Tyrosine Kinase Pathway - Biochemistry
Card 0 of 24
What are some hormones that exert their actions by activating receptor tyrosine activity?
I. Insulin
II. Epidermal growth factor
III. Platelet-derived growth factor
IV. Epinephrine
What are some hormones that exert their actions by activating receptor tyrosine activity?
I. Insulin
II. Epidermal growth factor
III. Platelet-derived growth factor
IV. Epinephrine
Tap to see back →
Insulin, platelet-derived growth factor and, epidermal growth factor all use receptors that have intrinsic tyrosine activity. The hormones bind to the receptor which activates the tyrosine kinase. This in turn induces receptor transautophosphorylation and activation of 
-domain downstream molecules. Epinephrine is a hormone that when bound, activates a G protein-coupled receptor and leads to activation of adenyl cyclase.
Insulin, platelet-derived growth factor and, epidermal growth factor all use receptors that have intrinsic tyrosine activity. The hormones bind to the receptor which activates the tyrosine kinase. This in turn induces receptor transautophosphorylation and activation of
Protein-tyrosine kinase activation can result in the activation of two classical second messengers, inositol triphosphate (IP3) and diacylglycerol (DAG). These molecules are produced as a result of a hydrolysis reaction that is stimulated by protein-tyrosine kinase activation.
What is the enzyme that catalyzes this hydrolysis reaction, and what molecule is cleaved into IP3 and DAG?
Protein-tyrosine kinase activation can result in the activation of two classical second messengers, inositol triphosphate (IP3) and diacylglycerol (DAG). These molecules are produced as a result of a hydrolysis reaction that is stimulated by protein-tyrosine kinase activation.
What is the enzyme that catalyzes this hydrolysis reaction, and what molecule is cleaved into IP3 and DAG?
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In this specific pathway, protein-tyrosine kinase phosphorylation activates phospholipase C (PLC), which then catalyzes the hydrolysis of 
, a membrane phospholipid, into IP3 and DAG. IP3 and DAG then go on to activate second messenger cascades. Protein kinases can be activated by tyrosine kinases, but PLC is the enzyme specifically required for the IP3/DAG cascade.
In this specific pathway, protein-tyrosine kinase phosphorylation activates phospholipase C (PLC), which then catalyzes the hydrolysis of
Receptor tyrosine kinases (RTKs) transduce extracellular signals into intracellular signaling cascades. This is possible because RTKs have an extracellular ligand binding domain to sense ligands outside of the cell, a transmembrane domain that spans the cell membrane, and an intracellular domain that activates pathways within the cell.
Which of the following best describesthe mechanism by which the cytosolic domains of RTKs activate downstream signaling cascades?
Receptor tyrosine kinases (RTKs) transduce extracellular signals into intracellular signaling cascades. This is possible because RTKs have an extracellular ligand binding domain to sense ligands outside of the cell, a transmembrane domain that spans the cell membrane, and an intracellular domain that activates pathways within the cell.
Which of the following best describesthe mechanism by which the cytosolic domains of RTKs activate downstream signaling cascades?
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Ligand binding stabilizes the dimerization of cytosolic domains of RTKs, and the intracellular domains can trans-phosphorylate one another (autophosphorylate) to activate the kinase domains. While there are other mechanisms of activation for RTKs, none of the other answers provide a correct mechanism for this activation.
Ligand binding stabilizes the dimerization of cytosolic domains of RTKs, and the intracellular domains can trans-phosphorylate one another (autophosphorylate) to activate the kinase domains. While there are other mechanisms of activation for RTKs, none of the other answers provide a correct mechanism for this activation.
1. Conformational change brings protein tyrosine kinases close together
2. Receptor dimerization
3. Autophosphorylation activates receptor tyrosine kinases
4. Hormone/ligand binds to extracellular subunits
Which of the following correctly places the steps of the receptor tyrosine kinase in order?
1. Conformational change brings protein tyrosine kinases close together
2. Receptor dimerization
3. Autophosphorylation activates receptor tyrosine kinases
4. Hormone/ligand binds to extracellular subunits
Which of the following correctly places the steps of the receptor tyrosine kinase in order?
Tap to see back →
The first step in all signaling pathways is ligand binding. This causes the extracellular domains to dimerize, inducing a conformational change in transmembrane segments. The cytoplasmic protein tyrosine kinase domains are then then brought close so they can cross-phosphorylate leading to receptor tyrosine kinase activation. Insulin signaling is a primary example of receptor tyrosine kinase signal transduction, and its receptor is already dimerized.
