Avent_fig4: Model of the band 3–Rh protein complex

Expert Reviews in Molecular Medicine: http://www.expertreviews.org/
Accession information: Vol. 8; Issue 13; 12 June 2006 Abstract
PDF

Model of the band 3–Rh protein complex

Neil D. Avent, Tracey E. Madgett, Zoe E. Lee, David J. Head, Deborah G. Maddocks and Lucy H. Skinner

Author contact details

Figure 4. Model of the band 3–Rh protein complex. Rh and band 3 proteins might form a functional CO₂/O₂ transporting complex in the red cell membrane (Refs 128, 156). Band 3 (‘anion exchanger’) protein comprises a membrane-spanning domain that exchanges chloride and bicarbonate, a C-terminal cytoplasmic domain that binds carbonic anhydrase (which catalyses the hydration of CO₂ and the dehydration of bicarbonate), and a long N-terminal cytoplasmic domain that binds haemoglobin, glyolytic enzymes, ankyrin, protein 4.2 and spectrin. The function of the N-terminal band 3 domain is to anchor the RBC membrane to the cytoskeleton. Both Rh and band 3 are known to associate directly with ankyrin through C-terminal (Rh) and N-terminal (band 3) domain associations to the D2 (Rh) and D3–D4 (band 3) domains of ankyrin. Band 3 (Ref. 103) and CD47 (Refs 98, 99, 100) also associate with protein 4.2 through C-terminal (CD47) and N-terminal (band 3) interactions. The ability of RhAG to transport ammonium bidirectionally is highlighted, which couples pH balancing of both intracellular and extracellular compartments.

References cited in Figure 4

98 Bruce, L.J. et al. (2002) Absence of CD47 in protein 4.2-deficient hereditary spherocytosis in man: an interaction between the Rh complex and the band 3 complex. Blood 100, 1878-1885, PubMed

99 Mouro-Chanteloup, I. et al. (2003) Evidence that the red cell skeleton protein 4.2 interacts with the Rh membrane complex member CD47. Blood 101, 338-344, PubMed

100 Dahl, K.N. et al. (2004) Protein 4.2 is critical to CD47-membrane skeleton attachment in human red cells. Blood 103, 1131-1136, PubMed

103 Toye, A.M. et al. (2005) Protein-4.2 association with band 3 (AE1, SLCA4) in Xenopus oocytes: effects of three natural protein-4.2 mutations associated with hemolytic anemia. Blood 105, 4088-4095, PubMed

128 Soupene, E., Inwood, W. and Kustu, S. (2004) Lack of the Rhesus protein Rh1 impairs growth of the green alga Chlamydomonas reinhardtii at high CO2. Proc Natl Acad Sci U S A 101, 7787-7792, PubMed

156 Tanner, M.J. (2002) Band 3 anion exchanger and its involvement in erythrocyte and kidney disorders. Curr Opin Hematol 9, 133-139, PubMed

| home | search | glossary | links | sitemap | contact |

Expert Reviews in Molecular Medicine © Cambridge University Press ISSN 1462-3994 (Disclaimer and copyright)
Editorial Office: Centre for Applied Research in Educational Technologies (CARET), 1st Floor, 16 Mill Lane, Cambridge, CB2 1SB, UK. Tel: +44 (0)1223 765 375; Fax: +44(0)1223 765 505; E-mail: ermm@caret.cam.ac.uk