Oncogenic targeting of an activated tyrosine kinase to the Golgi apparatus in a glioblastoma

Alan Charest*, Vicky Kheifets, Julie Park, Keara Michelle Lane, Kevin McMahon, Cathy L. Nutt, David Housman

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

75 Scopus citations


Activating oncogenic mutations of receptor tyrosine kinases (RTKs) have been reported in several types of cancers. In many cases, genomic rearrangements lead to the fusion of unrelated genes to the DNA coding for the kinase domain of RTKs. All RTK-derived fusion proteins reported so far display oligomerization sequences within the 5′ fusion partners that are responsible for oncogenic activation. Here, we report a mechanism by which an altered RTK gains oncogenic potential in a glioblastoma cell line. A microdeletion on 6q21 results in the fusion of FIG, a gene coding for a Golgi apparatus-associated protein, to the kinase domain of the protooncogene c-ROS. The fused protein product FIG-ROS is a potent oncogene, and its transforming potential resides in its ability to interact with and become localized to the Golgi apparatus. Thus we have found a RTK fusion protein whose subcellular location leads to constitutive kinase activation and results in oncogenic transformation.

Original languageEnglish (US)
Pages (from-to)916-921
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number3
StatePublished - Feb 4 2003

ASJC Scopus subject areas

  • General


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