The first step in all signaling pathways is ligand binding. This causes the extracellular domains to dimerize, inducing a conformational change in transmembrane segments. The cytoplasmic protein tyrosine kinase domains are then then brought close so they can cross-phosphorylate leading to receptor tyrosine kinase activation. Insulin signaling is a primary example of receptor tyrosine kinase signal transduction, and its receptor is already dimerized.
Which of the following correctly matches the SH2 (Src Homology 2) and SH3 (Src Homology 3) domains with their residues?
Which of the following correctly matches the SH2 (Src Homology 2) and SH3 (Src Homology 3) domains with their residues?
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SH2 and SH3 domains are Src homology domains that interact with insulin receptor tyrosine kinase substrates. They are especially important in the Ras-activated MAP kinase cascade. SH2 domains, because of their deep positive arginine pockets, tightly bind phosphotyrosine residues but not phosphoserine and phosphothreonine residues.
SH2 and SH3 domains are Src homology domains that interact with insulin receptor tyrosine kinase substrates. They are especially important in the Ras-activated MAP kinase cascade. SH2 domains, because of their deep positive arginine pockets, tightly bind phosphotyrosine residues but not phosphoserine and phosphothreonine residues.
Where do protein kinases most commonly add phosphate groups from ATP for signaling purposes?
Where do protein kinases most commonly add phosphate groups from ATP for signaling purposes?
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The most common point of transfer of an ATP phosphate group is to the hydroxyl of tyrosine, serine, and threonine. Tyrosine and serine/threonine-specific kinases, in particular, help regulate signal transduction. As for the other amino acids, another kinase that sometimes appears is a histidine kinase, mostly in prokaryotes. Sulfur, nitrogen, and carboxyl groups are not typical targets for phosphorylation within proteins for signaling purposes.
The most common point of transfer of an ATP phosphate group is to the hydroxyl of tyrosine, serine, and threonine. Tyrosine and serine/threonine-specific kinases, in particular, help regulate signal transduction. As for the other amino acids, another kinase that sometimes appears is a histidine kinase, mostly in prokaryotes. Sulfur, nitrogen, and carboxyl groups are not typical targets for phosphorylation within proteins for signaling purposes.
What are some hormones that exert their actions by activating receptor tyrosine activity?
I. Insulin
II. Epidermal growth factor
III. Platelet-derived growth factor
IV. Epinephrine
What are some hormones that exert their actions by activating receptor tyrosine activity?
I. Insulin
II. Epidermal growth factor
III. Platelet-derived growth factor
IV. Epinephrine
Tap to see back →
Insulin, platelet-derived growth factor and, epidermal growth factor all use receptors that have intrinsic tyrosine activity. The hormones bind to the receptor which activates the tyrosine kinase. This in turn induces receptor transautophosphorylation and activation of -domain downstream molecules. Epinephrine is a hormone that when bound, activates a G protein-coupled receptor and leads to activation of adenyl cyclase.
Insulin, platelet-derived growth factor and, epidermal growth factor all use receptors that have intrinsic tyrosine activity. The hormones bind to the receptor which activates the tyrosine kinase. This in turn induces receptor transautophosphorylation and activation of
Protein-tyrosine kinase activation can result in the activation of two classical second messengers, inositol triphosphate (IP3) and diacylglycerol (DAG). These molecules are produced as a result of a hydrolysis reaction that is stimulated by protein-tyrosine kinase activation.
What is the enzyme that catalyzes this hydrolysis reaction, and what molecule is cleaved into IP3 and DAG?
Protein-tyrosine kinase activation can result in the activation of two classical second messengers, inositol triphosphate (IP3) and diacylglycerol (DAG). These molecules are produced as a result of a hydrolysis reaction that is stimulated by protein-tyrosine kinase activation.
What is the enzyme that catalyzes this hydrolysis reaction, and what molecule is cleaved into IP3 and DAG?
Tap to see back →
In this specific pathway, protein-tyrosine kinase phosphorylation activates phospholipase C (PLC), which then catalyzes the hydrolysis of , a membrane phospholipid, into IP3 and DAG. IP3 and DAG then go on to activate second messenger cascades. Protein kinases can be activated by tyrosine kinases, but PLC is the enzyme specifically required for the IP3/DAG cascade.
In this specific pathway, protein-tyrosine kinase phosphorylation activates phospholipase C (PLC), which then catalyzes the hydrolysis of
Receptor tyrosine kinases (RTKs) transduce extracellular signals into intracellular signaling cascades. This is possible because RTKs have an extracellular ligand binding domain to sense ligands outside of the cell, a transmembrane domain that spans the cell membrane, and an intracellular domain that activates pathways within the cell.
