KINE 3012 Chapter Notes - Chapter 9.13: Kras, Gtpase, Hras

• School: York University
• Department: Kinesiology & Health Science
• Course: KINE 3012
• Professor: Michael Connor

Document Summary

Docking sites for intracellular signalling proteins: one kinase domains of rtk dimers are activated, they phosphorylate multiple additional sides in cytosolic part of receptor. This phosphorylation creates high affinity docking sites for intracellular signalling proteins: each protein binds to phosphorylated site on activated receptor, once bound to activated rtk, a signalling protein becomes phosphorylated on tyrosine & activated. However, binding might be enough for protein to become activated b/c conformational change: receptor phosphorylation triggers assembly of intracellular signalling complex which relay onward signal, different rtks bind different combinations of signalling proteins & activate different responses. Promote development of cancer: gef determines which membrane the gtpase is activated & which downstream proteins gtpase activates, grb2 is an adaptor protein that links sev receptor (rtk) to sos (ras-gef) protein. Sh2 domain of grb2 adaptor binds to activated receptor, while two. Once activates, ras activates various other signalling proteins to relay signal downstream.