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Chapter 11: Problem 2

The activation of receptor tyrosine kinases is characterized by (A) dimerization and phosphorylation. (B) dimerization and \(\mathrm{IP}_{3}\) binding. (C) a phosphorylation cascade. (D) GTP hydrolysis.

Short Answer

Expert verified
The correct answer is (A) dimerization and phosphorylation.

Step by step solution

01

Understand Receptor Tyrosine Kinases (RTKs)

Receptor Tyrosine Kinases (RTKs) are a type of cell surface receptor that, when activated, can trigger cellular responses. They play essential roles in various cellular processes such as growth, differentiation, and metabolism.
02

Recognize the Activation Mechanism

The activation of RTKs involves two key steps: dimerization and phosphorylation. Dimerization is when two receptor molecules come together, and phosphorylation is the addition of a phosphate group to specific tyrosine residues in the protein structure.
03

Match Options with RTKs Activation Steps

Based on the recognized activation mechanism: (A) dimerization and phosphorylation - Correct, this matches the activation process. (B) dimerization and \( \text{IP}_3 \) binding - Incorrect, \( \text{IP}_3 \) is more related to calcium signaling. (C) a phosphorylation cascade - Incorrect, this is a subsequent process following the initial activation. (D) GTP hydrolysis - Incorrect, this relates to G-protein-coupled receptors, not RTKs.
04

Select the Correct Answer

From the analysis, the correct description of RTK activation is given by option (A): dimerization and phosphorylation.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Dimerization in Receptor Tyrosine Kinases
Receptor Tyrosine Kinases (RTKs) are essential proteins that help cells communicate with their external environment. When a signal, like a growth factor, binds to the RTK, the first critical step is dimerization. Dimerization means that two RTK molecules pair up, forming a dimer.

This pairing is crucial because it brings the intracellular (inside the cell) parts of the receptors close enough to interact with each other.

Once they are close together, these intracellular parts can then go through further activation steps.

The purpose of dimerization is to set the stage for the next important process known as phosphorylation.
Phosphorylation in Receptor Tyrosine Kinases
Following dimerization, phosphorylation occurs. Phosphorylation is the process where a phosphate group is added to tyrosine residues (specific parts of the protein) inside the cell.

Here's how it works:
  • The close proximity of the intracellular parts of the dimerized RTKs allows one RTK to add phosphate groups to the other.
  • This addition happens at specific locations called tyrosine residues.
  • The phosphates serve as 'activation marks' that change the shape and function of the RTK.

Phosphorylation essentially 'turns on' the RTK, enabling it to send signals inside the cell. This step is vital because it activates the downstream signaling pathways leading to various cellular responses, such as growth and division.
Cell Signaling and RTKs
Once the RTKs are phosphorylated, they can interact with other proteins inside the cell to transmit the signal. This process is known as cell signaling.

In cell signaling, activated RTKs serve as a communication hub:
  • They attract and activate other proteins in the cell, which can further propagate the signal.
  • This causes a series of protein interactions known as a signaling cascade.
  • Eventually, these interactions lead to various cellular responses, such as changes in gene expression or cell behavior.

Cell signaling is essential for the cell to respond to its environment correctly. Through the precise steps of dimerization and phosphorylation, RTKs maintain proper cellular functioning and help the body adapt to different conditions.

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Most popular questions from this chapter

Which observation suggested to Sutherland the involvement of a second messenger in epinephrine's effect on liver cells? (A) Enzymaticactivity was proportional to the amount of calcium added to a cell-free extract. (B) Receptor studies indicated that epinephrine was a ligand. (C) Glycogen breakdown was observed only when epinephrine was administered to intact cells. (D) Glycogen breakdown was observed only when epinephrine and glycogen phosphorylase were mixed.

There are five basic tastes-sour, salty, sweet, bitter, and "umami." Salt is detected when the concentration of salt outside of a taste bud cell is higher than that inside of it, and ion channels allow the passive leakage of \(\mathrm{Na}^{+}\) into the cell. The resulting change in membrane potential (see Concept 7.4) sends the "salty" signal to the brain. Umami is a savory taste generated by glutamate (glutamic acid, found in monosodium glutamate, or MSG), which is used as a flavor enhancer in foods such as taco-flavored tortilla chips. The glutamate receptor is a \(\mathrm{GPCR},\) which, when bound, initiates a signaling pathway that ends with a cellular response, perceived by you as "taste." If you eat a regular potato chip and then rinse your mouth, you will no longer taste salt. But if you eat a flavored tortilla chip and then rinse, the taste persists. (Try it!) Propose a possible explanation for this difference.

Protein phosphorylation is commonly involved with which of the following? (A) ligand binding by receptor tyrosine kinases. (B) activation of G protein-coupled receptors. (C) activation of protein kinase molecules. (D) release of \(\mathrm{Ca}^{2+}\) from the ER lumen.

Which of the following occurs during apoptosis? (A) lysis of the cell (B) direct contact between signaling cells (C) fragmentation of the DNA (D) release of proteases outside the cell

Identify the evolutionary mechanisms that might account for the origin and persistence of cell-to-cell signaling systems in prokaryotes.
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