Final answer:
The statement is true; PI-3K is indeed recruited to an activated RTK where it plays a crucial role in signaling pathways that influence cellular metabolism, protein synthesis, and cell division.
Step-by-step explanation:
The statement that PI-3K is recruited to an activated Receptor Tyrosine Kinase (RTK) is true. PI-3K (phosphoinositide 3-kinase) is a critical signaling molecule that gets recruited to the membrane where it associates with the activated RTK. The RTK itself is activated via ligand binding, such as a growth factor-like EGF (Epidermal Growth Factor), which leads to the dimerization of the receptor and subsequent autophosphorylation of tyrosine residues. This phosphorylation creates docking sites for intracellular signaling proteins, including PI-3K. PI-3K then contributes to the generation of second messengers and the activation of other kinases, like AKT, ultimately influencing processes such as cellular metabolism, protein synthesis, and cell division. The activation of the MAP kinase pathway through a series of phosphorylation events can lead to the synthesis of proteins necessary for cell proliferation. Therefore, the recruitment of PI-3K is a part of the signaling cascade initiated by the activation of RTKs.