Tyrosine phosphorylation of vinexin in v-Src-transformed cells attenuates the affinity for vinculin.
Vinexin is an adaptor-type focal adhesion protein that interacts with vinculin. Here, we report the tyrosine phosphorylation of vinexin alpha in v-Src-transformed NIH3T3 cells. Point mutational analysis of vinexin alpha clarified that three tyrosine residues in vinexin alpha were phosphorylated. A non-phosphorylatable mutant of vinexin alpha had higher binding affinity for vinculin than its wild-type counterpart. In conclusion, vinexin alpha is tyrosine phosphorylated in v-Src-transformed cells, and this tyrosine phosphorylation of vinexin alpha attenuates the association of vinexin alpha with vinculin.
Umemoto
Tsutomu
T
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, Japan.
Tanaka
Kana
K
Ueda
Kazumitsu
K
Kioka
Noriyuki
N
D000818:Animals; D002461:Cell Line, Transformed; D051379:Mice; D009124:Muscle Proteins / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D041681:NIH 3T3 Cells; D015688:Oncogene Protein pp60(v-src) / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D014443:Tyrosine / Q000235:genetics / Q000378:metabolism*; D016596:Vinculin / Q000378:metabolism*; D048868:Adaptor Proteins, Signal Transducing
D009124:Muscle Proteins; D015688:Oncogene Protein pp60(v-src); D014443:Tyrosine; D016596:Vinculin; C117452:Sorbs3 protein, mouse; D048868:Adaptor Proteins, Signal Transducing