𝔖 Bobbio Scriptorium
✦   LIBER   ✦

The assembly of signalling complexes by receptor tyrosine kinases

✍ Scribed by George Panayotou; Michael D. Waterfield

Publisher
John Wiley and Sons
Year
1993
Tongue
English
Weight
951 KB
Volume
15
Category
Article
ISSN
0265-9247

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✦ Synopsis

Cell proliferation in response to growth factors is mediated by specific high affinity receptors. Ligand-binding by receptors of the protein tyrosine kinase family results in the stimulation of several intracellular signal transduction pathways. Key signalling enzymes are recruited to the plasma membrane through the formation of stable complexes with activated receptors. These interactions are mediated by the conserved, non-catalytic SH2 domains present in the signalling molecules, which bind with high affinity and specificity to tyrosine-phosphorylated sequences on the receptors. The assembly of enzyme complexes is emerging as a major mechanism of signal transduction and may regulate the pleiotropic effects of growth factors.

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✍ Jason M. Haugh; Ian C. Schneider; Jodee M. Lewis πŸ“‚ Article πŸ“… 2004 πŸ› Elsevier Science 🌐 English βš– 587 KB

Intracellular signaling proteins are very often regulated by site-specific phosphorylation. For example, growth factor receptors in eukaryotic cells contain intrinsic tyrosine kinase activity and use inter- and intra-molecular interactions to recruit and orient potential protein substrates for phosp