These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Mapping of the functional domains of the v-rel oncogene.
    Author: Garson K, Kang CY.
    Journal: Oncogene; 1990 Sep; 5(9):1431-4. PubMed ID: 2216467.
    Abstract:
    Previously, the v-rel oncogene was shown to code for a protein of 503 amino acids. The protein product of v-rel was identified as a 59 kDa protein (pp59v-rel), phosphorylated predominantly on serine residues. Although the signal required for the nuclear localization of pp59v-rel in chicken embryo fibroblasts was identified, the regions of v-rel important for transformation have not been mapped. In this study, 12 linker insertion mutants of v-rel were constructed and tested for transforming activity. Seven linker insertion mutants which mapped between amino acid residues 29 and 275 abolished transformation. The remaining 5 mutants which contained linker insertion mutations between amino acid residues 332 and 459 transformed at wild type levels. The results of this analysis localize the functional domains of the v-rel oncogene to the N-terminus. Earlier reports have shown that pp59v-rel resides in a high molecular weight complex with several other cellular proteins. The transforming mutants co-precipitated the same set of cellular proteins when immunoprecipitated with v-rel antiserum. This indicates that all transforming mutants retained the ability to bind within the reported complex.
    [Abstract] [Full Text] [Related] [New Search]