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Genes to Cells (2008) 13, 949-964. doi:10.1111/j.1365-2443.2008.01219.x
© 2008 Blackwell Publishing or its licensors

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Palmitoylation-dependent endosomal localization of AATYK1A and its interaction with Src

Koji Tsutsumi1,*, Mineko Tomomura2, Teiichi Furuichi3 and Shin-ichi Hisanaga1,*

1 Department of Biological Sciences, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397, Japan
2 Laboratory for Neuronal Growth Mechanisms, and
3 Laboratory for Molecular Neurogenesis, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan

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.


Communicated by: Takeo Kishimoto

* Correspondence: tutumi-kouji{at}ed.tmu.ac.jp or hisanaga-shinichi{at}tmu.ac.jp







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