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Questions and Answers
What is the primary effect of TGFβ signaling on cell proliferation?
What is the primary effect of TGFβ signaling on cell proliferation?
Which cellular component is commonly mutated in pancreatic cancers, affecting TGFβ signaling?
Which cellular component is commonly mutated in pancreatic cancers, affecting TGFβ signaling?
What is the role of JAKs in cytokine receptor signaling?
What is the role of JAKs in cytokine receptor signaling?
Which of the following cytokines is specifically responsible for T cell and NK cell proliferation?
Which of the following cytokines is specifically responsible for T cell and NK cell proliferation?
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In terms of cytokine receptor structure, how are they characterized?
In terms of cytokine receptor structure, how are they characterized?
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What is the function of the SH2 and PTB domains in the context of receptor tail phosphorylation?
What is the function of the SH2 and PTB domains in the context of receptor tail phosphorylation?
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How do Receptor Tyrosine Kinases (RTKs) differ from cytokine receptors?
How do Receptor Tyrosine Kinases (RTKs) differ from cytokine receptors?
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What effect does the loss of TGFβ signaling have on cell behavior?
What effect does the loss of TGFβ signaling have on cell behavior?
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What is the primary function of SHP1 in relation to JAK?
What is the primary function of SHP1 in relation to JAK?
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Which mechanism does SOCS use to regulate long-term signaling in cytokine receptors?
Which mechanism does SOCS use to regulate long-term signaling in cytokine receptors?
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What is a characteristic feature of Receptor Tyrosine Kinases (RTKs)?
What is a characteristic feature of Receptor Tyrosine Kinases (RTKs)?
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Which protein is known for activating Ras in the RTK signaling pathway?
Which protein is known for activating Ras in the RTK signaling pathway?
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What is the role of scaffold proteins in signaling pathways?
What is the role of scaffold proteins in signaling pathways?
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How does active Ras affect the MAP kinase pathway?
How does active Ras affect the MAP kinase pathway?
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What is the main outcome of ligand binding to an insulin receptor?
What is the main outcome of ligand binding to an insulin receptor?
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What mechanism is NOT used by SOCS to exert its regulatory effects?
What mechanism is NOT used by SOCS to exert its regulatory effects?
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Which of the following proteins is not part of the MAPK pathway?
Which of the following proteins is not part of the MAPK pathway?
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What type of molecules do cytokines primarily bind to?
What type of molecules do cytokines primarily bind to?
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What is the function of I-Smads in TGFβ signaling?
What is the function of I-Smads in TGFβ signaling?
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Which type of receptor is TGFβ-RI classified as?
Which type of receptor is TGFβ-RI classified as?
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How does the binding of TGFβ to TGFβ-RII affect TGFβ-RI?
How does the binding of TGFβ to TGFβ-RII affect TGFβ-RI?
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What structural feature is masked in R-Smads when they are inactive?
What structural feature is masked in R-Smads when they are inactive?
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What effect does the complex formed between SnoN or Ski and Smads have on TGFβ signaling?
What effect does the complex formed between SnoN or Ski and Smads have on TGFβ signaling?
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What role does TGFβ play in cellular processes?
What role does TGFβ play in cellular processes?
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Which of the following statements about TGFβ isoforms is correct?
Which of the following statements about TGFβ isoforms is correct?
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What type of protein forms the latent TGFβ complex in the extracellular matrix?
What type of protein forms the latent TGFβ complex in the extracellular matrix?
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The phosphorylation mechanism of R-Smads involves which of the following?
The phosphorylation mechanism of R-Smads involves which of the following?
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How does the mature form of TGFβ become active?
How does the mature form of TGFβ become active?
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What initial cytoplasmic event occurs upon TGFβ binding to its receptors?
What initial cytoplasmic event occurs upon TGFβ binding to its receptors?
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Which statement best describes the interaction of the TGFβ signaling pathway during early development?
Which statement best describes the interaction of the TGFβ signaling pathway during early development?
