Abi1/Hssh3bp1 pY213 links Abl kinase signaling to p85 regulatory subunit of PI-3 kinase in regulation of macropinocytosis in LNCaP cells.
Macropinocytosis is regulated by Abl kinase via an unknown mechanism. We previously demonstrated that Abl kinase activity is, itself, regulated by Abi1 subsequent to Abl kinase phosphorylation of Abi1 tyrosine 213 (pY213) [1]. Here we show that blocking phosphorylation of Y213 abrogated the ability of Abl to regulate macropinocytosis, implicating ... Abi1 pY213 as a key regulator of macropinocytosis. Results from screening the human SH2 domain library and mapping the interaction site between Abi1 and the p85 regulatory domain of PI-3 kinase, coupled with data from cells transfected with loss-of-function p85 mutants, support the hypothesis that macropinocytosis is regulated by interactions between Abi1 pY213 and the C-terminal SH2 domain of p85-thereby linking Abl kinase signaling to p85-dependent regulation of macropinocytosis.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Substitution, Cell Line, Tumor, Cyclic AMP, Cytoskeletal Proteins, Humans, Male, Mutation, Phosphatidylinositol 3-Kinases, Phosphopeptides, Phosphorylation, Phosphotyrosine, Pinocytosis, Protein Binding, Protein Kinase Inhibitors, Protein Structure, Tertiary, Proto-Oncogene Proteins c-abl, Signal Transduction
Adaptor Proteins, Signal Transducing, Amino Acid Substitution, Cell Line, Tumor, Cyclic AMP, Cytoskeletal Proteins, Humans, Male, Mutation, Phosphatidylinositol 3-Kinases, Phosphopeptides, Phosphorylation, Phosphotyrosine, Pinocytosis, Protein Binding, Protein Kinase Inhibitors, Protein Structure, Tertiary, Proto-Oncogene Proteins c-abl, Signal Transduction
FEBS Lett.
Date: Aug. 04, 2010
PubMed ID: 20598684
View in: Pubmed Google Scholar
Download Curated Data For This Publication
151440
Switch View:
- Interactions 2