Molecular identification of a major palmitoylated erythrocyte membrane protein containing the src homology 3 motif.

Ruff, Paul; Speicher, David W.; Husain-Chishti, A.

doi:10.1073/pnas.88.15.6595

Cited by 141 publications

(79 citation statements)

References 35 publications

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“…Erythrocyte membrane protein-p55 (MPP1) is a 55-kDa palmitoylated erythrocyte membrane protein that is constitutively and abundantly expressed in erythroid cells during their development from stem cells to fully differentiated reticulocytes (22). It is an integral membrane protein with guanylate kinase activity, allowing it to interact with the cytoskeleton and regulate cell proliferation and signal transduction.…”

Section: Gene Profiling Of Anemia In Renal Transplantationmentioning

confidence: 99%

Molecular Profiling of Anemia in Acute Renal Allograft Rejection Using DNA Microarrays

Chua

Barry

Salvatierra

et al. 2003

American Journal of Transplantation

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Compromised renal function after renal allograft transplantation often results in anemia in the recipient. Molecular mechanisms leading to anemia during acute rejection are not fully understood; inadequate erythropoietin production and iron deficiency have been reported to be the main contributors. To increase our understanding of the molecular events underlying anemia in acute rejection, we analyzed the gene expression profiles of peripheral blood lymphocytes (PBL) from four pediatric renal allograft recipients with acute rejection and concurrent anemia, using DNA microarrays containing 9000 human cDNA clones (representing 7469 unique genes). In these anemic rejecting patients, an 'erythropoiesis cluster' of 11 down-regulated genes was identified, involved in hemoglobin transcription and synthesis, iron and folate binding and transport. Additionally, some alloimmune response genes were simultaneously down-regulated. An independent data set of 36 PBL samples, some with acute rejection and some with concurrence of acute rejection and anemia, were analyzed to support a possible association between acute rejection and anemia. In conclusion, analysis using DNA microarrays has identified a cluster of genes related to hemoglobin synthesis and/or erythropoeisis that was altered in kidneys with renal allograft rejection compared with normal kidneys. The possible relationship between alterations in the expression of this cluster, reduced renal function, the alloimmune process itself, and other influences on the renal transplant awaits further analysis.Key words: Anemia, gene expression, microarrays, rejection, renal transplantation Abbreviations: ALAS, delta-aminolevulinate synthase-2; CA1, carbonic anhydrase I; EPO, erythropoietin; MPP1, membrane protein, palmitoylated 1 55 kDa; NF-E2, nuclear factor (erythroid-derived 2); PBL, peripheral blood lymphocytes; rHuEPO, recombinant human EPO; TGF-b, transforming growth factor-beta

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Section: Gene Profiling Of Anemia In Renal Transplantationmentioning

confidence: 99%

Molecular Profiling of Anemia in Acute Renal Allograft Rejection Using DNA Microarrays

Chua

Barry

Salvatierra

et al. 2003

American Journal of Transplantation

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“…PSD-95 is a major component of postsynaptic densities, which are junctions involved in the reception and transduction of synaptic stimuli (Cho et al 1992). A more divergent homolog of these genes is erythrocyte membrane protein p55, which is also peripherally associated with the plasma membrane (Ruff et al 1991;Bryant and Woods 1992). The conserved sequence homologous to Dsh in these genes, termed the "undefined domain" by Bryant and Woods (1992), occurs in three repeats in the amino-terminal half of Dlg and relatives.…”

Section: Dsh Represents a Novel Signal Transduction Moleculementioning

confidence: 99%

The Drosophila segment polarity gene dishevelled encodes a novel protein required for response to the wingless signal.

Klingensmith

Nusse²,

Perrimon³

1994

Genes Dev.

