2012年5月
Phosphorylation in the activation loop as the finishing touch in c-Kit activation
JOURNAL OF BIOCHEMISTRY
- 巻
- 151
- 号
- 5
- 開始ページ
- 457
- 終了ページ
- 459
- 記述言語
- 英語
- 掲載種別
- 記事・総説・解説・論説等(学術雑誌)
- DOI
- 10.1093/jb/mvs031
- 出版者・発行元
- OXFORD UNIV PRESS
Receptor tyrosine kinases are a group of transmembrane proteins that transmit signals in response to stimulation by ligands including growth factors and cytokines. They share a common mechanism of activation through receptor dimerization or oligomerization, but subsequent routes to their full activation appear to be various. A recent paper published by DiNitto et al. (Function of activation loop tyrosine phosphorylation in the mechanism of c-Kit autoactivation and its implication in sunitinib resistance. J. Biochem. 2010;147:601-609) analysed a process of c-Kit autoactivation in detail. They revealed that phosphorylation in the activation loop, which is crucial for activation of many types of tyrosine kinases, is dispensable for c-Kit activation. However, the phosphorylation affects the sensitivity of c-Kit to kinase inhibitors, thus representing the finishing touch in c-Kit activation.
- リンク情報
- ID情報
-
- DOI : 10.1093/jb/mvs031
- ISSN : 0021-924X
- Web of Science ID : WOS:000303332400001