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Which of the following correctly describes the TGFβ receptors?
Which of the following correctly describes the TGFβ receptors?
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Loss of TGFβ signaling can lead to abnormal cell proliferation and malignancy.
Loss of TGFβ signaling can lead to abnormal cell proliferation and malignancy.
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The absence of Smad 4 protein in pancreatic cancers enhances the activity of proteins that inhibit cell proliferation.
The absence of Smad 4 protein in pancreatic cancers enhances the activity of proteins that inhibit cell proliferation.
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Cytokines can operate exclusively in an autocrine manner, meaning they only affect the cells that secrete them.
Cytokines can operate exclusively in an autocrine manner, meaning they only affect the cells that secrete them.
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Receptor Tyrosine Kinases (RTKs) contain the tyrosine kinase enzyme as an intrinsic part of their polypeptide chain.
Receptor Tyrosine Kinases (RTKs) contain the tyrosine kinase enzyme as an intrinsic part of their polypeptide chain.
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Cytokine receptors are composed of separate polypeptides that include the receptor and kinase proteins.
Cytokine receptors are composed of separate polypeptides that include the receptor and kinase proteins.
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Interleukin-2 stimulates the proliferation of B cells and T cells.
Interleukin-2 stimulates the proliferation of B cells and T cells.
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Cytokine signaling involves the phosphorylation of receptor tails, which recruits cytosolic proteins to initiate intracellular signaling.
Cytokine signaling involves the phosphorylation of receptor tails, which recruits cytosolic proteins to initiate intracellular signaling.
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JAKs are not involved in the signaling mechanism of cytokine receptors.
JAKs are not involved in the signaling mechanism of cytokine receptors.
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TGFβ signals can induce bone formation and growth.
TGFβ signals can induce bone formation and growth.
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TGFβ-RIII has kinase activity and can directly activate R-Smads.
TGFβ-RIII has kinase activity and can directly activate R-Smads.
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Smads are transcription factors that play a role in the TGFβ signaling pathway.
Smads are transcription factors that play a role in the TGFβ signaling pathway.
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The latent TGFβ complex consists solely of the mature domain.
The latent TGFβ complex consists solely of the mature domain.
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I-Smads such as Smad7 enhance the phosphorylation of R-Smads.
I-Smads such as Smad7 enhance the phosphorylation of R-Smads.
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Phosphorylated Smad3 can bind to Co-Smads and form a complex that translocates to the nucleus.
Phosphorylated Smad3 can bind to Co-Smads and form a complex that translocates to the nucleus.
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TGFβ signaling generally promotes cell proliferation in mammalian cells.
TGFβ signaling generally promotes cell proliferation in mammalian cells.
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SnoN and Ski are oncoproteins that can enhance TGFβ-mediated transcriptional activation.
SnoN and Ski are oncoproteins that can enhance TGFβ-mediated transcriptional activation.
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TGFβ binds to TGFβ-RII or TGFβ-RI during signaling, where RI is the primary binding receptor on the cell surface.
TGFβ binds to TGFβ-RII or TGFβ-RI during signaling, where RI is the primary binding receptor on the cell surface.
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The NLS (Nuclear Localization Sequence) in R-Smads is exposed when they are unphosphorylated.
The NLS (Nuclear Localization Sequence) in R-Smads is exposed when they are unphosphorylated.
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R-Smads are inactive when they are unphosphorylated due to their associated domains.
R-Smads are inactive when they are unphosphorylated due to their associated domains.
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Integrins play a significant role in the release of active TGFβ by interacting with latent TGFβ-binding protein.
Integrins play a significant role in the release of active TGFβ by interacting with latent TGFβ-binding protein.
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TGFβ signaling involves both direct phosphorylation of proteins and complex formation between different receptor types.
TGFβ signaling involves both direct phosphorylation of proteins and complex formation between different receptor types.
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JAK is dephosphorylated by SHP1, which leads to further activation of cytokine receptors.
JAK is dephosphorylated by SHP1, which leads to further activation of cytokine receptors.
