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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
Published on: December 20, 2017
Palmitoylation-dependent endosomal localization of AATYK1A and its interaction with Src
Koji Tsutsumi1, Mineko Tomomura, Teiichi Furuichi
1Department of Biological Sciences, Tokyo Metropolitan University, Hachioji, Tokyo, Japan. tutumi-kouji@ed.tmu.ac.jp
Abstract:
Apoptosis-associated tyrosine kinase 1 (AATYK1), also named LMTK1, was previously isolated as an apoptosis-related gene from 32Dcl3 myeloid precursor cells, but its precise function remains unknown. AATYK1A, an isoform without a transmembrane domain, is highly expressed in neurons. We identified palmitoylation of AATYK1A at three N-terminal cysteine residues in cortical cultured neurons and COS-7 cells and found that palmitoylation determined localization of AATYK1A to the transferrin receptor-positive recycling endosomes. Further, we identified the tyrosine kinase Src as a novel AATYK1A-interacting protein. Src and Fyn phosphorylated AATYK1A at tyrosines 25 and 46 in a palmitoylation-dependent manner. The association of AATYK1A with Src in endosomes was also found to be palmitoylation-dependent. These results indicate that palmitoylation is a critical factor not only for the subcellular localization of AATYK1A but also for its interaction with Src.
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