ArticleBiophysical journal1996
Control of band 3 lateral and rotational mobility by band 4.2 in intact erythrocytes: release of band 3 oligomers from low-affinity binding sites.
Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed, 46 citations in OpenAlex.
- Antioxidant Effects ofOxidative medicine and cellular longevity · 2019Article
- Refined views of multi-protein complexes in the erythrocyte membrane.Blood cells, molecules & diseases · 2012Review
- Diagnostic power of laboratory tests for hereditary spherocytosis: a comparison study in 150 patients grouped according to molecular and clinical characteristics.Haematologica · 2012Article
- Investigating the key membrane protein changes during in vitro erythropoiesis of protein 4.2 (-) cells (mutations Chartres 1 and 2).Haematologica · 2010Article
- Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid alpha-spectrin in a calcium- and calmodulin-dependent manner.The Journal of biological chemistry · 2010Article
- Integral protein linkage and the bilayer-skeletal separation energy in red blood cells.Biophysical journal · 2008Article
- Associations of protein 4.2 with band 3 and ankyrin.Molecular and cellular biochemistry · 2006Article
- Mapping of a spectrin-binding domain of human erythrocyte membrane protein 4.2.The Biochemical journal · 2002Article
- Flexibility of the cytoplasmic domain of the anion exchange protein, band 3, in human erythrocytes.Biophysical journal · 2001Article
- Mild spherocytosis and altered red cell ion transport in protein 4. 2-null mice.The Journal of clinical investigation · 1999Article
- Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2.The Biochemical journal · 1999Article
- Membrane dynamics of the water transport protein aquaporin-1 in intact human red cells.Biophysical journal · 1999Article
- Weak dependence of mobility of membrane protein aggregates on aggregate size supports a viscous model of retardation of diffusion.Biophysical journal · 1999Article
- Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton.The Journal of cell biology · 1998Article
- Oligomeric state of human erythrocyte band 3 measured by fluorescence resonance energy homotransfer.Biophysical journal · 1998Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
Abstract
Band 4.2 is a human erythrocyte membrane protein of incompletely characterized structure and function. Erythrocytes deficient in band 4.2 protein were used to examine the functional role of band 4.2 in intact erythrocyte membranes. Both the lateral and the rotational mobilities of band 3 were increased in band 4.2-deficient erythrocytes compared to control cells. In contrast, the lateral mobility of neither glycophorins nor a fluorescent phospholipid analog was altered in band 4.2-deficient cells. Compared to controls, band 4.2-deficient erythrocytes manifested a decreased ratio of band 3 to spectrin, and band 4.2-deficient membrane skeletons had decreased extractability of band 3 under low-salt conditions. Normal band 4.2 was found to bind to spectrin in solution and to promote the binding of spectrin to ankyrin-stripped inside-out vesicles. We conclude that band 4.2 provides low-affinity binding sites for both band 3 oligomers and spectrin dimers on the human erythrocyte membrane. Band 4.2 may serve as an accessory linking protein between the membrane skeleton and the overlying lipid bilayer.
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