Expression and characterization of the PEBP homolog genes from Drosophila

Abstract

The phosphatidylethanolamine binding proteins (PEBPs) family is evolutionarily conserved and involved in different physiological phenomena. PEBPs were found in many species from bacteria to mammals. Despite numerous studies, PEBPs' biological function and mode of action remain elusive. Based on sequence homology, seven PEBP genes were detected in the Drosophila genome. Only one of them, the odorant binding protein (OBP), has been characterized. To date nothing is known concerning the expression pattern and biological roles of the six other PEBP genes. By RT-PCR and Western blot analysis, we examined expression of the PEBPs in different tissues and embryos. The 6 PEBPs were differentially expressed. Only one, CG10298, is specific of only one tissue: the testis. Additionally, by comparing in wild type and male-sterile mutants we show that CG10298 is present only during spermatid differentiation. Furthermore, by comparing structural parameters of the six PEBP proteins with those of human PEBP-1, we have established that PEBP CG10298 is most closely related to human PEBP.

RKIP: Much more than Raf Kinase inhibitory protein

“…In nematodes, PEBP is one of the membranous secreted proteins conferring a protective role against the host immunological responses (Morgan et al, 2006). Drosophila PEBP homologs, of which at least seven isoforms are known, are expressed in olfactory cells (Rautureau et al, 2009). Interestingly, PEBP1 overexpression has been shown to protect Drosophila against bacterial infection by enhancing the release of immunity‐related proteins in their hemolymph (Reumer et al, 2009), and in plants, RKIP was found to be associated with growth and differentiation, transforming plants from the vegetative to reproductive growth phases (Banfield and Brady, 2000).…”

Knockdown of PEBP4 inhibits human glioma cell growth and invasive potential via ERK1/2 signaling pathway

“…To examine the molecular mechanism underlying the effects of PEBP4 knockdown on glioma cell behaviors and the expression of related genes, we examined the relationship between PEBP4 downregulation and ERK1/2 signaling in the RAF1‐MEK‐ERK pathway, which is negatively modulated by the PEBP family . As shown in Figure A, knockdown of PEBP4 significantly increased the levels of phosphorylated ERK1/2 (p‐ERK1/2), suggesting that PEBP4 is an upstream modulator of ERK1/2 signaling.…”

“…One member of the PEBP family is RAF kinase inhibitory protein (RKIP)/PEBP1, which binds to RAF1 through the PE‐binding motif and inhibits the RAF1‐catalyzed phosphorylation/activation of mitogen‐activated protein kinase kinase (MEK/MAPKK) as well as the downstream extracellular signal‐regulated kinases (ERK), thus suppressing the RAF1‐MEK‐ERK signaling pathway . The members of the PEBP family participate in a number of biological processes, including lipid binding, hippocampus development, and inhibition of serine proteases and RAF1 kinase …”

Actomyosin contraction during cellularization is regulated in part by Src64 control of Actin 5C protein levels

“…It shifted position, suggesting that Src64 activity leads to the posttranslational modification of CG7054 (Tables 1 and 2). CG7054 encodes a phosphatidylethanolamine-binding protein (PEBP) homologous to human PEBP-1/Raf kinase inhibitor protein (RKIP), a protein that modulates mitogenactivated protein kinase (MAPK) and nuclear factor kappa-light-chainenhancer of B cells (NF-κB) signaling pathways (Attrill et al, 2016; E. T. Keller, 2004;Rautureau et al, 2009;K. Yeung et al, 1999; K. C. Yeung et al, 2001).…”