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First published online 3 March 2009
doi: 10.1242/jcs.034843

Journal of Cell Science 122, 965-975 (2009)
Published by The Company of Biologists 2009
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Research Article

Differential trafficking of Src, Lyn, Yes and Fyn is specified by the state of palmitoylation in the SH4 domain

Izumi Sato1,*, Yuuki Obata1,*, Kousuke Kasahara1, Yuji Nakayama1, Yasunori Fukumoto1, Takahito Yamasaki2, Kazunari K. Yokoyama2, Takashi Saito3 and Naoto Yamaguchi1,{ddagger}

1 Department of Molecular Cell Biology, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba 260-8675, Japan
2 Gene Engineering Division, RIKEN BioResource Center, Tsukuba, Ibaraki 305-0074, Japan
3 Laboratory for Cell Signaling, RIKEN Research Center for Allergy and Immunology, Yokohama, Kanagawa 230-0045, Japan

{ddagger} Author for correspondence (e-mail: nyama{at}p.chiba-u.ac.jp)

Accepted 24 November 2008

Src-family tyrosine kinases (SFKs), which participate in a variety of signal transduction events, are known to localize to the cytoplasmic face of the plasma membrane through lipid modification. Recently, we showed that Lyn, an SFK member, is exocytosed to the plasma membrane via the Golgi region along the secretory pathway. We show here that SFK trafficking is specified by the palmitoylation state. Yes is also a monopalmitoylated SFK and is biosynthetically transported from the Golgi pool of caveolin to the plasma membrane. This pathway can be inhibited in the trans-Golgi network (TGN)-to-cell surface delivery by temperature block at 19°C or dominant-negative Rab11 GTPase. A large fraction of Fyn, a dually palmitoylated SFK, is directly targeted to the plasma membrane irrespective of temperature block of TGN exit. Fyn(C6S), which lacks the second palmitoylation site, is able to traffic in the same way as Lyn and Yes. Moreover, construction of Yes(S6C) and chimeric Lyn or Yes with the Fyn N-terminus further substantiates the importance of the dual palmitoylation site for plasma membrane targeting. Taken together with our recent finding that Src, a nonpalmitoylated SFK, is rapidly exchanged between the plasma membrane and late endosomes/lysosomes, these results suggest that SFK trafficking is specified by the palmitoylation state in the SH4 domain.

Key words: Src-family tyrosine kinases, trafficking, palmitoylation, Lyn, Fyn, Yes


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© The Company of Biologists Ltd 2009