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SOCS proteins terminate long-term signaling by degrading associated target proteins.
SOCS proteins terminate long-term signaling by degrading associated target proteins.
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RTKs have intrinsic serine kinase activity, which differentiates them from cytokine receptors.
RTKs have intrinsic serine kinase activity, which differentiates them from cytokine receptors.
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Active Ras is bound to GDP and is responsible for activating the MAP kinase pathway.
Active Ras is bound to GDP and is responsible for activating the MAP kinase pathway.
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Scaffold proteins prevent accidental phosphorylation of substrates in various signaling pathways.
Scaffold proteins prevent accidental phosphorylation of substrates in various signaling pathways.
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Phosphotyrosine residues on the receptor tails of RTKs help recruit adapter proteins.
Phosphotyrosine residues on the receptor tails of RTKs help recruit adapter proteins.
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Ligand binding to cytokine receptors does not lead to phosphorylation of tyrosine residues.
Ligand binding to cytokine receptors does not lead to phosphorylation of tyrosine residues.
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Ras proteins are directly linked to cell surface receptors in signaling cascades.
Ras proteins are directly linked to cell surface receptors in signaling cascades.
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The MAPK pathway involves the activation of Raf, which is a serine/threonine kinase.
The MAPK pathway involves the activation of Raf, which is a serine/threonine kinase.
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JAK is activated by ligand binding to its corresponding cytokine receptor.
JAK is activated by ligand binding to its corresponding cytokine receptor.
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Study Notes
Overview of Cell-Surface Receptors
- Major classes of cell-surface receptors transduce signals via various pathways, many of which are complex.
- Many genes are regulated by multiple transcription factors, each activated by one or more extracellular signals.
- Significant cross-talk exists between signaling pathways, especially during early development.
Transforming Growth Factor β Signaling
- TGFβ superfamily signals are involved in various developmental processes, including induction of transformed phenotype, bone formation, mesoderm formation, and cell-adhesion molecule expression.
- TGFβ generally has anti-proliferative effects on mammalian cells, inhibiting cell proliferation.
- TGFβ signaling pathway is relatively simple:
- TGFβ binds to TGFβ receptors, directly phosphorylating and activating transcription factors.
Human TGFβ Signals
- Human isoforms (TGFβ1-3) are encoded by unique genes, tissue-specific, and developmentally regulated.
- TGFβ is synthesized as a precursor, cleaved after secretion, with the pro-domain remaining non-covalently associated with the mature domain.
- The latent TGFβ complex in the extracellular matrix includes the pro-domain, mature domain, and latent TGFβ-binding protein (LTBP).
- Mature TGFβ is released as an active homo- or hetero-dimer after proteolysis or LTBP conformational change, triggered by integrin or matrix protein binding to LTBP.
TGFβ Receptors
- Three receptor types: TGFβ RI, RII, and RIII.
- TGFβ-RIII binds and concentrates TGFβ, lacking kinase activity.
- TGFβ-RII is a dimeric transmembrane protein with cytosolic Serine/Threonine kinase activity for TGFβ-RI.
- TGFβ-RI is a dimeric transmembrane protein lacking extracellular TGFβ binding but possesses cytosolic Serine/Threonine kinase activity for R-Smads.
- TGFβ binding induces complex formation with two copies of TGFβ-RII and TGFβ-RI.
- TGFβ-RII phosphorylates and activates TGFβ-RI kinase activity.
- Activated TGFβ-RI directly phosphorylates and activates transcription factors called Smads.
Smads – Transcription Factors
- Three types of Smads:
- R-Smads (Receptor-regulated Smads): Smad2 and Smad3.
- Co-Smads: Smad4.
- I-Smads (Inhibitory or antagonistic Smads): Smad7.
- Structure of R-Smads:
- Inactive when unphosphorylated, with MH1 and MH2 domains associated, NLS masked, and inability to bind Co-Smad or DNA.
