期刊
ONCOGENE
卷 31, 期 28, 页码 3381-3391出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/onc.2011.510
关键词
cytoplasmic c-Fos; phospholipid synthesis regulation; c-Fos-tyr phosphorylation; c-Src; TC45 phosphatase
资金
- ANPCyT
- CONICET
- Ministerio de Ciencia, Tecnologi a e Innovacio n Productiva de Argentina
- SECyT-Universidad Nacional de Cordoba, Argentina
- JS McDonnell Foundation
Our previous work showed that in T98G cells, a human glioblastoma multiforme-derived cell line, the association of c-Fos to the endoplasmic reticulum (ER) and consequently, the capacity of c-Fos to activate phospholipid synthesis, is regulated by the phosphorylation state of tyrosine (tyr) residues # 10 and # 30 of c-Fos. The small amount of c-Fos present in quiescent cells is tyrphosphorylated, is dissociated from the ER membranes and does not activate phospholipid synthesis. However, on induction of the cell to re-enter growth, c-Fos expression is rapidly induced, it is found dephosphorylated, associated to ER membranes and activating phospholipid synthesis (Portal et al., 2007). Herein, using in vivo and in vitro experimental strategies, we show that the kinase c-Src is capable of phosphorylating tyr residues of c-Fos whereas the phosphatase TC45 T-cell protein-tyr phosphatase (TC-PTP) dephosphorylates them, thus enabling c-Fos/ER association and activation of phospholipid synthesis. Results also suggest that the regulation of the phosphorylation/dephosphorylation cycle of c-Fos occurs at the TC-PTP level: induction of cells to re-enter growth promotes the translocation of TC45 from a nuclear to a cytoplasmic location concomitant with its activation. Activated TC45 in its turn promotes dephosphorylation of pre-formed c-Fos, enabling cells to rapidly activate phospholipid synthesis to respond to its growth demands. Oncogene (2012) 31, 3381-3391; doi: 10.1038/onc.2011.510; published online 21 November 2011
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据