Assembly functions of vesicular stomatitis virus matrix protein are not disrupted by mutations at major sites of phosphorylation.

@article{Kaptur1995AssemblyFO,
  title={Assembly functions of vesicular stomatitis virus matrix protein are not disrupted by mutations at major sites of phosphorylation.},
  author={P E Kaptur and Margie O. McKenzie and Gail Williams Wertz and Douglas S Lyles},
  journal={Virology},
  year={1995},
  volume={206 2},
  pages={
          894-903
        }
}
The matrix (M) protein of vesicular stomatitis virus (VSV) plays a central role in virus assembly by binding the nucleocapsid core to the viral envelope during the budding process. A small percentage of M protein molecules are phosphorylated in vivo, but the role of phosphorylation in M protein function is unknown. Using limited proteolysis, we previously determined the sites of in vivo phosphorylation for VSV M protein to be Thr 31 (and possibly Ser 32) and a site N-terminal to position 19… CONTINUE READING
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