- TGFβ-RI phosphorylates three serine residues near the C-terminus, separating the MH1 and MH2 domains, exposing NLS.
TGFβ Signaling Pathway
- TGFβ binds to TGFβ-RIII or TGFβ-RII, with RIII presenting TGFβ to RII.
- Ligand-bound RII recruits and phosphorylates RI, activating it.
- Activated TGFβ-RI phosphorylates Smad3, exposing NLS.
- Two phosphorylated Smad3 interact with Smad4 and importin in the cytosol, forming a complex.
- The complex translocates to the nucleus, with Ran-GTP dissociating importin.
- The Smad complex associates with other transcription factors, forming an activation complex, triggering transcription (often growth-inhibitory genes).
- Dephosphorylation of Smads in the nucleus leads to their translocation to the cytoplasm.
I-Smads Regulate Smad Signaling
- I-Smads (Smad7) block TGFβ-RI’s ability to phosphorylate R-Smads, inhibiting intracellular signaling.
Oncoproteins Regulate Smad Signaling
- SnoN and Ski (Sloan-Kettering Cancer Institute) oncoproteins bind to Smad2/Smad4 or Smad3/Smad4 complexes after TGFβ stimulation.
- These complexes can still bind to DNA control regions but block transcription activation by DNA-bound Smad complexes.
- This blockage prevents the transcription of growth-inhibitory genes normally activated by the TGFβ pathway.
Cytokines & the JAK/STAT Pathway
- Ligand binding to cytokine receptors activates JAK, which phosphorylates tyrosine residues on the receptor tail.
- SH2 domain-containing STAT (Signal Transducers and Activators of Transcription) proteins are recruited.
- JAK phosphorylates STATs, causing them to dissociate from the receptor, dimerize, and expose NLS.
- The STAT dimer translocates to the nucleus, binds to enhancer sequences, and activates transcription of target genes.
Short Term Regulation of Cytokine Receptors
- Dephosphorylation of tyrosines on JAK by phosphatase SHP1 inactivates JAK.
- SHP1 binds to a phosphotyrosine on the receptor tail, removing phosphate from JAK, preventing further activation, occurring within minutes.
Long Term Regulation of Cytokine Receptors
- SOCS (suppressor of cytokine signaling) proteins inhibit or terminate long-term signaling.
- SOCS protein expression is induced by STAT proteins in Epo-stimulated cells.
- Mechanisms:
- Signal blocking: SOCS binds to phosphotyrosine residues on EpoR or JAK2.
- Protein degradation: SOCS target proteins for ubiquitin-proteasome degradation.
Receptor Tyrosine Kinases (RTKs)
- RTKs are similar to cytokine receptors with an intrinsic cytosolic tyrosine kinase activity.
- Ligands include growth factors and insulin, such as NGF, PDGF, FGF, and EGF.
- Ligand binding causes receptor dimerization, kinase activation, and tyrosine phosphorylation on receptor tails.
Ligand Binding to RTK & Ras Activation
- Phosphorylated tyrosines on RTK tails recruit adapter proteins with SH2 and PTB domains, coupling activated RTKs to signaling pathways, such as Ras activation.
- Ras is a monomeric, GTP-binding switch protein, inactive when bound to GDP and active when bound to GTP.
- Ras is anchored to the plasma membrane by a hydrophobic anchor.
Ligand Binding to RTK & Ras Activation
- Activated RTK recruits SH2 domain-containing GRB2.
- GRB2 recruits SOS protein (GEF activity).
- SOS replaces GDP with GTP on Ras, activating it.
Active Ras Turns on MAPKinase Pathway
- Ras/MAP kinase pathway:
- Ras activates Raf (S/T kinase).
- Raf activates MEK (kinase).
- MEK activates MAPK (kinase).
- MAPK translocates to the nucleus, inducing transcription.
- MAPK regulates the activity of many transcription factors.
Ras/MAPK Pathway
- The pathway involves a cascade of kinases, ultimately activating transcription factors.