Which of the following best describesthe mechanism by which the cytosolic domains of RTKs activate downstream signaling cascades?
Receptor tyrosine kinases (RTKs) transduce extracellular signals into intracellular signaling cascades. This is possible because RTKs have an extracellular ligand binding domain to sense ligands outside of the cell, a transmembrane domain that spans the cell membrane, and an intracellular domain that activates pathways within the cell.
Which of the following best describesthe mechanism by which the cytosolic domains of RTKs activate downstream signaling cascades?
Tap to see back →
Ligand binding stabilizes the dimerization of cytosolic domains of RTKs, and the intracellular domains can trans-phosphorylate one another (autophosphorylate) to activate the kinase domains. While there are other mechanisms of activation for RTKs, none of the other answers provide a correct mechanism for this activation.
Ligand binding stabilizes the dimerization of cytosolic domains of RTKs, and the intracellular domains can trans-phosphorylate one another (autophosphorylate) to activate the kinase domains. While there are other mechanisms of activation for RTKs, none of the other answers provide a correct mechanism for this activation.
1. Conformational change brings protein tyrosine kinases close together
2. Receptor dimerization
3. Autophosphorylation activates receptor tyrosine kinases
4. Hormone/ligand binds to extracellular subunits
Which of the following correctly places the steps of the receptor tyrosine kinase in order?
1. Conformational change brings protein tyrosine kinases close together
2. Receptor dimerization
3. Autophosphorylation activates receptor tyrosine kinases
4. Hormone/ligand binds to extracellular subunits
Which of the following correctly places the steps of the receptor tyrosine kinase in order?
Tap to see back →
The first step in all signaling pathways is ligand binding. This causes the extracellular domains to dimerize, inducing a conformational change in transmembrane segments. The cytoplasmic protein tyrosine kinase domains are then then brought close so they can cross-phosphorylate leading to receptor tyrosine kinase activation. Insulin signaling is a primary example of receptor tyrosine kinase signal transduction, and its receptor is already dimerized.
The first step in all signaling pathways is ligand binding. This causes the extracellular domains to dimerize, inducing a conformational change in transmembrane segments. The cytoplasmic protein tyrosine kinase domains are then then brought close so they can cross-phosphorylate leading to receptor tyrosine kinase activation. Insulin signaling is a primary example of receptor tyrosine kinase signal transduction, and its receptor is already dimerized.
Which of the following correctly matches the SH2 (Src Homology 2) and SH3 (Src Homology 3) domains with their residues?
Which of the following correctly matches the SH2 (Src Homology 2) and SH3 (Src Homology 3) domains with their residues?
Tap to see back →
SH2 and SH3 domains are Src homology domains that interact with insulin receptor tyrosine kinase substrates. They are especially important in the Ras-activated MAP kinase cascade. SH2 domains, because of their deep positive arginine pockets, tightly bind phosphotyrosine residues but not phosphoserine and phosphothreonine residues.
SH2 and SH3 domains are Src homology domains that interact with insulin receptor tyrosine kinase substrates. They are especially important in the Ras-activated MAP kinase cascade. SH2 domains, because of their deep positive arginine pockets, tightly bind phosphotyrosine residues but not phosphoserine and phosphothreonine residues.
Where do protein kinases most commonly add phosphate groups from ATP for signaling purposes?
Where do protein kinases most commonly add phosphate groups from ATP for signaling purposes?
Tap to see back →
The most common point of transfer of an ATP phosphate group is to the hydroxyl of tyrosine, serine, and threonine. Tyrosine and serine/threonine-specific kinases, in particular, help regulate signal transduction. As for the other amino acids, another kinase that sometimes appears is a histidine kinase, mostly in prokaryotes. Sulfur, nitrogen, and carboxyl groups are not typical targets for phosphorylation within proteins for signaling purposes.
The most common point of transfer of an ATP phosphate group is to the hydroxyl of tyrosine, serine, and threonine. Tyrosine and serine/threonine-specific kinases, in particular, help regulate signal transduction. As for the other amino acids, another kinase that sometimes appears is a histidine kinase, mostly in prokaryotes. Sulfur, nitrogen, and carboxyl groups are not typical targets for phosphorylation within proteins for signaling purposes.
Protein-tyrosine kinase activation can result in the activation of two classical second messengers, inositol triphosphate (IP3) and diacylglycerol (DAG). These molecules are produced as a result of a hydrolysis reaction that is stimulated by protein-tyrosine kinase activation.
