Inhibitory effect of SPE-39 due to tyrosine phosphorylation and ubiquitination on the function of Vps33B in the EGF-stimulated cells.

@article{Ishii2012InhibitoryEO,
  title={Inhibitory effect of SPE-39 due to tyrosine phosphorylation and ubiquitination on the function of Vps33B in the EGF-stimulated cells.},
  author={Ayumi Ishii and Kanae Kamimori and Mineyoshi Hiyoshi and Hiroshi Kido and Takeshi Ohta and Hiroaki Konishi},
  journal={FEBS letters},
  year={2012},
  volume={586 16},
  pages={2245-50}
}
Although SPE-39 is a binding protein to Vps33B that is one of the subunit in the mammalian HOPS complex, the elements of SPE-39 function remain unknown. Here, we show that tyrosine phosphorylation of SPE-39 following EGF stimulation plays a role in the stability of SPE-39 itself. Ubiquitination of the C-terminal region of SPE-39 was also elevated in response to EGF stimulation, and this process was regulated by the phosphorylation of Tyr-11 in SPE-39. However, association of Vps33B with SPE-39… CONTINUE READING

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