Helical image reconstruction of the outward-open human erythrocyte band 3 membrane domain in tubular crystals

Yamaguchi, Tomohiro; Fujii, Takashi; Abe, Yoshito; Hirai, Takeshi; Kang, Dongchon; Namba, Keiichi; Mitsuoka, Kaoru

doi:10.1016/j.jsb.2009.12.009

Cited by 15 publications

(9 citation statements)

References 45 publications

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“…Finally, a glutamate in putative TM8 forms an important part of the transport gate of AE1 (437,438,440,443). The three-dimensional structure of the AE1 TMD dimer has been solved at 7.5-Å resolution using cryo-electron microscopy (1068,1069). However, this resolution is not sufficient to visualize all TMs nor to assign amino acid sequence to regions of electron density.…”

Section: Structural Features and Variantsmentioning

confidence: 99%

The Divergence, Actions, Roles, and Relatives of Sodium-Coupled Bicarbonate Transporters

Parker

Boron

2013

Physiological Reviews

248

262

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The mammalian Slc4 (Solute carrier 4) family of transporters is a functionally diverse group of 10 multi-spanning membrane proteins that includes three Cl-HCO3 exchangers (AE1-3), five Na(+)-coupled HCO3(-) transporters (NCBTs), and two other unusual members (AE4, BTR1). In this review, we mainly focus on the five mammalian NCBTs-NBCe1, NBCe2, NBCn1, NDCBE, and NBCn2. Each plays a specialized role in maintaining intracellular pH and, by contributing to the movement of HCO3(-) across epithelia, in maintaining whole-body pH and otherwise contributing to epithelial transport. Disruptions involving NCBT genes are linked to blindness, deafness, proximal renal tubular acidosis, mental retardation, and epilepsy. We also review AE1-3, AE4, and BTR1, addressing their relevance to the study of NCBTs. This review draws together recent advances in our understanding of the phylogenetic origins and physiological relevance of NCBTs and their progenitors. Underlying these advances is progress in such diverse disciplines as physiology, molecular biology, genetics, immunocytochemistry, proteomics, and structural biology. This review highlights the key similarities and differences between individual NCBTs and the genes that encode them and also clarifies the sometimes confusing NCBT nomenclature.

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Section: Structural Features and Variantsmentioning

confidence: 99%

The Divergence, Actions, Roles, and Relatives of Sodium-Coupled Bicarbonate Transporters

Parker

Boron

2013

Physiological Reviews

248

262

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“…Whereas it is depicted as a typical electroneutral anion exchanger, the anion exchange rate through AE1 is extremely fast (10 000 per second) and Cl − slippage occurs occasionally (1 for 10 000 exchange). Crystallographic structures are not available yet with enough resolution to help understand the transport mechanism [53]. This mechanism should allow very rapid conformational changes that could resemble alternately opened gates for instance.…”

Section: Introductionmentioning

confidence: 99%

Band 3 Missense Mutations and Stomatocytosis: Insight into the Molecular Mechanism Responsible for Monovalent Cation Leak

Barneaud-Rocca

Pellissier

Borgèse

et al. 2011

International Journal of Cell Biology

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Missense mutations in the erythroid band 3 protein (Anion Exchanger 1) have been associated with hereditary stomatocytosis. Features of cation leaky red cells combined with functional expression of the mutated protein led to the conclusion that the AE1 point mutations were responsible for Na+ and K+ leak through a conductive mechanism. A molecular mechanism explaining mutated AE1-linked stomatocytosis involves changes in AE1 transport properties that become leaky to Na+ and K+. However, another explanation suggests that point-mutated AE1 could regulate a cation leak through other transporters. This short paper intends to discuss these two alternatives.

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“…The 10th membrane region is thought to be very flexible because residues near K743 are observed on the external side in some experiments 27,31 and on the cytoplasmic side in others. 41,44 Although the protein has been studied for a long time, only low-resolution structures, derived from two-dimensional (2D) crystals by negative stain 45 and tubular crystal, 46 were available for the AE1 membrane domain. Here, we report 7.5-Å-resolution projection and a three-dimensional (3D) map solved by cryo-electron crystallography using a 2D crystal.…”

Section: Introductionmentioning

confidence: 99%

Structure of the Membrane Domain of Human Erythrocyte Anion Exchanger 1 Revealed by Electron Crystallography

Yamaguchi

Ikeda

Abe

et al. 2010

Journal of Molecular Biology

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Helical image reconstruction of the outward-open human erythrocyte band 3 membrane domain in tubular crystals

Cited by 15 publications

References 45 publications

The Divergence, Actions, Roles, and Relatives of Sodium-Coupled Bicarbonate Transporters

The Divergence, Actions, Roles, and Relatives of Sodium-Coupled Bicarbonate Transporters

Band 3 Missense Mutations and Stomatocytosis: Insight into the Molecular Mechanism Responsible for Monovalent Cation Leak

Structure of the Membrane Domain of Human Erythrocyte Anion Exchanger 1 Revealed by Electron Crystallography

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