ArticleMolecular and cellular biochemistry2006
Associations of protein 4.2 with band 3 and ankyrin.
Article in Molecular and cellular biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Redox Homeostasis in Red Blood Cells: From Molecular Mechanisms to Antioxidant Strategies.Current issues in molecular biology · 2025Review
- Architecture of the human erythrocyte ankyrin-1 complex.Nature structural & molecular biology · 2022Article
- A novel ENU-induced ankyrin-1 mutation impairs parasite invasion and increases erythrocyte clearance during malaria infection in mice.Scientific reports · 2016Article
- Identification of the components of a glycolytic enzyme metabolon on the human red blood cell membrane.The Journal of biological chemistry · 2013Article
- Identification of contact sites between ankyrin and band 3 in the human erythrocyte membrane.Biochemistry · 2012Article
- Refined views of multi-protein complexes in the erythrocyte membrane.Blood cells, molecules & diseases · 2012Review
- Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor.The Journal of biological chemistry · 2011Article
- 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
- Malaria parasite proteins that remodel the host erythrocyte.Nature reviews. Microbiology · 2009Review
- Interactions of recombinant mouse erythrocyte transglutaminase with membrane skeletal proteins.The Journal of membrane biology · 2007Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-protein and protein-lipid interactions are thought to play the vital role in maintenance and deformation of red blood cell (RBC) membrane. Protein 4.2, a 76-KDa peripheral protein, binds to the cytoplasmic domain of band 3 (CDB3) and also interacts with ankyrin in RBCs. In order to explore the characteristics of protein 4.2-CDB3-ankyrin interactions, three protein 4.2-derived recombinant proteins encompassing amino acid residues 31-200, 1-300, and 187-260 respectively were expressed in Escherichia coli. Their interactions with CDB3 and ankyrin were investigated by using Far-Western blot and pull-down assay. The results showed that the CDB3-binding site of protein 4.2 is located in the region of residues 200-211 and the ankyrin-binding site is located in the region of residues 187-200 of protein 4.2. Our findings also suggested that the ankyrin D34 domain can interact directly with protein 4.2. The proper tertiary structures of these protein 4.2 fragments are essential for protein 4.2-ankyrin interaction. Meanwhile, ankyrin can enhance the interaction between protein 4.2 and CDB3.
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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.