Describe the three domains of a receptor tyrosine kinase. Explain the structure of the transmembrane domain and the amino acid composition and arrangement of this part of the receptor
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2. Describe the three domains of a receptor tyrosine kinase. Explain the structure of the transmembrane domain and the amino acid composition and arrangement of this part of the receptor
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- Discuss Concepts Describe the possible ways in which a G-proteincoupled receptor pathway could become defective and not trigger any cellular responses.6. Define a receptor tyrosine kinase and distinguish it from a serine/threonine kinase. (As we discuss ANY kinase in signalling pathways, pay close attention to what type of kinase it is...does it phosphorylate serene/threonine resides or tyrosine residues?)3. When you think about the primary structure of the mannose-6-P receptor, assuming that it is an integral membrane protein with one membrane-spanning domain and assuming that it has a ERSS, what are all of the different protein domains that must be present in this protein's primary structure to get it to where it needs to go and to carry out all of the functions/activities? (Draw a schematic of the protein structure/sequence and explain each region).
- 3. How does dimerization of a receptor tyrosine kinase promotes autophosphorylation of the intracellular domain of the receptor? How does the formation of a dimer helps the phosphorylation reaction?4. Describe where is the phosphate group added on a protein when it gets phosphorylated (what amino acid? what atom?). Then list all the ways that protein function may change after it gets phosphorylated PLEASE ANSWER BOTH. which of the following statements about heterotrimetric G proteins and their receptors is incorrect? A: when GTP binds to the alpha subunit of the G protein, the beta-gamma subunit dissociates from the alpha subunit B: G-protein coupled receptors contain nine transmembrane alpha helices C: binding of arrestin causes removal of the receptor from the membrane D: G protein- coupled receptors may be desensitized by serine phosphorylation I had chosen option A and got it wrong. What is the Correct answer and explain how it is. Also, where did i go wrong in choosing option A?Describe the 3 main steps for activation of receptor tyrosine kinases.
- 1. Based on the following description, draw the cell signaling pathway described (you only need to draw the pathway in one cell, but show the type of signaling described – you may need 2 diagrams). Compound X is released from cells in the pancreas and activates cells in the liver. What general type of cell signaling is this? When compound X binds its receptor on a liver cell, some of the amino acids (Y – one letter amino acid code) on the cytoplasmic side of the receptor are phosphorylated. Label what type of receptor this is. This leads to the receptor activating a cytoplasmic protein F which then activates a kinase K which then activates protein Z (diagram what is happening here – how is protein Z activated). Protein Z activation results in several genes being expressed. Label all your parts (don’t forget to label the ligand). Circle the signal transduction pathway and put a box around the cell response.10. A scientist working in a research laboratory has been examining different agonists of serotonin receptor 1B (5-НT1B), а G-protein-coupled re- ceptor. Compound A has a much higher affin- ity for 5-HT1B than compound B. Both com- pounds have a higher affinity for the receptor than serotonin. Which of the following de- scribes the relationship between compound A and compound B when considering the guan- ine-nucleotide exchange activity of 5-HT1B? (A) Km for the exchange reaction with com- pound A is higher than that with com- pound B (B) Km for the exchange reaction with com- pound A is lower than that with compound (C) Km values with compounds A and B2 of 16 Compound Binds to Elicits biological receptor response A Yes Yes B Yes No C No No Refer to the table above. Compound X is the natural ligand that binds to a receptor and stimulates a signal transduction pathway associated with the receptor. Based on the information given in the table, what are the roles of compounds A, B, and C? O A is an antagonist, B is an agonist, and C is a ligand. A is an agonist, B is an antagonist, and C has no role. A is a ligand, B has no role, and C is an antagonist. A is an agonist, B is an antagonist, and C is an agonist. A has no role, B is an agonist, and C is an antagonist.
- 1. What cellular event happens in response to the binding of a growth factor to its respective receptor on the membrane of the growth factor’s target cell? Describe what happens to a tyrosine kinase receptor once it binds the growth factor signal. 2. Describe the three domains of a receptor tyrosine kinase. Explain the structure of the transmembrane domain and the amino acid composition and arrangement of this part of the receptor PLEASE ANSWER BOTH7. Fill in the table below, outlining different aspects of glutamate singlaing in the mammalian brain. A legend of possible entries is provided below the table, specifically for the columns "marker genes", “associated G proteins" and "ionotropic targets" Marker gene Ionotropic receptors Possible associated G proteins Gs Gą G₁/Go Possible marker genes: Choline acetyltransferase Solute carrier family 17 Glutamate decarboxylase Dopamine ß hydroxylase Possible ionotropic targets: Cayl channels Cav2 channels GIRK channels M-type K¹ channels BK channels SK channels Metabotropic Associated receptors G protein mGluR 1,5 mGluR 2-4,6-7- Pre- or post- Ionotropic Neuronal effects synaptic action? target(s) Tryptophan hydroxylase 2 Tyrosine hydroxylase Histidine decarboxylase27) One of the main differences between receptor tyrosine kinase (RTK) signaling and G-protein coupled receptor (GPCR) signaling is that: GPCR signaling involves enzyme cascades, while RTK signaling does not. Only RTK signaling involves kinase activity. Only GPCR signaling involves a GTPase. GPCR signaling is more likely to have a short-term, reversible effect.