Oligomerizing potential of a focal adhesion LIM protein Hic-5 organizing a nuclear-cytoplasmic shuttling complex.

@article{Mori2006OligomerizingPO,
  title={Oligomerizing potential of a focal adhesion LIM protein Hic-5 organizing a nuclear-cytoplasmic shuttling complex.},
  author={Kazunori Mori and Masayuki Asakawa and Miki Cristina Hayashi and Miwako Imura and Takahiro Ohki and Etsuko Hirao and Joo-ri Kim-Kaneyama and Kiyoshi Nose and Motoko Shibanuma},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 31},
  pages={
          22048-61
        }
}
Hic-5 is a focal adhesion LIM protein serving as a scaffold in integrin signaling. The protein comprises four LD domains in its N-terminal half and four LIM domains in its C-terminal half with a nuclear export signal in LD3 and is shuttled between the cytoplasmic and nuclear compartments. In this study, immunoprecipitation and in vitro cross-linking experiments showed that Hic-5 homo-oligomerized through its most C-terminal LIM domain, LIM4. Strikingly, paxillin, the protein most homologous to… CONTINUE READING

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