1. Direct binding of the Na--H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation
- Author
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Derek C Huang, John Orlowski, Diane L. Barber, Sheryl P. Denker, and Heinz Furthmayr
- Subjects
Sodium-Hydrogen Exchangers ,Moesin ,Recombinant Fusion Proteins ,Molecular Sequence Data ,Arp2/3 complex ,macromolecular substances ,Cell Line ,Ezrin ,Stress Fibers ,Animals ,Humans ,Actin-binding protein ,Amino Acid Sequence ,Cytoskeleton ,Molecular Biology ,Cell Size ,Focal Adhesions ,Ion Transport ,biology ,Actin remodeling ,Membrane Proteins ,Cell Biology ,Blood Proteins ,Phosphoproteins ,Precipitin Tests ,Cell biology ,DNA-Binding Proteins ,Cytoskeletal Proteins ,Microscopy, Fluorescence ,Paracytophagy ,Mutation ,biology.protein ,MDia1 ,Protons ,Sequence Alignment ,Cell Division ,Hydrogen ,Protein Binding ,Transcription Factors - Abstract
The association of actin filaments with the plasma membrane maintains cell shape and adhesion. Here, we show that the plasma membrane ion exchanger NHE1 acts as an anchor for actin filaments to control the integrity of the cortical cytoskeleton. This occurs through a previously unrecognized structural link between NHE1 and the actin binding proteins ezrin, radixin, and moesin (ERM). NHE1 and ERM proteins associate directly and colocalize in lamellipodia. Fibroblasts expressing NHE1 with mutations that disrupt ERM binding, but not ion translocation, have impaired organization of focal adhesions and actin stress fibers, and an irregular cell shape. We propose a structural role for NHE1 in regulating the cortical cytoskeleton that is independent of its function as an ion exchanger.
- Published
- 2001