In which condition is Protein A kinase activated? #1B-arrestin is always active. #2 Lack of kinase domain in BARK #3 ß1-adrenergic membrane receptor lacking it's ligand-binding domain

Human Anatomy & Physiology (11th Edition)
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Chapter1: The Human Body: An Orientation
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In which condition is Protein A kinase activated? #1B-arrestin is always active. #2 Lack of kinase domain in BARK #3 ß1-adrenergic membrane receptor lacking it's ligand-binding domain
This diagram illustrates the biochemical pathway of adrenaline signaling through the β1-adrenergic receptor.

1. **Adrenaline**: Adrenaline molecules are depicted outside the cell, indicating their role as extracellular signaling molecules.

2. **β1-adrenergic receptor**: This is shown embedded within the plasma membrane. When adrenaline binds to this receptor, it activates the pathway.

3. **G protein**: Upon activation by the receptor, the G protein exchanges GDP for GTP. This activation is indicated by an arrow pointing from GDP to GTP.

4. **Adenylyl cyclase**: The activated G protein stimulates adenylyl cyclase, an enzyme also located in the plasma membrane. This is represented by arrows showing the transition from G protein to adenylyl cyclase.

5. **cAMP and ATP**: Adenylyl cyclase converts ATP to cyclic AMP (cAMP), a secondary messenger inside the cell.

6. **Protein Kinase A (PKA)**: cAMP activates Protein Kinase A, shown within the cell. Activation is marked by an arrow from cAMP to Protein Kinase A.

7. **Cellular Responses**:
   - **Increased heart rate**: Protein Kinase A activation leads to increased heart rate, denoted by an arrow.
   - **Increased fat breakdown**: Parallelly, there is also increased breakdown of fat, shown by another arrow emanating from Protein Kinase A.

8. **Repression Pathway**:
   - **BARK (Beta-Adrenergic Receptor Kinase)**: BARK can phosphorylate and inhibit the receptor.
   - **β-arrestin**: This molecule binds to phosphorylated receptors, blocking further G protein activation, represented by bars indicating repression.

The diagram includes a note stating that arrows represent activation, while bars represent repression. This diagram provides a simplified overview of the signaling events triggered by adrenaline binding to the β1-adrenergic receptor and its various cellular effects.
Transcribed Image Text:This diagram illustrates the biochemical pathway of adrenaline signaling through the β1-adrenergic receptor. 1. **Adrenaline**: Adrenaline molecules are depicted outside the cell, indicating their role as extracellular signaling molecules. 2. **β1-adrenergic receptor**: This is shown embedded within the plasma membrane. When adrenaline binds to this receptor, it activates the pathway. 3. **G protein**: Upon activation by the receptor, the G protein exchanges GDP for GTP. This activation is indicated by an arrow pointing from GDP to GTP. 4. **Adenylyl cyclase**: The activated G protein stimulates adenylyl cyclase, an enzyme also located in the plasma membrane. This is represented by arrows showing the transition from G protein to adenylyl cyclase. 5. **cAMP and ATP**: Adenylyl cyclase converts ATP to cyclic AMP (cAMP), a secondary messenger inside the cell. 6. **Protein Kinase A (PKA)**: cAMP activates Protein Kinase A, shown within the cell. Activation is marked by an arrow from cAMP to Protein Kinase A. 7. **Cellular Responses**: - **Increased heart rate**: Protein Kinase A activation leads to increased heart rate, denoted by an arrow. - **Increased fat breakdown**: Parallelly, there is also increased breakdown of fat, shown by another arrow emanating from Protein Kinase A. 8. **Repression Pathway**: - **BARK (Beta-Adrenergic Receptor Kinase)**: BARK can phosphorylate and inhibit the receptor. - **β-arrestin**: This molecule binds to phosphorylated receptors, blocking further G protein activation, represented by bars indicating repression. The diagram includes a note stating that arrows represent activation, while bars represent repression. This diagram provides a simplified overview of the signaling events triggered by adrenaline binding to the β1-adrenergic receptor and its various cellular effects.
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