Mutations to Components of MAPK Pathway Linked to Cancer
- Mutations in the MAPK pathway can lead to uncontrolled cell growth and cancer.
Role of Scaffold Proteins
- Scaffold proteins assemble upstream components of MAPK cascades into pathway-specific complexes, stabilizing them.
- They associate different kinases within a signaling pathway, preventing accidental phosphorylation of other substrates.
- This allows kinases of one pathway to interact with each other but not with kinases in other pathways.
Insulin & Protein Kinase B (PKB)
- Insulin binds to the insulin receptor (RTK), activating PKB and other signaling pathways.
Cancer & Loss of TGFβ Signals
- TGFβ signaling typically inhibits cell proliferation.
- Loss of components in the signaling pathway contributes to abnormal cell proliferation and malignancy.
- Many cancers involve mutations in the TGFβ signaling pathway, making them resistant to growth inhibition by TGFβ.
OTHER RECEPTORS
- Two categories of receptors activate tyrosine kinases:
- Receptor Tyrosine Kinases (RTKs), where the tyrosine kinase is an intrinsic part of the receptor.
- Cytokine receptors, where the receptor and kinase are separate polypeptides.
EPO, TPO, G-CSF
- Erythropoietin (EPO) stimulates red blood cell production.
- Thrombopoietin (TPO) promotes platelet formation.
- Granulocyte colony-stimulating factor (G-CSF) regulates white blood cell production.
Cytokine Signaling
- Cytokines are small secreted proteins that regulate cell growth and differentiation.
- They can act in an autocrine, paracrine, and endocrine manner.
- Cytokine binding to their receptors activates intracellular signaling cascades, leading to responses like:
- Increased or decreased expression of membrane proteins.
- Cell proliferation.
- Secretion of effector molecules.
Cytokine Signaling
- Cytokine receptors are two monomeric transmembrane proteins, each associated with JAK (Janus Kinases), a separate cytosolic protein tyrosine kinase.
- Cytokine binding causes:
- Receptor dimerization.
- Tyrosine phosphorylation and activation of JAKs.
- Tyrosine phosphorylation of receptor tails.
Recruitment of Cytosolic Proteins to Receptor Tails
- Phosphorylated tyrosines on the activated receptor tail recruit proteins with SH2 or PTB domains.
- JAK phosphorylates these recruited proteins, enhancing their activity.
- These proteins then signal and activate transcription.
TGFβ Signaling Pathway
- Transforming growth factor β (TGFβ) is a large class of signaling molecules involved in diverse developmental processes.
- TGFβ signaling generally inhibits cell proliferation in many mammalian cells.
- TGFβ isoforms are encoded by unique genes, display tissue specificity, and are developmentally regulated.
- TGFβ is synthesized as a larger precursor that gets cleaved after secretion.
- Mature TGFβ is released as an active homo- or hetero-dimer after proteolysis or conformational changes in the Latent TGFβ-binding protein (LTBP).
- TGFβ receptors include TGFβ RI, RII, and RIII.
- TGFβ-RIII is the most abundant receptor, concentrating TGFβ on the cell surface but lacking kinase activity.
- TGFβ-RII binds TGFβ and possesses cytosolic Serine/Threonine kinase activity to activate TGFβ-RI.
- TGFβ-RI does not bind TGFβ directly but possesses cytosolic Serine/Threonine kinase activity for activating Smads.
- TGFβ binding initiates complex formation with two copies of TGFβ-RII and TGFβ-RI.
- TGFβ-RII phosphorylates and activates TGFβ-RI kinase activity.
- Activated TGFβ-RI directly phosphorylates and activates Smads, the transcription factors mediating TGFβ signaling.
Smads and Transcriptional Regulation
- Smads are a family of transcription factors involved in TGFβ signaling.
- Three types of Smads: R-Smads, Co-Smads, and I-Smads.
- R-Smads (Smad2, Smad3): Receptor-regulated Smads, activated by TGFβ-RI phosphorylation.
