Question: RTKs can activate the enzyme phosphoinositide 3-kinase, which phosphorylates inositol phospholipids. These phospholipids then do what? Choose one: a.)serve as docking sites that recruit specific intracellular signaling proteins to the plasma membrane b.)activate G proteins c.)activate Ras d.)serve as phosphate donors in ...

Choose one: The RTKS are internalized and digested in lysosomes. SH2 domains are internalized and digested in lysosomes. Tyrosine kinases remove the phosphates from RTK and other intracellular signaling proteins. The RTK is inactivated by phospholipase C. SH2 domains remove the phosphates from RTKS and other intracellular signaling proteins.

Question: G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs) are two basic receptor types by which cells transduce signals. Classify the phrases by whether they describe GPCRs, RTKs, both types of receptors, or neither of these two types:

Question: 12. a. Describe the structure of GPCRs versus RTKs. b. Describe how ligand binding causes changes to the GPCR versus RTK that are crucial for initiation of the signaling cascade inside of the cell. c. Describe the G proteins used by GPCR versus RTKs. How are these G proteins different and how are they activated? 13.

Question: Select statements that accurately describe receptor tyrosine kinases (RTK). A ligand binds to the extracellular domain. The structure includes a transmembrane helix. Some RTKs are dimeric in the presence of a ligand. The intracellular domain has kinase domains. V GTPase activity is required for autophosphorylation (cross-phosphorylation).

Question: Select statements that accurately describe receptor tyrosine kinases (RTK). A ligand binds to the extracellular domain. The intracellular domain has kinase domains. The structure includes a transmembrane helix. The a subunit contains seven a helices that span the membrane. RTKs are usually monomeric in the absence of a ligand.

1st attempt What do the phosphorylated tyrosines on activated RTKS do? Choose one: They activate the enzymatic activity of the RTKS. They serve as binding sites for G proteins. They serve as binding sites for a variety of intracellular signaling proteins. They …

Which of the following explains why Ras is activated quickly by RTKS? a. RTKS phosphorylate Ras b. Ras changes conformation upon ligand binding to prepare for activation. Ras binds phosphorylated tyrosine residues on RTKS C. d. Ras is maintained at the cytosolic side of the plasma membrane through a lipid-mediated attachment e. Ras is a kinase

Ligand binding to the extracellular RTK domain stimulates dimerization of RTKs, and the cytosolic domains cross-phosphorylate one another to activate the kinase domains. b. Ligand binding to the extracellular RTK domain triggers an influx of calcium through calcium channels, activating second messengers within the cell.

Select statements that accurately describe receptor tyrosine kinases (RTK). GTPase activity is required for autophosphorylation (cross-phosphorylation). The a subunit contains seven a helices that span the membrane. The intracellular domain has kinase domains. The structure includes a transmembrane helix. RTKs are usually monomeric in the ...