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Brain armadillo protein δ‐catenin interacts with Abl tyrosine kinase and modulates cellular morphogenesis in response to growth factors
Author(s) -
Lu Q.,
Mukhopadhyay N.K.,
Griffin J.D.,
Paredes M.,
Medina M.,
Kosik K.S.
Publication year - 2002
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.10151
Subject(s) - microbiology and biotechnology , proto oncogene tyrosine protein kinase src , hepatocyte growth factor , rac gtp binding proteins , biology , morphogenesis , abl , tyrosine kinase , catenin , tyrosine phosphorylation , phosphorylation , rac1 , wnt signaling pathway , signal transduction , receptor , biochemistry , gene
δ‐Catenin associates with adhesive junctions and facilitates cellular morphogenesis (Lu et al., 1999). Here we show that δ‐catenin colocalizes with actin filaments and Abl tyrosine kinase in the growth cones of cultured hippocampal neurons. PC12 cells induced to express δ‐catenin show accelerated neurite extension upon nerve growth factor (NGF) stimulation. STI571, an Abl family kinase inhibitor, further accentuates these stimulatory effects. δ‐Catenin is a potent substrate for Abl in vitro using an immunocomplex assay and most of the Abl‐induced tyrosine phosphorylation within cells is present in the N‐terminus of δ‐catenin. When δ‐catenin‐expressing epithelial cells are induced to scatter in response to hepatocyte growth factor (HGF), STI571 leads to the rapid redistribution of δ‐catenin and changes in cellular morphology. We suggest that δ‐catenin is a possible Abl substrate and acts downstream of Abl to orchestrate actin‐based cellular morphogenesis. © 2002 Wiley‐Liss, Inc.