Evidence of both extra- and intracellular cysteine targets of protein modification for activation of RET kinase

Anwarul A. Akhand, Takanari Ikeyama, Satoru Akazawa, Masashi Kato, Khaled Hossain, Kozue Takeda, Haruhiko Suzuki, Masahide Takahashi, Izumi Nakashima

研究成果: Article

10 被引用数 (Scopus)

抄録

By use of a specifically sulfhydryl group-reactive chemical, 1,4-butanediyl-bismethanethiosulfonate (BMTS), we studied the localization of oxidative stress-responsive target cysteines for activation of a receptor-type protein tyrosine kinase, c-RET. The chemical, which reacted with RET proteins on the cell surface for sulfhydryl-linked aggregation, induced autophosphorylation and activation of RET kinase. When extracellular domain-deleted RET mutant (RET-PTC-1) cells were exposed to BMTS, neither the molecular status nor the activity of the enzyme was affected, suggesting that the target cysteines of BMTS to which cells were exposed for reaction are located in the cysteine-rich region of the extracellular domain of RET kinase. Despite this result, the exposure of a subcellular form of c-RET or RET-PTC-1 kinase isolated by immunoprecipitation to BMTS did induce activation of the enzyme. These results suggest that cysteines in both the extracellular and the intracellular domains of RET can work as target sites of accessible BMTS and possibly other oxidative elements for structural modification and activation of RET kinase.

本文言語English
ページ(範囲)826-831
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
292
4
DOI
出版ステータスPublished - 12-04-2002
外部発表はい

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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