The role of v-Fgr myristoylation and the Gag domain in membrane binding and cellular transformation.
The role of v-Fgr myristoylation and the Gag domain in membrane binding and cellular transformation.
复制标题
v-Fgr 肉豆蔻酰化和 Gag 结构域在膜结合和细胞转化中的作用。
DOI：
10.1006/viro.1998.9323
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发表时间：
1998
期刊：
影响因子：
--
通讯作者：
Reddy,EP
中科院分区：
文献类型：
--
作者：
Baker,SJ;Cosenza,SC;Reddy,EP
Thev-fgroncogene encodes a chimeric oncoprotein composed of feline sarcoma virus (FeSV)-derived gag and cellular-derived actin and c-Fgr sequences. v-Fgr is myristoylated and membrane bound, two criteria which must be met forsrckinases to induce cellular transformation. Although inhibition of myristoylation resulted in a decreased ability of v-Fgr to sediment with membranes from an NIH-3T3 P100 fraction, deletion of the gag domain caused nearly all of the protein to remain unbound and cytosolic. Systematic deletions within gag indicate that while amino acids 3 through 9 are critical determinants of myristoylation and/or define a domain which directs membrane localization, these residues cooperate with additional gag sequences when anchoring the protein to the plasma membrane. Furthermore, nonmyristoylated and/or cytoplasmic variants of v-Fgr failed to induce anchorage-independent growth of NIH-3T3 cells, indicating that proper subcellular localization of v-Fgr is a key factor in its ability to induce transformation.
