Abstract
Rak is a 54 kDa protein tyrosine kinase originally isolated from breast cancer cells and expressed in epithelial cells. It resembles the protooncogene Src structurally but lacks an amino-terminal myristylation site and localizes to the nuclear and perinuclear regions of the cell. We report here that expression of Rak in 2 different breast cancer cell lines inhibits growth and causes G1 arrest of the cell cycle. This growth inhibition is kinase-dependent but does not require the Rak SH2 or SH3 domain. Rak also binds to the pRb tumor-suppressor protein but inhibits growth even in cells that lack pRb. These results suggest that Rak regulates cell growth by phosphorylating perinuclear proteins and has a function that is distinct from the Src-related kinase family.
Original language | English |
---|---|
Pages (from-to) | 139-146 |
Number of pages | 8 |
Journal | International Journal of Cancer |
Volume | 104 |
Issue number | 2 |
DOIs | |
State | Published - Mar 20 2003 |
Keywords
- Breast cancer
- Cell cycle
- Rak
- Src
- Tyrosine kinase
ASJC Scopus subject areas
- Oncology
- Cancer Research