Search

Your search keyword '"Ni, C. Y."' showing total 3 results
Start Over Author "Ni, C. Y." Search Limiters Full Text
3 results on '"Ni, C. Y."'

2. gamma -Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase.

Author

Ni CY, Murphy MP, Golde TE, and Carpenter G

Subjects
Active Transport, Cell Nucleus, Amino Acid Sequence, Amyloid Precursor Protein Secretases, Animals, Aspartic Acid Endopeptidases, COS Cells, Carbamates pharmacology, Cell Division drug effects, Cell Line, Cell Membrane metabolism, Cytoplasm metabolism, Dipeptides pharmacology, ErbB Receptors chemistry, Fatty Acids, Unsaturated pharmacology, Humans, Membrane Proteins genetics, Membrane Proteins metabolism, Metalloendopeptidases metabolism, Mice, Molecular Sequence Data, Mutation, Neuregulin-1 pharmacology, Presenilin-1, Protease Inhibitors pharmacology, Protein Structure, Tertiary, Receptor, ErbB-4, Recombinant Fusion Proteins metabolism, Signal Transduction, Tetradecanoylphorbol Acetate pharmacology, Transcriptional Activation, Tumor Cells, Cultured, Cell Nucleus metabolism, Endopeptidases metabolism, ErbB Receptors metabolism
Abstract

ErbB-4 is a transmembrane receptor tyrosine kinase that regulates cell proliferation and differentiation. After binding of its ligand heregulin (HRG) or activation of protein kinase C (PKC) by 12-O-tetradecanoylphorbol-13-acetate (TPA), the ErbB-4 ectodomain is cleaved by a metalloprotease. We now report a subsequent cleavage by gamma-secretase that releases the ErbB-4 intracellular domain from the membrane and facilitates its translocation to the nucleus. gamma-Secretase cleavage was prevented by chemical inhibitors or a dominant negative presenilin. Inhibition of gamma-secretase also prevented growth inhibition by HRG. gamma-Secretase cleavage of ErbB-4 may represent another mechanism for receptor tyrosine kinase-mediated signaling.

Published
2001
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results