Interaction of Cap Z with actin. The NH2-terminal domains of the alpha 1 and beta subunits are not required for actin capping, and alpha 1 beta and alpha 2 beta heterodimers bind differentially to actin.

@article{Casella1994InteractionOC,
  title={Interaction of Cap Z with actin. The NH2-terminal domains of the alpha 1 and beta subunits are not required for actin capping, and alpha 1 beta and alpha 2 beta heterodimers bind differentially to actin.},
  author={James F. Casella and M{\'o}nica A. Torres},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 9},
  pages={6992-8}
}
Cap Z is a widely distributed, highly conserved, heterodimeric protein that binds to the barbed ends of actin filaments, but does not sever filaments. In chicken, two variant cDNAs (alpha 1 and alpha 2) encoding proteins homologous to the alpha subunit of Cap Z have been described versus one for the beta subunit. To establish the effect of each subunit and of the two potential heterodimers (alpha 1 beta and alpha 2 beta) on actin and to explore the functional domains of the proteins, RNA… CONTINUE READING
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