Philippe Gascard
Japan
Review Article
4.1 Proteins: Ion Transporters in Check
Author(s): Wataru Nunomura, Hideki Wakui, Yuichi Takakuwa and Philippe GascardWataru Nunomura, Hideki Wakui, Yuichi Takakuwa and Philippe Gascard
The classical function of 4.1R in erythrocytes is to contribute to the mechanical properties of the membrane by promoting the interaction between spectrin and actin. It is now well recognized that 4.1R is required for the stable anchorage of numerous cell surface erythrocyte membrane proteins. 4.1R is the prototypical member of the family of 4.1 proteins, which are expressed in many cell types, besides erythrocytes. The other members of the protein 4.1 family include 4.1N, 4.1G, and 4.1B.NHE1 (Na+/H+ exchanger isoform 1) has been reported to be hyperactive in 4.1R-null erythrocytes, supporting a functional interaction between NHE1 and 4.1R. We recently demonstrated that 4.1R binds directly to the cytoplasmic domain of NHE1 (NHE1cd). This interaction involves an EED motif in the 4.1R FERM (4.1/ezrin/radixin/moesin) domain and two clusters of basic amino acids in the NHE1cd, K519R and R.. View More»
DOI: 10.4172/jpb.1000286