What is the enzyme that catalyzes this hydrolysis reaction, and what molecule is cleaved into IP3 and DAG?
Protein-tyrosine kinase activation can result in the activation of two classical second messengers, inositol triphosphate (IP3) and diacylglycerol (DAG). These molecules are produced as a result of a hydrolysis reaction that is stimulated by protein-tyrosine kinase activation.
What is the enzyme that catalyzes this hydrolysis reaction, and what molecule is cleaved into IP3 and DAG?
Tap to see back →
In this specific pathway, protein-tyrosine kinase phosphorylation activates phospholipase C (PLC), which then catalyzes the hydrolysis of , a membrane phospholipid, into IP3 and DAG. IP3 and DAG then go on to activate second messenger cascades. Protein kinases can be activated by tyrosine kinases, but PLC is the enzyme specifically required for the IP3/DAG cascade.
In this specific pathway, protein-tyrosine kinase phosphorylation activates phospholipase C (PLC), which then catalyzes the hydrolysis of
Receptor tyrosine kinases (RTKs) transduce extracellular signals into intracellular signaling cascades. This is possible because RTKs have an extracellular ligand binding domain to sense ligands outside of the cell, a transmembrane domain that spans the cell membrane, and an intracellular domain that activates pathways within the cell.
Which of the following best describesthe mechanism by which the cytosolic domains of RTKs activate downstream signaling cascades?
Receptor tyrosine kinases (RTKs) transduce extracellular signals into intracellular signaling cascades. This is possible because RTKs have an extracellular ligand binding domain to sense ligands outside of the cell, a transmembrane domain that spans the cell membrane, and an intracellular domain that activates pathways within the cell.
Which of the following best describesthe mechanism by which the cytosolic domains of RTKs activate downstream signaling cascades?
Tap to see back →
Ligand binding stabilizes the dimerization of cytosolic domains of RTKs, and the intracellular domains can trans-phosphorylate one another (autophosphorylate) to activate the kinase domains. While there are other mechanisms of activation for RTKs, none of the other answers provide a correct mechanism for this activation.
Ligand binding stabilizes the dimerization of cytosolic domains of RTKs, and the intracellular domains can trans-phosphorylate one another (autophosphorylate) to activate the kinase domains. While there are other mechanisms of activation for RTKs, none of the other answers provide a correct mechanism for this activation.
1. Conformational change brings protein tyrosine kinases close together
2. Receptor dimerization
3. Autophosphorylation activates receptor tyrosine kinases
4. Hormone/ligand binds to extracellular subunits
Which of the following correctly places the steps of the receptor tyrosine kinase in order?
1. Conformational change brings protein tyrosine kinases close together
2. Receptor dimerization
3. Autophosphorylation activates receptor tyrosine kinases
4. Hormone/ligand binds to extracellular subunits
Which of the following correctly places the steps of the receptor tyrosine kinase in order?
Tap to see back →
The first step in all signaling pathways is ligand binding. This causes the extracellular domains to dimerize, inducing a conformational change in transmembrane segments. The cytoplasmic protein tyrosine kinase domains are then then brought close so they can cross-phosphorylate leading to receptor tyrosine kinase activation. Insulin signaling is a primary example of receptor tyrosine kinase signal transduction, and its receptor is already dimerized.
The first step in all signaling pathways is ligand binding. This causes the extracellular domains to dimerize, inducing a conformational change in transmembrane segments. The cytoplasmic protein tyrosine kinase domains are then then brought close so they can cross-phosphorylate leading to receptor tyrosine kinase activation. Insulin signaling is a primary example of receptor tyrosine kinase signal transduction, and its receptor is already dimerized.
Which of the following correctly matches the SH2 (Src Homology 2) and SH3 (Src Homology 3) domains with their residues?
Which of the following correctly matches the SH2 (Src Homology 2) and SH3 (Src Homology 3) domains with their residues?
Tap to see back →
SH2 and SH3 domains are Src homology domains that interact with insulin receptor tyrosine kinase substrates. They are especially important in the Ras-activated MAP kinase cascade. SH2 domains, because of their deep positive arginine pockets, tightly bind phosphotyrosine residues but not phosphoserine and phosphothreonine residues.
SH2 and SH3 domains are Src homology domains that interact with insulin receptor tyrosine kinase substrates. They are especially important in the Ras-activated MAP kinase cascade. SH2 domains, because of their deep positive arginine pockets, tightly bind phosphotyrosine residues but not phosphoserine and phosphothreonine residues.
