Identification and functional characterization of protein 4.1R and actin-binding sites in erythrocyte beta spectrin: regulation of the interactions by phosphatidylinositol-4,5-bisphosphate.

@article{An2005IdentificationAF,
  title={Identification and functional characterization of protein 4.1R and actin-binding sites in erythrocyte beta spectrin: regulation of the interactions by phosphatidylinositol-4,5-bisphosphate.},
  author={Xiuli An and Gargi Debnath and Xinhua Guo and Shuwen Liu and Samuel E. Lux and Anthony J. Baines and Walter B Gratzer and Narla Mohandas},
  journal={Biochemistry},
  year={2005},
  volume={44 31},
  pages={10681-8}
}
The ternary complex of spectrin, F-actin, and protein 4.1R defines the erythrocyte membrane skeletal network, which governs the stability and elasticity of the membrane. It has been shown that both 4.1R and actin bind to the N-terminal region (residues 1-301) of the spectrin beta chain, which contains two calponin homology domains, designated CH1 and CH2. Here, we show that 4.1R also binds to the separate CH1 and CH2 domains. Unexpectedly, truncation of the CH2 domain by its 20 amino acids… CONTINUE READING

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