Topology models of anion exchanger 1 that incorporate the anti-parallel V-shaped motifs found in the EM structureThis paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health and Disease, and has undergone the Journal’s usual peer review process.

Hirai, Takeshi; Yamaguchi, Tomohiro; Ikeda, Yoshikazu

doi:10.1139/o10-160

Cited by 13 publications

(7 citation statements)

References 64 publications

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“…These observations further support our conclusion that the epitope(s) for mono-specific anti-5C IgY antibody is exposed on the surface of normal RBCs. Our findings provide direct evidence for the exofacial folding of 5C and 6A regions of band 3 in the normal human RBC membrane, thus lending support to multiple topology models for human RBC band 3 delineating the TM10-12 segments of the membrane domain [42–46]. …”

Section: Discussionsupporting

confidence: 60%

“…Three independent topology models predict a significant part of the 5C region is exposed on the RBC surface [42–44], and two of these models suggest a considerable part of the 6A region is also exposed [43, 44]. Recent determination of the structure of Band 3/AE1 membrane domain dimer at 7.5-Å resolution by electron microscopy revealed a partial exposure of the 5ABC region, particularly sequence corresponding to the 5C region, and somewhat ambiguous topology of the 6A region [45, 46]. Despite these structural insights, conclusive biochemical validation of the accessibility of specific regions of band 3 in intact erythrocytes is lacking.…”

Section: Introductionmentioning

confidence: 99%

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Human erythrocyte band 3 functions as a receptor for the sialic acid-independent invasion of Plasmodium falciparum. Role of the RhopH3–MSP1 complex

Baldwin

Yamodo

Ranjan

et al. 2014

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Plasmodium falciparum takes advantage of two broadly defined alternate invasion pathways when infecting human erythrocytes: one that depends on and the other that is independent of host sialic acid residues on the erythrocyte surface. Within the sialic acid-dependent (SAD) and sialic acid-independent (SAID) invasion pathways, several alternate host receptors are used by Plasmodium falciparum based on its particular invasion phenotype. Earlier, we reported that two putative extracellular regions of human erythrocyte band 3 termed 5C and 6A function as host invasion receptor segments binding parasite proteins MSP1 and MSP9 via a SAID mechanism. In this study, we developed two mono-specific anti-peptide chicken IgY antibodies to demonstrate that the 5C and 6A regions of band 3 are exposed on the surface of human erythrocytes. These antibodies inhibited erythrocyte invasion by the Plasmodium falciparum 3D7 and 7G8 strains (SAID invasion phenotype), and the blocking effect was enhanced in sialic acid-depleted erythrocytes. In contrast, the IgY antibodies had only a marginal inhibitory effect on FCR3 and Dd2 strains (SAD invasion phenotype). A direct biochemical interaction between erythrocyte band 3 epitopes and parasite RhopH3, identified by the yeast two-hybrid screen, was established. RhopH3 formed a complex with MSP119 and 5ABC region of band 3, and a recombinant segment of RhopH3 inhibited parasite invasion in human erythrocytes. Together, these findings provide evidence that erythrocyte band 3 functions as a major host invasion receptor in the SAID invasion pathway by assembling a multi-protein complex composed of parasite ligands RhopH3 and MSP1.

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Section: Discussionsupporting

confidence: 60%

Section: Introductionmentioning

confidence: 99%

Human erythrocyte band 3 functions as a receptor for the sialic acid-independent invasion of Plasmodium falciparum. Role of the RhopH3–MSP1 complex

Baldwin

Yamodo

Ranjan

et al. 2014

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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“…In support of the above model, the three-dimensional structure of the AE1 membrane domain shows V-shaped densities near the center of the dimer at 7.5 Å resolution (Hirai, Hamasaki, Yamaguchi, & Ikeda, 2011; Yamaguchi et al, 2010). Interestingly, similar V-shaped densities exist in the previously reported structure of a prokaryotic chloride channel (ClC) protein.…”

Section: Structure Of Slc4a Transporterssupporting

confidence: 62%

SLC4A Transporters

Choi

2012

Current Topics in Membranes

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SLC4A gene family proteins include bicarbonate transporters that move HCO3− across the plasma membrane and regulate intracellular pH and transepithelial movement of acid–base equivalents. These transporters are Cl/HCO3 exchangers, electrogenic Na/HCO3 cotransporters, electroneutral Na/HCO3 cotransporters, and Na+-driven Cl/HCO3 exchanger. Studies of the bicarbonate transporters in vitro and in vivo have demonstrated their physiological importance for acid–base homeostasis at the cellular and systemic levels. Recent advances in structure/function analysis have also provided valuable information on domains or motifs critical for regulation, ion translocation, and protein topology. This chapter focuses on the molecular mechanisms of ion transport along with associated structural aspects from mutagenesis of particular residues and from chimeric constructs. Structure/function studies have helped to understand the mechanism by which ion substrates are moved via the transporters. This chapter also describes some insights into the structure of SLC4A1 (AE1) and SLC4A4 (NBCe1) transporters. Finally, as some SLC4A transporters exist in concert with other proteins in the cells, the structural features associated with protein–protein interactions are briefly discussed.

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“…We have identified cross-links between several AE1 cytoplasmic domains, and structural models for the protein are currently being developed. Additionally, the cross-linking data have allowed us to resolve one key controversy concerning this protein, which is whether the transmembrane antiporter is comprised of 12 or 14 transmembrane spans [89], as the cross-linking data is only consistent with the 14-span model.…”

Section: Further Enhancing Zero-length Cx-msmentioning

confidence: 99%

Probing structures of large protein complexes using zero-length cross-linking

Rivera-Santiago

Sriswasdi

Harper

et al. 2015

Methods

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Structural mass spectrometry (MS) is a field with growing applicability for addressing complex biophysical questions regarding proteins and protein complexes. One of the major structural MS approaches involves the use of chemical cross-linking coupled with MS analysis (CX-MS) to identify proximal sites within macromolecules. Identified cross-linked sites can be used to probe novel protein–protein interactions or the derived distance constraints can be used to verify and refine molecular models. This review focuses on recent advances of “zero-length” cross-linking. Zero-length cross-linking reagents do not add any atoms to the cross-linked species due to the lack of a spacer arm. This provides a major advantage in the form of providing more precise distance constraints as the cross-linkable groups must be within salt bridge distances in order to react. However, identification of cross-linked peptides using these reagents presents unique challenges. We discuss recent efforts by our group to minimize these challenges by using multiple cycles of LC–MS/MS analysis and software specifically developed and optimized for identification of zero-length cross-linked peptides. Representative data utilizing our current protocol are presented and discussed.

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Cited by 13 publications

References 64 publications

Human erythrocyte band 3 functions as a receptor for the sialic acid-independent invasion of Plasmodium falciparum. Role of the RhopH3–MSP1 complex

Human erythrocyte band 3 functions as a receptor for the sialic acid-independent invasion of Plasmodium falciparum. Role of the RhopH3–MSP1 complex

SLC4A Transporters

Probing structures of large protein complexes using zero-length cross-linking

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