Where do protein kinases most commonly add phosphate groups from ATP for signaling purposes?
Where do protein kinases most commonly add phosphate groups from ATP for signaling purposes?
Tap to see back →
The most common point of transfer of an ATP phosphate group is to the hydroxyl of tyrosine, serine, and threonine. Tyrosine and serine/threonine-specific kinases, in particular, help regulate signal transduction. As for the other amino acids, another kinase that sometimes appears is a histidine kinase, mostly in prokaryotes. Sulfur, nitrogen, and carboxyl groups are not typical targets for phosphorylation within proteins for signaling purposes.
The most common point of transfer of an ATP phosphate group is to the hydroxyl of tyrosine, serine, and threonine. Tyrosine and serine/threonine-specific kinases, in particular, help regulate signal transduction. As for the other amino acids, another kinase that sometimes appears is a histidine kinase, mostly in prokaryotes. Sulfur, nitrogen, and carboxyl groups are not typical targets for phosphorylation within proteins for signaling purposes.
What are some hormones that exert their actions by activating receptor tyrosine activity?
I. Insulin
II. Epidermal growth factor
III. Platelet-derived growth factor
IV. Epinephrine
What are some hormones that exert their actions by activating receptor tyrosine activity?
I. Insulin
II. Epidermal growth factor
III. Platelet-derived growth factor
IV. Epinephrine
Tap to see back →
Insulin, platelet-derived growth factor and, epidermal growth factor all use receptors that have intrinsic tyrosine activity. The hormones bind to the receptor which activates the tyrosine kinase. This in turn induces receptor transautophosphorylation and activation of -domain downstream molecules. Epinephrine is a hormone that when bound, activates a G protein-coupled receptor and leads to activation of adenyl cyclase.
Insulin, platelet-derived growth factor and, epidermal growth factor all use receptors that have intrinsic tyrosine activity. The hormones bind to the receptor which activates the tyrosine kinase. This in turn induces receptor transautophosphorylation and activation of
Protein-tyrosine kinase activation can result in the activation of two classical second messengers, inositol triphosphate (IP3) and diacylglycerol (DAG). These molecules are produced as a result of a hydrolysis reaction that is stimulated by protein-tyrosine kinase activation.
What is the enzyme that catalyzes this hydrolysis reaction, and what molecule is cleaved into IP3 and DAG?
Protein-tyrosine kinase activation can result in the activation of two classical second messengers, inositol triphosphate (IP3) and diacylglycerol (DAG). These molecules are produced as a result of a hydrolysis reaction that is stimulated by protein-tyrosine kinase activation.
What is the enzyme that catalyzes this hydrolysis reaction, and what molecule is cleaved into IP3 and DAG?
Tap to see back →
In this specific pathway, protein-tyrosine kinase phosphorylation activates phospholipase C (PLC), which then catalyzes the hydrolysis of , a membrane phospholipid, into IP3 and DAG. IP3 and DAG then go on to activate second messenger cascades. Protein kinases can be activated by tyrosine kinases, but PLC is the enzyme specifically required for the IP3/DAG cascade.
In this specific pathway, protein-tyrosine kinase phosphorylation activates phospholipase C (PLC), which then catalyzes the hydrolysis of
Receptor tyrosine kinases (RTKs) transduce extracellular signals into intracellular signaling cascades. This is possible because RTKs have an extracellular ligand binding domain to sense ligands outside of the cell, a transmembrane domain that spans the cell membrane, and an intracellular domain that activates pathways within the cell.
Which of the following best describesthe mechanism by which the cytosolic domains of RTKs activate downstream signaling cascades?
Receptor tyrosine kinases (RTKs) transduce extracellular signals into intracellular signaling cascades. This is possible because RTKs have an extracellular ligand binding domain to sense ligands outside of the cell, a transmembrane domain that spans the cell membrane, and an intracellular domain that activates pathways within the cell.
Which of the following best describesthe mechanism by which the cytosolic domains of RTKs activate downstream signaling cascades?
Tap to see back →
Ligand binding stabilizes the dimerization of cytosolic domains of RTKs, and the intracellular domains can trans-phosphorylate one another (autophosphorylate) to activate the kinase domains. While there are other mechanisms of activation for RTKs, none of the other answers provide a correct mechanism for this activation.
Ligand binding stabilizes the dimerization of cytosolic domains of RTKs, and the intracellular domains can trans-phosphorylate one another (autophosphorylate) to activate the kinase domains. While there are other mechanisms of activation for RTKs, none of the other answers provide a correct mechanism for this activation.