Genomes and Genes
Gene Symbol: EPB42
Description: erythrocyte membrane protein band 4.2
Alias: SPH5, erythrocyte membrane protein band 4.2, P4.2, erythrocyte protein 4.2, erythrocyte surface protein band 4.2
- Hayette S, Dhermy D, dos Santos M, Bozon M, Drenckhahn D, Alloisio N, et al. A deletional frameshift mutation in protein 4.2 gene (allele 4.2 Lisboa) associated with hereditary hemolytic anemia. Blood. 1995;85:250-6 pubmed..Antibodies to red cell protein 4.2 showed a doublet (72 and 70 kD) both in the controls and the patient. This finding raises an interesting question concerning the relationship between this doublet and erythroid protein 4.2. ..
- Hayette S, Morle L, Bozon M, Ghanem A, Risinger M, Korsgren C, et al. A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia. Br J Haematol. 1995;89:762-70 pubmed..We infer that the nearly total absence of protein 4.2 in the patients results from imbalance between destruction and synthesis of mutated protein 4.2 prior to its binding to the membrane. ..
- Najfeld V, Ballard S, Menninger J, Ward D, Bouhassira E, Schwartz R, et al. The gene for human erythrocyte protein 4.2 maps to chromosome 15q15. Am J Hum Genet. 1992;50:71-5 pubmed..Our results demonstrate that the locus of the P4.2 gene is located within 15q15. ..
- Korsgren C, Cohen C. Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII. Proc Natl Acad Sci U S A. 1991;88:4840-4 pubmed..These and other similarities suggest that the gene for band 4.2 is closely related to and possibly derived from that for the a subunit of factor XIII and that the proteins may share common structural and functional properties. ..
- Korsgren C, Lawler J, Lambert S, Speicher D, Cohen C. Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2. Proc Natl Acad Sci U S A. 1990;87:613-7 pubmed..Consistent with this active site substitution, erythrocyte membranes or inside-out vesicles, which contain band 4.2, show no evidence of transglutaminase activity by two types of in vitro assay. ..
- Azim A, Marfatia S, Korsgren C, Dotimas E, Cohen C, Chishti A. Human erythrocyte dematin and protein 4.2 (pallidin) are ATP binding proteins. Biochemistry. 1996;35:3001-6 pubmed..2. Although the functional significance of ATP binding is not yet clear, our findings open new perspectives for the function of dematin and protein 4.2 in vivo. ..
- Bhattacharyya R, Das A, Moitra P, Pal B, Mandal I, Basu J. Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2. Biochem J. 1999;340 ( Pt 2):505-12 pubmed..2-CDB3 interaction. This is also the first demonstration that palmitoylation serves as a positive modulator of this interaction. ..
- Bruce L, Ghosh S, King M, Layton D, Mawby W, Stewart G, et al. Absence of CD47 in protein 4.2-deficient hereditary spherocytosis in man: an interaction between the Rh complex and the band 3 complex. Blood. 2002;100:1878-85 pubmed..2 gene (EPB42). The proband's mother was found to be heterozygous for this substitution. Unlike protein 4...
- Low P, Willardson B, Mohandas N, Rossi M, Shohet S. Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability. Blood. 1991;77:1581-6 pubmed
- Cui Y, Wang J, Zhang X, Lang R, Bi M, Guo L, et al. ECRG2, a novel candidate of tumor suppressor gene in the esophageal carcinoma, interacts directly with metallothionein 2A and links to apoptosis. Biochem Biophys Res Commun. 2003;302:904-15 pubmed..ECRG2 might reduce the function of MT2A on the regulation of cell proliferation and induction of apoptosis. The physical interaction of ECRG2 and MT2A may play an important role in the carcinogenesis of esophageal cancer. ..
- Ciciotte S, Gwynn B, Moriyama K, Huizing M, Gahl W, Bonifacino J, et al. Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel protein that is part of the pallidin-muted complex (BLOC-1). Blood. 2003;101:4402-7 pubmed
- Sung L, Chien S, Fan Y, Lin C, Lambert K, Zhu L, et al. Human erythrocyte protein 4.2: isoform expression, differential splicing, and chromosomal assignment. Blood. 1992;79:2763-70 pubmed..4-kilobase (kb) cDNA to human metaphase chromosomes, the gene for P4.2 was mapped to bands q15-q21 of chromosome 15, and it is not linked to the gene for coagulation factor XIIIa (plasma transglutaminase, TGase). ..
- Risinger M, Dotimas E, Cohen C. Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated. J Biol Chem. 1992;267:5680-5 pubmed..Study of myristylation of band 4.2, an abundant normal cellular protein, and its role in membrane binding may produce insights relevant to other myristylated cellular proteins. ..
- Su Y, Ding Y, Jiang M, Jiang W, Hu X, Zhang Z. Associations of protein 4.2 with band 3 and ankyrin. Mol Cell Biochem. 2006;289:159-66 pubmed..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. ..
- Dgany O, Avidan N, Delaunay J, Krasnov T, Shalmon L, Shalev H, et al. Congenital dyserythropoietic anemia type I is caused by mutations in codanin-1. Am J Hum Genet. 2002;71:1467-74 pubmed..The specific mechanisms by which codanin-1 underlies normal erythropoiesis remain to be elucidated. ..
- Mandal D, Moitra P, Basu J. Mapping of a spectrin-binding domain of human erythrocyte membrane protein 4.2. Biochem J. 2002;364:841-7 pubmed..2 confirmed that these residues are crucial in mediating protein 4.2-spectrin interactions. ..
