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Lecture 11

Cell Bio lecture 11.docx

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Course Code
Biology 2382B
Robert Cumming

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Receptor Tyrosine Kinases (RTKs) Ras, a GTPase Switch Protein Activation of RTKs -Tyrosine Kinase activity not present in absence of ligand -Ligand binding triggers dimerization which activates Kinase activity -RTK phosphorylates itself, and additional tyrosine residues adjacent to the kinase part of the cytosolic domain Activating Ras -EGF binds EGFR; activating EGF Dimer (an RTK) -Phosphorylation of cytosolic tyrosine Adaptor Proteins residues -contain unique domains that recognize specific -GRB2 has SH2 domain; binds tyrosine sequences -SH3 domain binds proline of Sos (a guanine nucleotide exchange factor; GEF) -Adaptor Proteins contain Adaptor Domains: -Sos bins to inactive form of Ras; promoting dissociation of GDP and GTP SH2 -recognizes phosphorylated tyrosines on RTK binds Ras -Ras now active PTB -Docking site for other signal transduction proteinRas/MAPK Pathway -Active Ras binds inactive Raf and -Allows more phosphorylation on adaptor proteins removes the inhibitory protein;14-3-3 -Raf is a kinase and now phosphorylates MEK -MEK then phosphorylates MAPK -MAPK can now translocate to the nucleus and activate many transcription factors Dis
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