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LIFE 210 (38)

Receptor tyrosine kinases, Ras, PI 3-kinase

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Colorado State University
Life Science
LIFE 210
Paul Laybourn

2 November Like GPCRs, enzyme linked receptors are transmembrane proteins, but typically single pass. The intracellular domain has enzymatic activity or associates directly with an enzyme. Some subfamilies of receptor tyrosine kinase (RTKs) RTKs are the most numerous enzyme-coupled receptors (~60 genes) Activation of receptor tyrosine kinases (RTKs) Ligand binding causes receptor dimerization bringing the kinase domains of two receptor chains together Transautophosphorylation on multiple tyrosine residues – higher activity Phosphorylated RTKs serve as docking sites for intracellular signaling proteins SH2 and PTB domains within signaling proteins recognize phospho – tyrosine Formation of a signaling complex that relays the signal onward Some proteins bind activated RTKs to down regulate them by endocytosis. Development of cancer when this is not effective. Ras is a monomeric GTPase that relays signals from RTKs Has a covalently attached lipid for membrane anchoring Molecular switch: GTP/GDP. Activated by GEFs, inactivated by GAPs Can act as a signaling hub 30% of tumors have hyperactive mutant forms of Ras How an RTK can activate the GTPase Ras? An example from the fly eye Adaptors and GEFs couple RTK activation to Ras activation Ras activates a mitogen-activated protein (MAP) kinase mod
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