Two separate functions are encoded by the carboxyl-terminal domains of the yeast cyclase-associated protein and its mammalian homologs. Dimerization and actin binding.

@article{Zelicof1996TwoSF,
  title={Two separate functions are encoded by the carboxyl-terminal domains of the yeast cyclase-associated protein and its mammalian homologs. Dimerization and actin binding.},
  author={Audrey Zelicof and V P Protopopov and Della David and Xueyan Lin and Vardit Lustgarten and Jeffrey E Gerst},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 30},
  pages={18243-52}
}
The yeast adenylyl cyclase-associated protein, CAP, was identified as a component of the RAS-activated cyclase complex. CAP consists of two functional domains separated by a proline-rich region. One domain, which localizes to the amino terminus, mediates RAS signaling through adenylyl cyclase, while a domain at the carboxyl terminus is involved in the regulation of cell growth and morphogenesis. Recently, the carboxyl terminus of yeast CAP was shown to sequester actin, but whether this function… CONTINUE READING

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