Biology 2382B Lecture Notes - Lecture 16: Gene Duplication, Hyperactivation, Chromosome
Document Summary
Receptor tyrosine kinases (rtk) is a class of receptors that are widely expressed: structure, dimerization, autophosphorylation. Rtk controls functions related to mitogenic signaing. Adapter proteins, grb2: ptb, sh2, sh3. Ras and its regulation (gef, gap, sos) Ras/map kinase pathway operation (raf, mek, mapk), egf. Extracellular (ligand-binding) domain: ligands include growth factors and insulin. Cytoplasmic domain with intrinsic tyrosine kinase activity which is stimulated by ligand binding due to receptor dimerization. Ras acts as a gtpase switch protein to signal further (cid:498)downstream(cid:499) kinases. Aberrant signaling is at root of many human cancers. Transmembrane protein with an extracellular domain that binds a ligand (usually a growth factor) Single transmembrane domain with alpha helical structure unlike g protein coupled receptor that has 7 domains. Cytoplasmic (intracellular) domain has intrinsic tyrosine kinase domains. When ligand binds to the extracellular portion, it results in dimerization of the receptor to another receptor.