- Mouro Chanteloup I, Delaunay J, Gane P, Nicolas V, Johansen M, Brown E, et al. Evidence that the red cell skeleton protein 4.2 interacts with the Rh membrane complex member CD47. Blood. 2003;101:338-44 pubmed..2(-) and Rh(null) red cells. ..
- Huang L, Kuo Y, Gitschier J. The pallid gene encodes a novel, syntaxin 13-interacting protein involved in platelet storage pool deficiency. Nat Genet. 1999;23:329-32 pubmed..Whereas the mocha and pearl SPD mutants have defects in Ap-3, our findings suggest that pa SPD mutants are defective in a more downstream event of vesicle-trafficking: namely, vesicle-docking and fusion. ..
- Tanimoto T, Hoshijima M, Kawata M, Yamamoto K, Ohmori T, Shiku H, et al. Binding of ras p21 to bands 4.2 and 6 of human erythrocyte membranes. FEBS Lett. 1988;226:291-6 pubmed..2 or 6 protein. These results indicate that v-Ki-ras p21 can bind directly to bands 4.2 and 6 of human erythrocyte membranes as far as tested in an in vitro cell-free system. ..
- Sung L, Chien S, Chang L, Lambert K, Bliss S, Bouhassira E, et al. Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane. Proc Natl Acad Sci U S A. 1990;87:955-9 pubmed..Sequence alignment of P4.2 with these two transglutaminases, however, revealed that P4.2 lacks the critical cysteine residue required for the enzymatic crosslinking of substrates. ..
- Bustos S, Reithmeier R. Protein 4.2 interaction with hereditary spherocytosis mutants of the cytoplasmic domain of human anion exchanger 1. Biochem J. 2011;433:313-22 pubmed publisher..2 was associated with the cytoskeleton of HEK-293 cells. The present study shows that cytoplasmic HS mutants cause impaired binding of protein 4.2 to AE1, leaving protein 4.2 susceptible to loss during erythrocyte development. ..
- Satchwell T, Shoemark D, Sessions R, Toye A. Protein 4.2: a complex linker. Blood Cells Mol Dis. 2009;42:201-10 pubmed publisher..2 that may represent the active, membrane associated protein 4.2 molecule in red blood cells and also explain the dependence of protein 4.2 on band 3 binding for stability...
- Cui Y, Wang J, Zhang X, Bi M, Guo L, Lu S. Using yeast two-hybrid system to identify ECRG2 associated proteins and their possible interactions with ECRG2 gene. World J Gastroenterol. 2003;9:1892-6 pubmed..A further understanding of the association between ECRG2 and MT should facilitate the functions of ECRG2 gene. ..
- Dahl K, Parthasarathy R, Westhoff C, Layton D, Discher D. Protein 4.2 is critical to CD47-membrane skeleton attachment in human red cells. Blood. 2004;103:1131-6 pubmed..2 strongly influences CD47 levels as well as the extent of membrane skeleton attachment in the RBC, whereas protein 4.2 affects membrane skeletal attachment of RhAG, Rh, and band 3 to a lesser extent. ..
- Das A, Bhattacharya R, Kundu M, Chakrabarti P, Basu J. Human erythrocyte membrane protein 4.2 is palmitoylated. Eur J Biochem. 1994;224:575-80 pubmed..Protein 4.2 could be depalmitoylated with hydroxylamine, suggesting a thioester linkage. Depalmitoylated protein 4.2 showed significantly decreased binding to protein-4.2-depleted membranes, compared to native protein 4.2. ..
- White R, Peters L, Adkison L, Korsgren C, Cohen C, Lux S. The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene. Nat Genet. 1992;2:80-3 pubmed..This is the first gene defect to be associated with a platelet storage pool deficiency, and may allow the identification of a novel structure or biological pathway that influences granulogenesis. ..
- Bouhassira E, Schwartz R, Yawata Y, Ata K, Kanzaki A, Qiu J, et al. An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2NIPPON). Blood. 1992;79:1846-54 pubmed..2-deficiency is related to the pathogenesis of the hemolytic anemia in this variant form of recessively inherited spherocytosis. ..
- Dotimas E, Speicher D, GuptaRoy B, Cohen C. Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2). Biochim Biophys Acta. 1993;1148:19-29 pubmed..Our results show that endogenous pallidin on the red-cell membrane is a poor substrate for the kinase, possibly because it is fully phosphorylated, or inaccessible to the kinase. ..
- Takaoka Y, Ideguchi H, Matsuda M, Sakamoto N, Takeuchi T, Fukumaki Y. A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka). Br J Haematol. 1994;88:527-33 pubmed..2 defect. ..
- Korsgren C, Cohen C. Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3. J Biol Chem. 1988;263:10212-8 pubmed..2 with band 4.1. Our results show that band 4.2 can form multiple associations with red cell membrane proteins and may therefore play an as yet unrecognized structural role on the membrane. ..
- Rybicki A, Musto S, Schwartz R. Identification of a band-3 binding site near the N-terminus of erythrocyte membrane protein 4.2. Biochem J. 1995;309 ( Pt 2):677-81 pubmed..2 tryptic peptides lacking this site. The V63RRGQPFTIILYF site is highly conserved in mouse and human erythrocyte P4.2 as well as between P4.2 and transglutaminase proteins, which are evolutionarily related to P4.2. ..