Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Quick Search
My eDoc
Session History
Support Wiki
Direct access to
document ID:

          Institute: MPI für molekulare Zellbiologie und Genetik     Collection: Publikationen MPI-CBG 2011-arch     Display Documents

ID: 585273.0, MPI für molekulare Zellbiologie und Genetik / Publikationen MPI-CBG 2011-arch
Key Amino Acid Residues of Ankyrin-Sensitive Phosphatidylethanolamine/Phosphatidylcholine-Lipid Binding Site of beta I-Spectrin
Authors:Wolny, Marcin; Grzybek, Michal; Bok, Ewa; Chorzalska, Anna; Lenoir, Marc; Czogalla, Aleksander; Adamczyk, Klaudia; Kolondra, Adam; Diakowski, Witold; Overduin, Michael; Sikorski, Aleksander F
Date of Publication (YYYY-MM-DD):2011
Title of Journal:PLoS ONE
Issue / Number:6
Sequence Number of Article:e21538
Copyright:not available
Review Status:not specified
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:It was shown previously that an ankyrin-sensitive, phosphatidylethanolamine/phosphatidylcholine (PE/PC) binding site maps to the N-terminal part of the ankyrin-binding domain of β-spectrin (ankBDn). Here we have identified the amino acid residues within this domain which are responsible for recognizing monolayers and bilayers composed of PE/PC mixtures. In vitro binding studies revealed that a quadruple mutant with substituted hydrophobic residues W1771, L1775, M1778 and W1779 not only failed to effectively bind PE/PC, but its residual PE/PC-binding activity was insensitive to inhibition with ankyrin. Structure prediction and analysis, supported by in vitro experiments, suggests that "opening" of the coiled-coil structure underlies the mechanism of this interaction. Experiments on red blood cells and HeLa cells supported the conclusions derived from the model and in vitro lipid-protein interaction results, and showed the potential physiological role of this binding. We postulate that direct interactions between spectrin ankBDn and PE-rich domains play an important role in stabilizing the structure of the spectrin-based membrane skeleton.
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:thuem
Affiliations:MPI für molekulare Zellbiologie und Genetik
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.