The role of v-Fgr myristoylation and the gag domain in membrane binding and cellular transformation

Stacey J. Baker, Stephen C. Cosenza, E. Premkumar Reddy

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


The v-fgr oncogene encodes a chimeric oncoprotein composed of feline sarcoma virus (FeSV)-derived gag and cellularderived actin and c-Fgr sequences. v-Fgr is myristoylated and membrane bound, two criteria which must be met for src kinases 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.

Original languageEnglish
Pages (from-to)1-11
Number of pages11
Issue number1
StatePublished - 15 Sep 1998
Externally publishedYes


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