Tyrosine residues direct the ubiquitination and degradation of the NY-1 hantavirus G1 cytoplasmic tail.

@article{Geimonen2003TyrosineRD,
  title={Tyrosine residues direct the ubiquitination and degradation of the NY-1 hantavirus G1 cytoplasmic tail.},
  author={Erika Geimonen and Imelyn Fernandez and Irina N. Gavrilovskaya and Erich R. Mackow},
  journal={Journal of virology},
  year={2003},
  volume={77 20},
  pages={
          10760-868
        }
}
The hantavirus G1 protein contains a long C-terminal cytoplasmic tail of 142 residues. Hantavirus pulmonary syndrome-associated hantaviruses contain conserved tyrosine residues near the C terminus of G1 which form an immunoreceptor tyrosine activation motif (ITAM) and interact with Src and Syk family kinases. During studies of the G1 ITAM we observed that fusion proteins containing the G1 cytoplasmic tail were poorly expressed. Expression of G1 cytoplasmic tail constructs were dramatically… CONTINUE READING
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