Phospho-specific recognition by 14-3-3 proteins and antibodies monitored by a high throughput label-free optical biosensor.

Label-free detection of molecular interactions has considerable potential in facilitating assay development. When combined with high throughput capability, it may be applied to small molecule screens for drug candidates. Phosphorylation is a key posttranslational process that confers diverse regulation in biological systems involving specific protein-protein interactions recognizing the phosphorylated motifs.

C-terminal recognition by 14-3-3 proteins for surface expression of membrane receptors.

Diverse functions of 14-3-3 proteins are directly coupled to their ability to interact with targeted peptide substrates. RSX(pS/pT)XP and RXPhiX(pS/pT)XP are two canonical consensus binding motifs for 14-3-3 proteins representing the two common binding modes, modes I and II, between 14-3-3 and internal peptides. Using a genetic selection, we have screened a random peptide library and identified a group of C-terminal motifs, termed SWTY, capable of overriding an endoplasmic reticulum localization signal and redirecting membrane proteins to cell surface.

NF-kappaB p50 facilitates neutrophil accumulation during LPS-induced pulmonary inflammation.

Background: Transcription factors have distinct functions in regulating immune responses. During Escherichia coli pneumonia, deficiency of NF-kappaB p50 increases gene expression and neutrophil recruitment, suggesting that p50 normally limits these innate immune responses. p50-deficient mice were used to determine how p50 regulates responses to a simpler, non-viable bacterial stimulus in the lungs, E.

Exon truncation by alternative splicing of murine ICAM-1.

The murine gene for intercellular adhesion molecule-1 (ICAM-1) encodes multiple products, arising from alternative splicing. Full-length ICAM-1 contains five extracellular Ig domains, each encoded by a separate exon. Alternatively spliced forms have Ig domains 2, 3, and/or 4 excised as a result of exon skipping.

Functions of IkappaB proteins in inflammatory responses to Escherichia coli LPS in mouse lungs.

Acute inflammation induced by intrapulmonary LPS requires nuclear factor (NF)-kappaB RelA. This study elucidates the effects of intrapulmonary LPS on IkappaB proteins, endogenous inhibitors of RelA, and the effects of deficiency of IkappaB-beta. IkappaB-alpha, IkappaB-beta, and IkappaB-epsilon each complexed with RelA in uninfected murine lungs.