Phosphorylation sites in human erythrocyte band 3 protein

Yannoukakos, Drakoulis; Vasseur, Corinne; Piau, Jean-Pierre; Wajcman, Henri; Bursaux, E

doi:10.1016/0005-2736(91)90291-f

Cited by 60 publications

(49 citation statements)

References 28 publications

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“…Spectrin/band 3 ratios were obtained by scanning the gels. Membranes were depleted of integral proteins, converted into inside-out vesicles, and treated with chymotrypsin, and the 41-43-kD cytoplasmic domain of band 3 was isolated by DE-52 cellulose column chromatography (20). This fragment was then digested with trypsin, the resulting peptides were separated by reverse phase HPLC, and their amino acid content was determined (21).…”

Section: Methodsmentioning

confidence: 99%

A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis.

Jenkins¹,

Abou‐Alfa²,

Dhermy³

et al. 1996

J. Clin. Invest.

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Section: Methodsmentioning

confidence: 99%

A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis.

Jenkins¹,

Abou‐Alfa²,

Dhermy³

et al. 1996

J. Clin. Invest.

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“…Nevertheless, a close physical proximity must be real because ankyrin also competes with other peripheral proteins that bind at the NH 2 terminus of band 3 (38) 2 . Because the NH 2 terminus of cdb3 is not only required for stable interaction with protein 4.1 (38) but also for association with various glycolytic enzymes (33,39) and p72 syk (40,41), it is also conceivable that binding of ankyrin to cdb3 might be involved in regulation of other protein interactions at the NH 2 terminus.…”

Section: Figmentioning

confidence: 99%

Identification of a Critical Ankyrin-binding Loop on the Cytoplasmic Domain of Erythrocyte Membrane Band 3 by Crystal Structure Analysis and Site-directed Mutagenesis

Chang

Low

2003

Journal of Biological Chemistry

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The cytoplasmic domain of erythrocyte membrane band 3 (cdb3) serves as a center of membrane organization, interacting with such proteins as ankyrin, protein 4.1, protein 4.2, hemoglobin, several glycolytic enzymes, a tyrosine phosphatase, and a tyrosine kinase, p72syk . The crystallographic structure of the cdb3 dimer has revealed that residues 175-185 assume a ␤-hairpin loop similar to a putative ankyrin-binding motif at the cytoplasmic surface of the Na ؉ /K ؉ -ATPase. To test whether this hairpin loop constitutes an ankyrin-binding site on cdb3, we have deleted amino acids 175-185 and substituted the 11-residue loop with a Gly-Gly dipeptide that bridges the deletion without introducing strain into the structure. Although the deletion mutant undergoes the same native conformational changes exhibited by wild type cdb3 and binds other peripheral proteins normally, the mutant exhibits no affinity for ankyrin. This suggests that the exposed ␤-hairpin turn indeed constitutes a major ankyrin-binding site on cdb3. Other biochemical studies suggest that ankyrin also docks at the NH 2 terminus of band 3. Thus, antibodies to the NH 2 terminus of cdb3 block ankyrin binding to the cdb3, and ankyrin binding to cdb3 prevents p72 syk phosphorylation of cdb3 at its NH 2 terminus (predominantly at Tyr-8). However, a truncation mutant of cdb3 lacking the NH 2 -terminal 50 residues displays the same binding affinity as wild type cdb3. These data thus suggest that the NH 2 terminus of cdb3 is proximal to but not required for the cdb3-ankyrin interaction.Ankyrin mediates the attachment of a diverse set of membrane spanning proteins to spectrin-based membrane skeletons. Depending on the cell type, ankyrin may bridge between the ␤ subunit of spectrin and the anion exchanger (1), the Na ϩ /K ϩ -ATPase (2, 3), a voltage-dependent Na ϩ channel (4), or the Na ϩ /Ca 2ϩ exchanger (5). Cell adhesion molecules such as CD44 (6) and L1CAM family members (7,8), as well as calcium-release channels such as IP3 receptor (9) and ryanodine receptor (10) are also known to associate with ankyrin.Ankyrin is folded into three independent domains that include an 89-kDa NH 2 -terminal membrane-binding domain, followed by a 62-kDa spectrin-binding domain and a COOHterminal regulatory domain. The membrane-binding domain of ankyrin consists of 24 tandem repeats of a 33-amino acid motif known as the ankyrin repeat that is involved in protein recognition (11)(12)(13)(14). Because ankyrin interacts with a highly diverse group of membrane proteins, much effort has been devoted to identifying the structural features that mediate these interactions (15-18).The major linkage between the membrane bilayer and spectrin-based cortical skeleton in erythrocytes is mediated by ankyrin binding to band 3. Because previous studies (19 -22) aimed at mapping the docking site(s) of ankyrin on the cytoplasmic domain of erythrocyte membrane band 3 (cdb3) 1 were conducted without the benefit of the crystal structure of cdb3, these investigations of necessity led to inexact conc...

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“…Tyrosine phosphorylation of membrane proteins has been implicated in regulating various functions of the red cell, including glycolysis, morphology and ion transport activity. 4,[16][17] Increased tyrosine kinase activity induced by oxidative stress has been observed in various cell types, including normal and pathologic red cells. In sickle-cell disease, exposing the red cells to deoxygenation resulted in increased tyrosine kinase activity, concommittant with cellular dehydration.…”

Section: Discussionmentioning

confidence: 99%

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Tohtong¹,

Metheenukul²,

Wilairat³

2002

ScienceAsia

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The steady-state levels of β-spectrin phosphorylation in HbH (α-thalassemia 1/α-thalassemia 2), HbH/HbConstant Spring (α-thalassemia 1/HbCS, hereafter called HbH/HbCS) and nonsplenectomized β-thalassemia/HbE (hereafter called β-thal/HbE) red cells were quantitated using Western hybridization. Phosphorylation of β-spectrin serine and threonine residues from thalassemic samples was not significantly different from normal control. However, tyrosine phosphorylation was higher than normal control in HbH (p<0.01), HbH/HbCS (p<0.05) and β-thal/HbE (p<0.05) samples. Tyrosine phosphorylation of β-spectrin was observed only in the presence of vanadate, a phenomenon not hitherto reported. As tyrosine kinase activity has been linked to oxidative stress, loss of membrane lipid asymmetry and procoagulant activity of the red cell membrane, the observed increase in β-spectrin tyrosine phosphorylation of the thalassemic red cells is likely, at least in part, to account for these parameters.

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Phosphorylation sites in human erythrocyte band 3 protein

Cited by 60 publications

References 28 publications

A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis.

A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis.

Identification of a Critical Ankyrin-binding Loop on the Cytoplasmic Domain of Erythrocyte Membrane Band 3 by Crystal Structure Analysis and Site-directed Mutagenesis

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