High impact information on Ephb1

• The study of Net should help in understanding the interplay between Net and other members of the Elk subfamily and their contribution to signal transduction through Ras to the nucleus [1].
• Ezrin function is required for ROCK-mediated fibroblast transformation by the Net and Dbl oncogenes [2].
• These results provide insights into the cross-talk between pathways that inhibit and stimulate transformation at the level of Net, a regulator of gene expression [3].
• Tumor-associated mutant p53s are less efficient inhibitors. p53 inhibits by preventing phosphorylation of Net by MAP kinases [4].
• Our results show that p53 can repress specific gene expression by inhibiting Net, a factor implicated in cell cycle entry [4].

Biological context of Ephb1

• The Elk cytoplasmic domain is therefore able to induce tyrosine phosphorylation and DNA synthesis in response to an extracellular ligand, suggesting that Elk and related polypeptides function as ligand-dependent receptor tyrosine kinases [5].
• We report that wild-type p53 inhibits an effector of the Ras oncogene/mitogen-activated protein (MAP) kinase pathway, the transcription factor Net [4].
• Loss of p53 in vivo leads to increased Net phosphorylation in response to wound healing and UV irradiation of skin [4].
• Therefore, Stat3betatc was coexpressed with the catalytic domain of the Elk receptor tyrosine kinase [6].
• Mouse Elk oncogene maps to chromosome X and a novel Elk oncogene (Elk3) maps to chromosome 10 [7].

Anatomical context of Ephb1

• EGF stimulation also induced DNA synthesis in fibroblasts stably expressing the EGF-Elk receptors [5].
• These non-genomic effects of estradiol produce biologic effects as evidenced by Elk activation and by morphologic changes in cell membranes [8].
• In order to assess whether this decreased zona-binding ability is due to perturbations in the mechanical properties of the sperm membranes, we attempted to examine the molecular dynamics employing a lipophilic spin label (16-doxyl stearate) and a protein-binding label (Mal-Net) in two sets of independent experiments [9].
• The differentiation of T lymphocytes. IV. Net increases in low theta cells, maintenance of biological activity and death of high theta cells during short-term culture of mouse thymocytes [10].

Associations of Ephb1 with chemical compounds

• Biological and biochemical activities of a chimeric epidermal growth factor-Elk receptor tyrosine kinase [5].
• Both CSF-1 and LPS rapidly activate the MAPK network and induce the phosphorylation of two distinct ternary complex factors (TCFs), TCF/Elk and TCF/SAP [11].
• Consistent with these results, we found that apigenin induced a 7.4-fold induction in the phosphorylation of Elk, the downstream phosphorylation target of ERK kinase [12].
• In addition, merlin inhibited serum-induced Elk phosphorylation, a downstream effector of ERKs [13].
• The ATP-dependent and ATP-independent processes of DNA synthesis are inhibited to the same extent by Mal-Net, pHMB, ara CTP and phosphonoacetate [14].

Other interactions of Ephb1

• Based on binding characteristics, receptor autophosphorylation, and cellular transformation assays, we find that the transmembrane-type ligands Lerk2 and Elf2 have common and specific receptors within the Elk subclass of receptors [15].
• Similarities and differences in the way transmembrane-type ligands interact with the Elk subclass of Eph receptors [15].
• All the GPI-anchored ligands bind and activate one subclass of the Eph receptors (that represented by Eck) while the two transmembrane ligands bind and activate the other major subclass of receptors (represented by Elk) [16].

References