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Breast cancer cell line proliferation blocked by the Src-related Rak tyrosine kinase

โœ Scribed by Tanya Meyer; LiHui Xu; Jinli Chang; Edison T. Liu; Rolf J. Craven; William G. Cance

Book ID
102861744
Publisher
John Wiley and Sons
Year
2003
Tongue
French
Weight
564 KB
Volume
104
Category
Article
ISSN
0020-7136

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โœฆ Synopsis

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 aminoโ€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 G~1~ arrest of the cell cycle. This growth inhibition is kinaseโ€dependent but does not require the Rak SH2 or SH3 domain. Rak also binds to the pRb tumorโ€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 Srcโ€related kinase family. ยฉ 2002 Wileyโ€Liss, Inc.

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