scholarly journals Crystal structure of the anion exchanger domain of human erythrocyte band 3

Science ◽  
2015 ◽  
Vol 350 (6261) ◽  
pp. 680-684 ◽  
Author(s):  
T. Arakawa ◽  
T. Kobayashi-Yurugi ◽  
Y. Alguel ◽  
H. Iwanari ◽  
H. Hatae ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Anion Exchanger ◽  
Human Erythrocyte ◽  
Band 3

scholarly journals Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3.

1994 ◽  
Vol 13 (14) ◽  
pp. 3230-3235 ◽  
Author(s):  
D.N. Wang ◽  
V.E. Sarabia ◽  
R.A. Reithmeier ◽  
W. Kühlbrandt
Keyword(s):  
Anion Exchanger ◽  
Human Erythrocyte ◽  
Three Dimensional ◽  
Band 3 ◽  
Membrane Domain

scholarly journals Transmembrane folding of the human erythrocyte anion exchanger (AE1, Band 3) determined by scanning and insertional N-glycosylation mutagenesis

1999 ◽  
Vol 339 (2) ◽  
pp. 269-279 ◽  
Author(s):  
Milka POPOV ◽  
Jing LI ◽  
Reinhart A. F. REITHMEIER
Keyword(s):  
Anion Exchanger ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Translation System ◽  
Acceptor Site ◽  
Oligosaccharide Structure ◽  
Hek 293 ◽  
Transmembrane Segments ◽  
Free Translation ◽  
A Cell

The human erythrocyte anion exchanger (AE1, Band 3) contains up to 14 transmembrane segments, with a single site of N-glycosylation at Asn642 in extracellular (EC) loop 4. Scanning and insertional N-glycosylation mutagenesis were used to determine the folding pattern of AE1 in the membrane. Full-length AE1, when expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells, retained a high-mannose oligosaccharide structure. Scanning N-glycosylation mutagenesis of EC loop 4 showed that N-glycosylation acceptor sites (Asn-Xaa-Ser/Thr) spaced 12 residues from the ends of adjacent transmembrane segments could be N-glycosylated. An acceptor site introduced at position 743 in intracellular (IC) loop 5 that could be N-glycosylated in a cell-free translation system was not N-glycosylated in transfected cells. Mutations designed to disrupt the folding of this loop enhanced the level of N-glycosylation at Asn743in vitro. The results suggest that this loop might be transiently exposed to the lumen of the endoplasmic reticulum during biosynthesis but normally folds rapidly, precluding N-glycosylation. EC loop 4 insertions into positions 428, 484, 754 and 854 in EC loops 1, 2, 6 and 7 respectively were efficiently N-glycosylated, showing that these regions were extracellular. EC loop 4 insertions into positions 731 or 785 were poorly N-glycosylated, which was inconsistent with an extracellular disposition for these regions of AE1. Insertion of EC loop 4 into positions 599 and 820 in IC loops 3 and 6 respectively were not N-glycosylated in cells, which was consistent with a cytosolic disposition for these loops. Inhibitor-affinity chromatography with 4-acetamido-4´-isothiocyanostilbene-2,2´-disulphonate (SITS)-Affi-Gel was used to assess whether the AE1 mutants were in a native state. Mutants with insertions at positions 428, 484, 599, 731 and 785 showed impaired inhibitor binding, whereas insertions at positions 754, 820 and 854 retained binding. The results indicate that the folding of the C-terminal region of AE1 is more complex than originally proposed and that this region of the transporter might have a dynamic aspect.

Structural and functional consequences of an N-glycosylation mutation (HEMPAS) affecting human erythrocyte membrane glycoproteins

1998 ◽  
Vol 76 (5) ◽  
pp. 823-835 ◽  
Author(s):  
Homa Kameh ◽  
Carolina Landolt-Marticorena ◽  
Jeffrey HM Charuk ◽  
Harry Schachter ◽  
Reinhart AF Reithmeier
Keyword(s):  
Erythrocyte Membrane ◽  
Anion Exchanger ◽  
Human Erythrocyte ◽  
Glucose Transporter ◽  
Lectin Binding ◽  
Genetic Defect ◽  
Band 3 ◽  
Lymphoid Cells ◽  
Detergent Solution ◽  
Oligosaccharide Structure

Band 3, the human erythrocyte anion exchanger (AE1), and the glucose transporter (GLUT1) proteins each contain a single site of N-glycosylation that is heterogeneously glycosylated. Lectin binding and enzymatic deglycosylation assays showed that the polylactosaminyl oligosaccharide structure of these glycoproteins was altered to a high mannose or hybrid glycan form in three patients with hereditary erythroblastic multinuclearity, with a positive acidified-serum lysis test (HEMPAS). Offspring from one of the HEMPAS patients had intermediate levels of polylactosaminyl oligosaccharide associated with AE1 and GLUT1, suggesting they may have been heterozygous for the genetic defect. The array of polylactosaminyl-containing glycoproteins present in EBV-transformed lymphoblasts derived from fresh blood of HEMPAS patients was similar to control lymphoblasts. HEMPAS lymphoblasts do not therefore express the defect in polylactosamine synthesis found in erythroid cells, indicating that lymphoid cells are not deficient in the processing enzymes or contain an alternative oligosaccharide processing pathway. Purified HEMPAS band 3 had an unaltered oligomeric structure but dimers aggregated more rapidly in detergent solution than normal band 3. The altered oligosaccharide structure did not affect the sensitivity of band 3 to proteolytic digestion in intact red cells but a greater amount of HEMPAS band 3 was associated with the cytoskeleton. The transport activities of AE1 and GLUT1 in HEMPAS erythrocytes were similar to those in normal controls. This shows that the HEMPAS glycosylation defect does not impair the functional accumulation of these two important erythrocyte membrane transporters even though it produces subtle structural changes in band 3 that result in its increased cytoskeletal interaction and self association in detergent solution.Key words: anion exchanger, band 3, erythrocyte, glycoprotein, HEMPAS.

Crystallization of Human Erythrocyte Band 3, the anion exchanger, at the International Space Station “KIBO”

2018 ◽  
Vol 559 ◽  
pp. 91-93 ◽  
Author(s):  
Hinako Hatae ◽  
Koji Inaka ◽  
Ryo Okamura ◽  
Naoki Furubayashi ◽  
Masayuki Kamo ◽  
...  
Keyword(s):  
International Space Station ◽  
Anion Exchanger ◽  
Human Erythrocyte ◽  
Space Station ◽  
Band 3 ◽  
International Space
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