From structure to function: possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site

Schoentgen, Françoise; Jollès, Pierre

doi:10.1016/0014-5793(95)00376-k

Cited by 87 publications

(64 citation statements)

References 31 publications

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“…This protein is homologous to the mammalian phosphatidylethanolamine-binding protein (PEBP). PEBP is expressed in a wide range of tissues but was originally isolated as a cytosolic 21-to 23-kDa protein from bovine brain and binds hydrophobic ligands, in particular phosphatidylethanolamine (26). Putative PEBP homologues have been identified in a variety of organisms, including Drosophila, C. elegans, and Saccharomyces cerevisiae; the parasites Plasmodium, Onchocerca volvulus, and Toxocara canis; and the flowering plants Arabidopsis and Antirrhinum (27).…”

Section: Resultsmentioning

confidence: 99%

A proteomic approach for the analysis of instantly released wound and immune proteins in Drosophila melanogaster hemolymph

Vierstraete

Verleyen

Baggerman

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

138

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Insects respond to microbial infection by the rapid and transient expression of several genes encoding antibacterial peptides. In this paper we describe a powerful technique, two-dimensional difference gel electrophoresis, that, when combined with mass spectrometry, can be used to study the immune response of Drosophila melanogaster at the protein level. By comparatively analyzing the hemolymph proteome of 2,000 third-instar Drosophila larvae, we identified 10 differential proteins that appear in the fruit fly hemolymph very early after an immune-challenge with lipopolysaccharides. These proteins can be assigned to the immune response, because they are not induced after sterile injury. Reduction of intergel variability or quantification problems related to conventional two-dimensional electrophoresis and improvement of image analysis were achieved by the use of two fluorescent dyes to label the two different protein samples. Some of the immune-induced proteins, such as thioestercontaining protein 2, can be assigned to specific aspects of the immune response; others were already reported as being involved in stress response. An immune-induced protein (CG18594) is homologous to a mammalian serine protease inhibitor that mediates the mitogen-activated protein kinase and the NF-B signaling pathways. In addition, a number of proteins that had not been associated with the immune response before were isolated and identified, and some of these were still present in the hemolymph 4 h after injury. Determining the function of all of these immune-induced proteins represents an exciting challenge for increasing our knowledge of insect immunity.immune response proteins ͉ two-dimensional difference gel electrophoresis ͉ stress response ͉ secretome ͉ innate immunity

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Section: Resultsmentioning

confidence: 99%

A proteomic approach for the analysis of instantly released wound and immune proteins in Drosophila melanogaster hemolymph

Vierstraete

Verleyen

Baggerman

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

138

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“…Mammalian RKIP/PEBP is distinct from other known proteins and its function is still being elucidated. In addition to binding phospholipids, RKIP has been reported to bind nucleotides and opioids [3]. However, our recent NMR studies have shown that most of these ligands do not bind to RKIP in solution at neutral pH (data not shown).…”

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confidence: 90%

Raf kinase inhibitory protein: a signal transduction modulator and metastasis suppressor

2008

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Cells have a multitude of controls to maintain their integrity and prevent random switching from one biological state to another. Raf Kinase Inhibitory Protein (RKIP), a member of the phosphatidylethanolamine binding protein (PEBP) family, is representative of a new class of modulators of signaling cascades that function to maintain the "yin yang" or balance of biological systems. RKIP inhibits MAP kinase (Raf-MEK-ERK), G protein-coupled receptor (GPCR) kinase and NFκB signaling cascades. Because RKIP targets different kinases dependent upon its state of phosphorylation, RKIP also acts to integrate crosstalk initiated by multiple environmental stimuli. Loss or depletion of RKIP results in disruption of the normal cellular stasis and can lead to chromosomal abnormalities and disease states such as cancer. Since RKIP and the PEBP family have been reviewed previously, the goal of this analysis is to provide an update and highlight some of the unique features of RKIP that make it a critical player in the regulation of cellular signaling processes.

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“…Despite its widespread expression, little is known about the role of this protein family. Various functions have been suggested for these molecules, such as binding of lipids (48), inhibition of serine proteases (49), or acting as Drosophila OBPs (50). It has been shown that a rat PEBP, Raf-1 kinase inhibitor protein (RKIP), acts as a negative regulator of the mitogen-activated protein kinase cascade, which controls mitogenesis and cell differentiation (51).…”

Section: Molecules With Putative Roles In Immune Responsementioning

confidence: 99%

Proteomic Analysis of the Systemic Immune Response of Drosophila

Lévy

Bulet

Ehret‐Sabatier

2004

Molecular & Cellular Proteomics

134

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From structure to function: possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site

Cited by 87 publications

References 31 publications

A proteomic approach for the analysis of instantly released wound and immune proteins in Drosophila melanogaster hemolymph

A proteomic approach for the analysis of instantly released wound and immune proteins in Drosophila melanogaster hemolymph

Raf kinase inhibitory protein: a signal transduction modulator and metastasis suppressor

Proteomic Analysis of the Systemic Immune Response of Drosophila

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