Functional interaction between Rh proteins and the spectrin-based skeleton in erythroid and epithelial cells.
We summarize the different experimental approaches which provide evidence that direct interaction of Rh and RhAG to ankyrin-R constitutes, together with the AE-1 (Band 3)-ankyrin-protein 4.2 and GPC-protein 4.1-p55 complexes, another major anchoring site between the red cell membrane bilayer and the underlying spectrin-based skeleton. The observations that some residues of the ankyrin binding site are mutated in Rh and RhAG proteins from some weak D and Rh(null) variants, respectively, suggest that the Rh-RhAG/ankyrin-R interaction plays a crucial role in the biosynthesis and/or the stability of the Rh complex in the red cell membrane. Similarly, binding to ankyrin G is required for cell surface expression of the non-erythroid member of the Rh protein family, RhBG, at the basolateral membrane domain of polarized epithelial cells. The next challenge will be to determine whether binding to the membrane skeleton may be critical for the emerging ammonium transport function of Rh proteins in erythroid and non-erythroid cells.
Inserm, U665, F-75015 Paris, France.
V
V
Nicolas
I
I
Mouro-Chanteloup
C
C
Lopez
P
P
Gane
A
A
Gimm
N
N
Mohandas
J-P
JP
Cartron
C
C
Le Van Kim
Y
Y
Colin
D000818:Animals; D017487:Ankyrins / Q000378:metabolism; D001665:Binding Sites; D001798:Blood Proteins / Q000378:metabolism; D051928:CD47 Antigen / Q000378:metabolism; D016764:Cell Polarity; D003598:Cytoskeletal Proteins / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism*; D004847:Epithelial Cells / Q000378:metabolism* / Q000648:ultrastructure; D041905:Erythroid Cells / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D008562:Membrane Glycoproteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D008954:Models, Biological; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012204:Rh-Hr Blood-Group System / Q000378:metabolism*; D013049:Spectrin / Q000378:metabolism*; D013102:Spherocytes / Q000378:metabolism / Q000648:ultrastructure; D013329:Structure-Activity Relationship; D020798:Two-Hybrid System Techniques
C110202:ANK1 protein, human; C490613:ANK3 protein, human; D017487:Ankyrins; D001798:Blood Proteins; D051928:CD47 Antigen; D003598:Cytoskeletal Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; C498523:RHAG protein, human; D011993:Recombinant Fusion Proteins; D012204:Rh-Hr Blood-Group System; C028841:erythrocyte membrane band 4.1 protein; C044791:erythrocyte membrane band 4.2 protein; D013049:Spectrin