371

209

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“…p55 is a heavily palmitoylated peripheral membrane protein of the red blood cell membrane (1). The primary structure of p55 defines several distinct domains including the PDZ domain, the SH3 domain, the protein 4.1 binding domain, the tyrosine phosphorylation domain, and a carboxyl-terminal guanylate kinase-like domain (2).…”

mentioning

confidence: 99%

The PDZ Domain of Human Erythrocyte p55 Mediates Its Binding to the Cytoplasmic Carboxyl Terminus of Glycophorin C

Marfatia

Morais-Cabral²,

Kim

et al. 1997

Journal of Biological Chemistry

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The PDZ domain, also known as the GLGF repeat/DHR domain, is an ϳ90-amino acid motif discovered in a recently identified family of proteins termed MAGUKs (membrane-associated guanylate kinase homologues). Sequence comparison analysis has since identified PDZ domains in over 50 proteins. Like SH2 and SH3 domains, the PDZ domains mediate specific protein-protein interactions, whose specificities appear to be dictated by the primary structure of the PDZ domain as well as its binding target. Using recombinant fusion proteins and a blot overlay assay, we show that a single copy of the PDZ domain in human erythrocyte p55 binds to the carboxyl terminus of the cytoplasmic domain of human erythroid glycophorin C. Deletion mutagenesis of 21 amino acids at the amino terminus of the p55 PDZ domain completely abrogates its binding activity for glycophorin C. Using an alanine scan and surface plasmon resonance technique, we identify residues in the cytoplasmic domain of glycophorin C that are critical for its interaction with the PDZ domain. The recognition specificity of the p55 PDZ domain appears to be unique, since the three PDZ domains of hDlg (human lymphocyte homologue of the Drosophila discs large tumor suppressor) do not bind the cytoplasmic domain of glycophorin C. Taken together with our previous studies, these results complete the identification of interacting domains in the ternary complex between p55, glycophorin C, and protein 4.1. Implications of these findings are discussed in terms of binding specificity and the regulation of cytoskeleton-membrane interactions.p55 is a heavily palmitoylated peripheral membrane protein of the red blood cell membrane (1). The primary structure of p55 defines several distinct domains including the PDZ domain, the SH3 domain, the protein 4.1 binding domain, the tyrosine phosphorylation domain, and a carboxyl-terminal guanylate kinase-like domain (2). The domain organization of p55 is similar to a family of proteins termed MAGUKs 1 (membraneassociated guanylate kinase homologues), which appear to play important roles in the regulation of signaling pathways and cytoskeleton-membrane interactions (3-6). Among various protein domains of MAGUKs, the PDZ domain has been a focus of intense scrutiny (5-8). Like the SH2 and SH3 domains, the PDZ domains recruit cytoplasmic proteins to specific submembranous sites. For example, the PDZ 1 ϩ 2 domain, but not the PDZ 3 domain, of PSD-95 and hDlg interacts with the carboxyl terminus of the NMDA receptors and the Shaker type K ϩ channels, and this interaction plays an important role in the clustering of ion channels (5, 6). The PDZ domains have also been shown to interact with other PDZ domains. The PDZ domain of neuronal nitric-oxide synthase binds to the PDZ domain of syntrophin at the sarcolemma in skeletal muscle and to the PDZ 2 domain of PSD-95 at the synaptic junctions of neuronal cells (9, 10). These observations suggest that the primary structures of both the PDZ domain and its target peptide govern the specificity as well as the affin...

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Molecular identification of a major palmitoylated erythrocyte membrane protein containing the src homology 3 motif.

Cited by 141 publications

References 35 publications

Molecular Profiling of Anemia in Acute Renal Allograft Rejection Using DNA Microarrays

Molecular Profiling of Anemia in Acute Renal Allograft Rejection Using DNA Microarrays

The Drosophila segment polarity gene dishevelled encodes a novel protein required for response to the wingless signal.

The PDZ Domain of Human Erythrocyte p55 Mediates Its Binding to the Cytoplasmic Carboxyl Terminus of Glycophorin C

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