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Commentary |
National Human Genome Research Institute, 49 Convent Drive, 49/4A38, National Institutes of Health, Bethesda, MD 20892, USA
* Author for correspondence (e-mail: pams{at}nhgri.nih.gov )
The Tec kinases represent the second largest family of mammalian
non-receptor tyrosine kinases and are distinguished by the presence of
distinct proline-rich regions and pleckstrin homology domains that are
required for proper regulation and activation. Best studied in lymphocyte and
mast cells, these kinases are critical for the full activation of
phospholipase-C 
(PLC-) and Ca2+ mobilization
downstream of antigen receptors. However, it has become increasingly clear
that these kinases are activated downstream of many cell-surface receptors,
including receptor tyrosine kinases, cytokine receptors, integrins and
G-protein-coupled receptors. Evidence suggests that the Tec kinases influence
a wide range of signaling pathways controlling activation of MAP kinases,
actin reorganization, transcriptional regulation, cell survival and cellular
transformation. Their impact on cellular physiology suggests that the Tec
kinases help regulate multiple cellular processes beyond Ca2+
mobilization.
Key words: Tyrosine kinase, Pleckstrin homology domain, Phospholipase C-, Calcium mobilization, Actin cytoskeleton
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