Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses

Article Abstract:

Testing of whether or not endogenous endothelial and P19 cell EphB1 (ELK) and EphB2 (Nuk) receptors tell the difference between different oligomeric forms of an ephrin-B1/Fc fusion ligand has been carried out. Cell-cell contact for cells expressing both EphB1 and ephrin-B was necessary for EphB1 activation and recruiting low molecular weight phosphotyrosine phosphatase (LMW-PTP) to EphB1 complexes. The EphB1-binding site for LMW-PTP is necessary for tetrameric ephrin-B1 to recruit LMW-PTP and to promote attachment. Distinct EphB1-signaling complexes are put together with different cellular attachment responses regulated by a receptor-switch system that responds to given ephrin-B1 oligomers.

Analysis, Proteins, Protein tyrosine kinase, Protein-tyrosine kinase, Cell receptors, Genetic translation, Translation (Genetics)

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Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain

Article Abstract:

Signaling by proinflammatory cytokines has been investigated and it can be seen that oligomerization of TRAF2 and TRAF6 is adequate for IKK and JNK activation and target gene induction via an amino-terminal effector domain. Tumor necrosis factor (TNF-alpha) and interleukin-1 (IL-1) bring on transcription factors NF-kappaB and AP-1 through activation of the MAP kinases the IkappaB kinase (IKK) and JNK and p38 and respectively. Replacing the carboxy-terminal TRAF domain of TRAF6 and TRAF2 with immunopyhilin FKBP12 repeats showed that the effector domains are made up of the amino-terminal RING and Zn fingers.

United States, Physiological aspects, Inflammation, Protein kinases, Cytokines, Genetic research

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LIN-12/Notch signaling: lessons from worms and flies

Article Abstract:

Lessons about LIN-12/Notch signaling can be derived from the study of invertebrates such as Caenorhabditis elegans and Drosophila melanogaster. The LIN-12/Notch proteins act as receptors for signals between cells in development. LIN-12/Notch signal transduction has been elucidated through new in vivo evidence that seems to indicate direct participation of the intracellular domain of the proteins in regulating target gene expression. Protein turnover and processing are additional influences on Lin-12/Notch activity.

Drosophila, Caenorhabditis elegans, Cell interaction, Cell interactions, Invertebrates

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