Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Sci. STKE, 30 March 2004
Vol. 2004, Issue 226, p. tw121
[DOI: 10.1126/stke.2262004TW121]



The human FHIT gene is frequently altered in many cancers, and as such, its proposed product, a diadenosine polyphosphate hydrolase, is thought to be a tumor suppressor. Its overexpression suppresses cell growth, and transgenic mice that lack the FHIT gene have a higher incidence of spontaneous tumors. However, the pathway by which Fhit induces apoptosis is still not known, although its tumor suppression effect is independent of its enzymatic activity. Pekarsky et al. examined the amino acid sequence of Fhit and identified a potential phosphorylation site for the cytoplasmic tyrosine kinase Src. Their study demonstrates that Src directly phosphorylates a single tyrosine residue in Fhit in vitro. Overexpression of a constitutively activated form of Src in cultured human embryonic kidney cells resulted in tyrosine phosphorylation of Fhit. Phosphorylated Fhit was also detected in lysates of several normal human tissues and cells, but not in any human tumor cell lines examined. Downstream targets of phosphorylated Fhit that operate in cell growth regulation remain to be determined.

Y. Pekarsky, P. N. Garrison, A. Palamarchuk, N. Zanesi, R. I. Aqeilan, K. Huebner, L. D. Barnes, C. M. Croce, Fhit is a physiological target of the protein kinase Src. Proc. Natl. Acad. Sci. U.S.A. 101, 3775-3779 (2004). [Abstract] [Full Text]

Citation: Fhit for Action. Sci. STKE 2004, tw121 (2004).

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882