Characterization of Akt overexpression in MiaPaCa-2 cells: prohibitin is an Akt substrate both in vitro and in cells.

Akt (PKB) is a serine/threonine protein kinase that plays an important role in the transduction of signals affecting apoptosis, cell proliferation and survival. The Akt gene is frequently hyperactivated in tumors and has been shown to be amplified in a number of types of human cancers. Furthermore, Akt activity is elevated in cell lines with the mutated PTEN tumor suppressor gene.

Role of focal adhesion kinase in human cancer: a potential target for drug discovery.

The focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that localizes to the points of cell contact with the extracellular matrix, called focal adhesions. FAK is involved in several cellular processes including invasion, motility, proliferation and apoptosis. In in vivo animal studies, FAK has been shown to contribute to tumor development and malignancy.

Chkl binds and phosphorylates BAD protein.

Chk1 (checkpoint kinase 1) is a serine-threonine kinase that is critical for G2/M arrest in response to DNA damage. Chk1 phosphorylates Cdc25C at serine-216, a major regulatory site, in response to DNA damage. Furthermore, Chk1 also phosphorylates Cdc25A on serine 123 which accelerates its degradation through the ubiquitin-proteasome pathway and arrests cells in late G2-phase after DNA damage.

Functional analysis of focal adhesion kinase (FAK) reduction by small inhibitory RNAs.

The focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that localizes to the points of cell contact with the extracellular matrix, called focal adhesions. Many factors induce tyrosine phosphorylation of FAK including growth factors, neuropeptides and integrin-dependent adhesion to the extracellular matrix. FAK has been implicated in several cellular processes such as invasion, motility, proliferation and apoptosis.