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Multiple Choice
Dephosphorylation and which of the following are the two basic mechanisms that can inactivate receptor tyrosine kinases?
A
Allosteric activation
B
Increased ligand binding
C
Receptor internalization
D
Covalent modification by acetylation
Verified step by step guidance
1
Step 1: Understand the role of receptor tyrosine kinases (RTKs). RTKs are enzymes that play a critical role in cell signaling by phosphorylating tyrosine residues on target proteins. Their activation is typically initiated by ligand binding, leading to downstream signaling cascades.
Step 2: Recognize the mechanisms of RTK inactivation. Dephosphorylation is one mechanism, where phosphate groups are removed from tyrosine residues, effectively halting the signaling process. The second mechanism involves receptor internalization, where the receptor is removed from the cell surface and transported into the cell, preventing further interaction with ligands.
Step 3: Eliminate incorrect options. Allosteric activation refers to the enhancement of enzyme activity, which is the opposite of inactivation. Increased ligand binding would also enhance RTK activity rather than inactivate it. Covalent modification by acetylation is not a common mechanism for RTK inactivation.
Step 4: Focus on receptor internalization. This process involves the receptor being endocytosed into the cell, often leading to degradation or recycling, which effectively stops its signaling activity.
Step 5: Conclude that the two basic mechanisms for RTK inactivation are dephosphorylation and receptor internalization, as these directly halt the signaling pathways initiated by RTKs.