ArticleBiochemistry2011
Phosphorylation-dependent perturbations of the 4.1R-associated multiprotein complex of the erythrocyte membrane.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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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
26 citing papers in PubMed, 50 citations in OpenAlex.
- Molecular hydrogen exposure improves functional state of red blood cells in the early postoperative period: a randomized clinical study.Medical gas researchTrial
- Comprehensive Phenotypic and Proteomic Analyses of Human Reticulocyte Maturation.Blood red cells & iron · 2025Article
- Red blood cell signaling is functionally conserved iniScience · 2024Article
- Phosphoproteomics and morphology of stored human red blood cells treated by protein tyrosine phosphatases inhibitor.Blood advances · 2024Article
- The RBC's road to ghost and removal: splenic clearance.Blood advances · 2021Article
- Article
- 4.1N-Mediated Interactions and Functions in Nerve System and Cancer.Frontiers in molecular biosciences · 2021Review
- Development of Mechanical Stability in Late-Stage Embryonic Erythroid Cells: Insights From Fluorescence Imaged Micro-Deformation Studies.Frontiers in physiology · 2021Article
- Human erythrocytes: cytoskeleton and its origin.Cellular and molecular life sciences : CMLS · 2020Review
- Protein 4.1R negatively regulates CD8Immunology · 2019Article
- The Effects of Different Signaling Pathways in Adenylyl Cyclase Stimulation on Red Blood Cells Deformability.Frontiers in physiology · 2019Article
- Non-muscle myosin II drives vesicle loss during human reticulocyte maturation.Haematologica · 2018Article
- SOPflugers Archiv : European journal of physiology · 2017Article
- Epitope-Specific Suppression of IgG Responses by Passively Administered Specific IgG: Evidence of Epitope Masking.Frontiers in immunology · 2017Article
- Band 3 Erythrocyte Membrane Protein Acts as Redox Stress Sensor Leading to Its Phosphorylation by p (72) Syk.Oxidative medicine and cellular longevity · 2016Article
- The human Kell blood group binds the erythroid 4.1R protein: new insights into the 4.1R-dependent red cell membrane complex.British journal of haematology · 2015Article
- Spectrin and phospholipids - the current picture of their fascinating interplay.Cellular & molecular biology letters · 2014Review
- Article
- A deep intronic mutation in the ankyrin-1 gene causes diminished protein expression resulting in hemolytic anemia in mice.G3 (Bethesda, Md.) · 2013Article
- Involvement of Src in the membrane skeletal complex, MPP6-4.1G, in Schmidt-Lanterman incisures of mouse myelinated nerve fibers in PNS.Histochemistry and cell biology · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The bulk of the red blood cell membrane proteins are partitioned between two multiprotein complexes, one associated with ankyrin R and the other with protein 4.1R. Here we examine the effect of phosphorylation of 4.1R on its interactions with its partners in the membrane. We show that activation of protein kinase C in the intact cell leads to phosphorylation of 4.1R at two sites, serine 312 and serine 331. This renders the 4.1R-associated transmembrane proteins GPC, Duffy, XK, and Kell readily extractable by nonionic detergent with no effect on the retention of band 3 and Rh, both of which also interact with 4.1R. In solution, phosphorlyation at either serine suppresses the capacity of 4.1R to bind to the cytoplasmic domains of GPC, Duffy, and XK. Phosphorylation also exerts an effect on the stability in situ of the ternary spectrin-actin-4.1R complex, which characterizes the junctions of the membrane skeletal network, as measured by the enhanced competitive entry of a β-spectrin peptide possessing both actin- and 4.1R-binding sites. Thus, phosphorylation weakens the affinity of 4.1R for β-spectrin. The two 4.1R phosphorylation sites lie in a domain flanked in the sequence by the spectrin- and actin-binding domain and a domain containing the binding sites for transmembrane proteins. It thus appears that phosphorylation of a regulatory domain in 4.1R results in structural changes transmitted to the functional interaction centers of the protein. We consider possible implications of our findings for the altered membrane function of normal reticulocytes and sickle red cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.