Fatty acid composition of lipids which copurify with band 3

Maneri, Leonard Remo; Low, Philip S.

doi:10.1016/0006-291x(89)92209-2

Cited by 22 publications

(10 citation statements)

References 28 publications

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“…When the results obtained from this study are considered with the findings of others concerning 1) putative conformational changes associated with band 3 oligomerization (Casey and Reithmeier, 1991;Salhany et al, 1997;Schopfer and Salhany, 1992;Vince et al, 1997); 2) the role of ligands in stabilizing dimeric band 3 in vitro (Maneri and Low, 1989;Schopfer and Salhany, 1992;Vince et al, 1997); and 3) the binding of ankyrin to band 3, which shifts the monomer/dimer/tetramer equilibrium in favor of the tetramer (Huber et al, 1996), a model describing solubilized band 3 hydrodynamic behavior may be proposed: FIGURE 6 Fitting of data obtained from the Omega function analysis. The best fit for the sample at 5000 rpm was obtained from a dimer/ tetramer/hexamer model of the pooled data from Fig.…”

Section: Discussionsupporting

confidence: 57%

“…Second, the number of lipids copurifying with band 3 has been shown to be critical to the oligomeric state of the protein. Band 3 copurifies with five to seven tightly bound long-chain phospholipids, and removal of these phospholipids by prolonged washing of the matrix-bound protein promotes aggregation (Maneri and Low, 1989). Differences between the two studies may be due to differences in the column washing procedures employed.…”

Section: Discussionmentioning

confidence: 99%

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Hydrodynamic Properties of Human Erythrocyte Band 3 Solubilized in Reduced Triton X-100

Taylor

Boulter

Harding

et al. 1999

Biophysical Journal

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The oligomeric state and function of band 3, purified by sulfhydryl affinity chromatography in reduced Triton X-100, was investigated. Size exclusion high-performance liquid chromatography showed that a homogeneous population of band 3 dimers could be purified from whole erythrocyte membranes. The elution profile of band 3 purified from membranes that had been stripped of its cytoskeleton before solubilization was a broad single peak describing a heterogeneous population of oligomers with a mean Stokes radius of 100 A. Sedimentation velocity ultracentrifugation analysis confirmed particle heterogeneity and further showed monomer/dimer/tetramer equilibrium self-association. Whether the conversion of dimer to the form described by a Stokes radius of 100 A was initiated by removal of cytoskeletal components, alkali-induced changes in band 3 conformation, or alkali-induced loss of copurifying ligands remains unclear. After incubation at 20 degrees C for 24 h, both preparations of band 3 converted to a common form characterized by a mean Stokes radius of 114 A. This form of the protein, examined by equilibrium sedimentation ultracentrifugation, is able to self-associate reversibly, and the self-association can be described by a dimer/tetramer/hexamer model, although the presence of higher oligomers cannot be discounted. The ability of the different forms of the protein to bind stilbene disulfonates revealed that the dimer had the highest inhibitor binding affinity, and the form characterized by a mean Stokes radius of 114 A to have the lowest.

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Section: Discussionsupporting

confidence: 57%

Section: Discussionmentioning

confidence: 99%

Hydrodynamic Properties of Human Erythrocyte Band 3 Solubilized in Reduced Triton X-100

Taylor

Boulter

Harding

et al. 1999

Biophysical Journal

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“…This observation is surprising as AE1’s extracellular surface does not contain secondary structure elements compared to e.g., NDCBE (SLC4A8) 13 . We also reveal several bound lipids and sterols, whose effects on AE1 structure and function have been heavily speculated on 19,27,28 . Contrasting previous studies that propose cholesterol at the dimer interface, we only observe cholesterol bound on membrane-facing surfaces 19 .…”

Section: Discussionmentioning

confidence: 93%

Substrate Binding and Inhibition of the Anion Exchanger 1 Transporter

Capper

Yang

Stone

et al. 2022

Preprint

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Anion Exchanger 1 (AE1, SLC4A1) is the primary bicarbonate (HCO3-) transporter expressed in erythrocyte membranes where it mediates transport of CO2 between lungs and other tissues via import/export of bicarbonate. It is also a key regulator of erythrocyte structure and antigenic recognition. Previous biochemical studies, and a low-resolution crystal structure of the transmembrane domain have provided initial insight into AE1 structure and function. However, key questions remain regarding substrate binding and transport as well as the mechanism of inhibition. The orientation of the intracellular domain as well as the localization of lipid and sterol binding sites also remain enigmatic. We herein present seven novel high resolution cryo-EM structures of the full length human transporter in the apo, bicarbonate-bound, and several inhibitor-bound states combined with uptake- and computational studies. To our knowledge, these studies represent the first full length human, and substrate bound, SLC4 transporter structure. Our results reveal important molecular details about substrate binding and transport, as well as the diverse mechanisms of AE1 inhibition by both research chemicals and prescription drugs. We also provide novel insights into the full-length transporter architecture, identify the conformational space of the Diego blood antigen system and elucidate multiple lipid and sterol binding sites.

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“…Some crystal structures of membrane proteins contain tightly-bound lipids, including cholesterol (Hunte and Richers, 2008). In the case of Band 3, removing these lipids results in destabilization of the protein and aggregation (Maneri and Low, 1989;Vince et al, 1997). Lipids play a key role in oligomerization of membrane transporters (Gupta et al, 2017).…”

Section: Molecular Dynamics Simulationsmentioning

confidence: 99%

Organization and Dynamics of the Red Blood Cell Band 3 Anion Exchanger SLC4A1: Insights From Molecular Dynamics Simulations

Kalli

Reithmeier

2022

Front. Physiol.

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Molecular dynamics (MD) simulations have provided new insights into the organization and dynamics of the red blood cell Band 3 anion exchanger (AE1, SLC4A1). Band 3, like many solute carriers, works by an alternating access mode of transport where the protein rapidly (104/s) changes its conformation between outward and inward-facing states via a transient occluded anion-bound intermediate. While structural studies of membrane proteins usually reveal valuable structural information, these studies provide a static view often in the presence of detergents. Membrane transporters are embedded in a lipid bilayer and associated lipids play a role in their folding and function. In this review, we highlight MD simulations of Band 3 in realistic lipid bilayers that revealed specific lipid and protein interactions and were used to re-create a model of the Wright (Wr) blood group antigen complex of Band 3 and Glycophorin A. Current MD studies of Band 3 and related transporters are focused on describing the trajectory of substrate binding and translocation in real time. A structure of the intact Band 3 protein has yet to be achieved experimentally, but cryo-electron microscopy in combination with MD simulations holds promise to capture the conformational changes associated with anion transport in exquisite molecular detail.

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Fatty acid composition of lipids which copurify with band 3

Cited by 22 publications

References 28 publications

Hydrodynamic Properties of Human Erythrocyte Band 3 Solubilized in Reduced Triton X-100

Hydrodynamic Properties of Human Erythrocyte Band 3 Solubilized in Reduced Triton X-100

Substrate Binding and Inhibition of the Anion Exchanger 1 Transporter

Organization and Dynamics of the Red Blood Cell Band 3 Anion Exchanger SLC4A1: Insights From Molecular Dynamics Simulations

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