Claudia Litterst

An LXXLL motif in the transactivation domain of STAT6 mediates recruitment of NCoA-1/SRC-1.

NCoA-1/SRC-1 is an essential coactivator of STAT5 that binds to the FDL motif in the alpha-helical region of the STAT5 transactivation domain.

Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain.

Coactivators in gene regulation by STAT5.

Cadherins mediate both the association between PS1 and beta-catenin and the effects of PS1 on beta-catenin stability.

Metalloproteinase/Presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling.

FAD mutants unable to increase neurotoxic Abeta 42 suggest that mutation effects on neurodegeneration may be independent of effects on Abeta.

Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor.

Peptide EphB2/CTF2 generated by the gamma-secretase processing of EphB2 receptor promotes tyrosine phosphorylation and cell surface localization of N-methyl-D-aspartate receptors.

Interaction of STAT6 with its co-activator SRC-1/NCoA-1 is regulated by dephosphorylation of the latter via PP2A.