Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger (band 3, AE1)

1998 ◽  
Vol 26 (3) ◽  
pp. 516-520 ◽  
Author(s):  
E. J. Chambers ◽  
D. Askin ◽  
G. B. Bloomberg ◽  
S. M. Ring ◽  
M. J. A. Tanner
Keyword(s):  
Anion Exchanger ◽  
Band 3 ◽  
Red Cell ◽  
Transmembrane Region ◽  
Cytoplasmic Loop

scholarly journals Band 3, the human red cell chloride/bicarbonate anion exchanger (AE1, SLC4A1), in a structural context

2016 ◽  
Vol 1858 (7) ◽  
pp. 1507-1532 ◽  
Author(s):  
Reinhart A.F. Reithmeier ◽  
Joseph R. Casey ◽  
Antreas C. Kalli ◽  
Mark S.P. Sansom ◽  
Yilmaz Alguel ◽  
...  
Keyword(s):  
Anion Exchanger ◽  
Band 3 ◽  
Red Cell ◽  
Structural Context

Physiological influence of complete lack of red cell anion exchanger in cattle with hereditary band 3 deficiency

1994 ◽  
Vol 1 ◽  
pp. 235
Author(s):  
Mutsumi Inaba ◽  
Miyuki Takeuchi ◽  
Kota Sato ◽  
Ken-ichiro Ono ◽  
Yoshimitsu Maede
Keyword(s):  
Anion Exchanger ◽  
Band 3 ◽  
Red Cell

Heterologous expression of the red-cell anion exchanger (band 3; AEI)

1999 ◽  
Vol 27 (6) ◽  
pp. 917-923 ◽  
Author(s):  
Jonathan D. Groves ◽  
Mark D. Parker ◽  
David Askin ◽  
Pierre Falson ◽  
Marc le Maire ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Anion Exchanger ◽  
Band 3 ◽  
Red Cell

Structural Studies on the Effects of the Deletion in the Red Cell Anion Exchanger (band 3, AE1) Associated with South East Asian Ovalocytosis

1999 ◽  
Vol 285 (3) ◽  
pp. 1289-1307 ◽  
Author(s):  
Eric J. Chambers ◽  
Graham B. Bloomberg ◽  
Susan M. Ring ◽  
Michael J.A. Tanner
Keyword(s):  
Anion Exchanger ◽  
East Asian ◽  
Band 3 ◽  
Red Cell ◽  
Structural Studies

scholarly journals Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1)

1999 ◽  
Vol 344 (3) ◽  
pp. 687-697 ◽  
Author(s):  
Jonathan D. GROVES ◽  
Michael J. A. TANNER
Keyword(s):  
Anion Exchanger ◽  
Band 3 ◽  
Glycosylation Site ◽  
Intramolecular Interactions ◽  
Red Cell ◽  
Chloride Uptake ◽  
C Terminus ◽  
Free Translation ◽  
Membrane Spanning ◽  
General Method

The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642. We have shown that the integrity of six different loops are not essential for stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes. We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation. The fragments initiating in the loops preceding spans 2, 9 and 11 did not insert into the membrane with the expected orientation. Furthermore, N-glycosylation of Asn-642 might facilitate the membrane integration of span 7. The correct integration of spans 2-3 required the presence of the region containing span 4 and that the luminal exposure of the C-terminus of span 7 is increased in the presence of the region including span 6 or span 8. The results suggest the span 8 region is required for the correct folding of spans 9-10, at least in the presence of the span 11-12 region. Our results suggest that there are intramolecular interactions between the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12. Spans 1, 4, 5, 6 and 8 might act as a scaffold for the assembly of spans 2-3, 7 and 9-10. This approach might provide a general method for dissecting the interactions between membrane-spanning regions of polytopic membrane proteins.

scholarly journals Complementation studies with co-expressed fragments of human red cell band 3 (AE1): the assembly of the anion-transport domain in Xenopus oocytes and a cell-free translation system

1998 ◽  
Vol 332 (1) ◽  
pp. 161-171 ◽  
Author(s):  
Jonathan D. GROVES ◽  
Lin WANG ◽  
Michael J. A. TANNER
Keyword(s):  
Xenopus Oocytes ◽  
Band 3 ◽  
Translation System ◽  
Red Cell ◽  
Membrane Domain ◽  
Cytoplasmic Loop ◽  
Free System ◽  
Anion Transporter ◽  
Free Translation ◽  
The Individual

We examined the assembly of the membrane domain of the human red cell anion transporter (band 3; AE1) by co-expression of recombinant N- and C-terminal fragments in Xenopus oocytes and in cell-free translation with canine pancreatic microsomes. Co-immunoprecipitation was performed in non-denaturing detergent solutions using antibodies directed against the N- and C-termini of the membrane domain. Eleven of the twelve fragments were expressed stably in oocytes in the presence or absence of their respective partners. However, the fragment containing from putative span nine to the C-terminus could be detected in oocytes only when co-expressed with its complementary partner containing the first eight spans. Co-expression of pairs of fragments divided in the first, second, third and fourth exofacial loops and in the fourth cytoplasmic loop resulted in a concentration-dependent association, but a pair of fragments divided in the sixth cytoplasmic loop did not co-immunoprecipitate. When two complementary fragments were translated separately in the cell-free system and the purified microsomes were then mixed, co-immunoprecipitation was observed only if the membranes were first fused using polyethylene glycol. This shows that co-immunoprecipitation results from specific interactions within the membrane and is not an artefact of detergent solubilization or immunoprecipitation. We demonstrate that band 3 assembly can occur within the membrane after translation, insertion and initial folding of the individual fragments have been completed. We conclude that most band 3 fragments contain the necessary information to fold in the membrane and adopt a structure that is sufficiently similar to the native protein that it permits correct assembly with its complementary partner.

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