ROS1 is a proto-oncogene and member of the sevenless subfamily of tyrosine kinase insulin receptor genes. ROS1 is highly-expressed in a variety of tumor cell lines and functions as a growth or differentiation factor receptor. The FIG gene can fuse with the ROS1 gene in glioblastoma cell lines. The resulting ROS1/FIG fusion protein is a constitutively activated tyrosine kinase. Direct interaction of ROS1 and the phosphatase SHP-1 can lead to efficient downregulation of ROS1-mediated signaling. Binding sites in the ROS1 cytoplasmic domain display high affinity binding to the SHP-1 N-terminal SH2 domain.
Journal of cell science, 117(Pt 21), 5165-5178 (2004-10-01)
Signaling of receptor tyrosine kinases (RTKs) is regulated by protein-tyrosine phosphatases (PTPs). We previously discovered the efficient downregulation of Ros RTK signaling by the SH2 domain PTP SHP-1, which involves a direct interaction of both molecules. Here, we studied the
The transmembrane proto-oncogene receptor tyrosine kinase (RTK) ROS is an orphan receptor that is aberrantly expressed in neoplasms of the central nervous system. Here, we report the fusion of its carboxy-terminal kinase domain to the amino-terminal portion of a protein
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