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Palmitoylation‐dependent endosomal localization of AATYK1A and its interaction with Src
Author(s) -
Tsutsumi Koji,
Tomomura Mineko,
Furuichi Teiichi,
Hisanaga Shinichi
Publication year - 2008
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2008.01219.x
Subject(s) - biology , endosome , palmitoylation , microbiology and biotechnology , proto oncogene tyrosine protein kinase src , computational biology , phosphorylation , biochemistry , intracellular , enzyme , cysteine
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.