Mutation of the Highly Conserved Ser-40 of the HIV-1 p6 Gag Protein to Phe Causes the Formation of a Hydrophobic Patch, Enhances Membrane Association, and Polyubiquitination of Gag

@inproceedings{Hahn2014MutationOT,
  title={Mutation of the Highly Conserved Ser-40 of the HIV-1 p6 Gag Protein to Phe Causes the Formation of a Hydrophobic Patch, Enhances Membrane Association, and Polyubiquitination of Gag},
  author={Friedrich F. Hahn and Christian Setz and Melanie Friedrich and Pia Rauch and Sara Marie Solbak and Nils {\AA}ge Fr{\o}ystein and Petra Henklein and J{\"o}rg Votteler and Torgils Fossen and Ulrich Schubert},
  booktitle={Viruses},
  year={2014}
}
The HIV-1 p6 Gag protein contains two late assembly (l-) domains that recruit proteins of the endosomal sorting complex required for transport (ESCRT) pathway to mediate membrane fission between the nascent virion and the cell membrane. It was recently demonstrated that mutation of the highly conserved Ser-40 to Phe (S40F) disturbs CA-SP1 processing, virus morphogenesis, and infectivity. It also causes the formation of filopodia-like structures, while virus release remains unaffected. Here, we… CONTINUE READING

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