erythrocyte membrane mechanical properties.
    Author: An XL, Takakuwa Y, Nunomura W, Manno S, Mohandas N.
    Journal: J Biol Chem; 1996 Dec 27; 271(52):33187-91. PubMed ID: 8969174.
    Abstract:
    Protein 4.1 is an important structural component of the erythrocyte membrane. In contrast to our detailed understanding of the role of protein 4.1 in regulating membrane mechanical properties through modulation of spectrin-actin interaction, very little is known regarding the functional implications of protein 4.1 interaction with band 3. In the present study, we explored the potential role of protein 4.1-band 3 interaction in modulating membrane mechanical properties. Based on recent studies which identified the sequence motif IRRRY in band 3 as the protein 4.1 interacting domain, we studied the functional consequences of specific dissociation of band 3-protein 4.1 interaction by the synthetic peptide IRRRY. We show that protein 4.1 bound to the inside-out vesicles could be dissociated from band 3 but not from glycophorin C by IRRRY. Furthermore, incorporation of IRRRY into resealed ghosts resulted in decreased membrane deformability and increased membrane mechanical stability. The observed alterations in membrane properties appears to result from increased band 3-ankyrin interaction following dissociation of protein 4.1 from band 3. These studies have enabled us to identify an important functional role for band 3-protein 4.1 interaction in modulating erythrocyte membrane properties.
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