Low molecular weight protein-tyrosine phosphatase controls the rate and the strength of NIH-3T3 cells adhesion through its phosphorylation on tyrosine 131 or 132.

@article{Chiarugi2000LowMW,
  title={Low molecular weight protein-tyrosine phosphatase controls the rate and the strength of NIH-3T3 cells adhesion through its phosphorylation on tyrosine 131 or 132.},
  author={Paola Chiarugi and Maria Letizia Taddei and Paolo Cirri and Doriana Talini and Francesca Buricchi and Guido Camici and Giampaolo Manao and Giovanni Raugei and G. Manao G. Ramponi},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 48},
  pages={37619-27}
}
The low molecular weight protein-tyrosine phosphatase (LMW-PTP) is an enzyme involved in platelet-derived growth factor (PDGF)-induced mitogenesis and cytoskeleton rearrangement. Our previous results demonstrated that LMW-PTP is able to bind and dephosphorylate activated PDGF receptor, thus inhibiting cell proliferation. Recently we have shown that LMW-PTP is specifically phosphorylated by c-Src in a cytoskeleton-associated fraction in response to PDGF, and this phosphorylation increases LMW… CONTINUE READING