- Co-Smads (Smad4): Required for complex formation with R-Smads to translocate to the nucleus.
- I-Smads (Smad7): Inhibitory or antagonistic Smads, blocking the phosphorylation of R-Smads by TGFβ-RI.
- R-Smads are inactive when unphosphorylated, with their MH1 and MH2 domains associated, the NLS masked, preventing Co-Smad and DNA binding.
- Phosphorylation of three serine residues near the C-terminus of R-Smads separates the MH1 and MH2 domains, exposing the NLS.
- Phosphorylated R-Smads interact with Co-Smads and importin, forming a complex that translocates to the nucleus.
TGFβ Signaling Pathway
- TGFβ binds to the TGFβ-RIII, presenting it to RII, or binds directly to RII.
- Ligand-bound RII recruits and phosphorylates RI, activating it.
- Activated TGFβ-RI phosphorylates Smad3, exposing its NLS.
- Two phosphorylated Smad3 molecules interact with Smad4 and importin in the cytosol, forming a large complex.
- The Smad complex translocates to the nucleus, with Ran-GTP dissociating importin.
- The Smad complex associates with other transcription factors, forming an activation complex.
- This activation complex binds to DNA regulatory regions, initiating the transcription of specific target genes, often growth-inhibitory genes.
- Dephosphorylation of Smads in the nucleus results in their translocation to the cytoplasm.
Regulation of Smad Signaling
- I-Smads (Smad7) block the ability of TGFβ-RI to phosphorylate R-Smads, inhibiting intracellular signaling.
- Oncoproteins SnoN and Ski bind to Smad2/Smad4 or Smad3/Smad4 complexes after TGFβ stimulation.
- These complexes can still bind to DNA control regions but block transcription activation by DNA-bound Smad complexes.
- This action inhibits the transcription of growth-inhibitory genes normally induced by the TGFβ pathway.
Cancer and Loss of TGFβ Signaling
- TGFβ signaling generally inhibits cell proliferation.
- Mutations in TGFβ signaling pathways can disrupt this inhibition, leading to abnormal cell proliferation and malignancy.
- Many cancers involve mutations in TGFβ receptors or Smad proteins, rendering them resistant to growth inhibition by TGFβ.
- In many human pancreatic cancers, deletions in the Smad4 gene result in non-functional or absent Smad4 protein, leading to uncontrolled cell proliferation.
Receptor Tyrosine Kinases (RTKs)
- RTKs are similar to cytokine receptors but possess intrinsic tyrosine kinase activity in their cytosolic domains.
- Examples of RTK ligands include growth factors (NGF, PDGF, FGF, EGF) and Insulin.
- Ligand binding causes receptor dimerization, activates the kinase, and leads to tyrosine phosphorylation on the receptor tails.
Ligand Binding to RTKs and Ras Activation
- Phosphorylated tyrosines on RTK tails recruit adapter proteins with SH2 and PTB domains.
- These adapter proteins couple activated RTKs to downstream signaling components, including Ras activation.
- Ras is a monomeric, GTP-binding switch protein, inactive with bound GDP and active with bound GTP.
- Ras is not directly linked to cell-surface receptors but is anchored to the plasma membrane by a hydrophobic anchor.
- Activated RTK recruits the SH2 domain-containing protein GRB2, which recruits SOS protein with GEF activity.
- SOS facilitates the exchange of GDP for GTP on Ras, activating it.
Active Ras and the MAP Kinase Pathway
- Active Ras binds to and activates Raf (a Ser/Thr kinase).
- Raf activates MEK (another kinase), which activates MAPK (mitogen-activated protein kinase).
- MAPK translocates to the nucleus, inducing transcription.
- MAPK regulates the activity of numerous transcription factors.
Mutations in the MAP Kinase Pathway and Cancer
- Mutations to components of the MAP Kinase pathway can lead to uncontrolled cell proliferation and cancer.
Scaffold Proteins in Signaling Pathways
- Upstream components of MAPK cascades assemble into large, pathway-specific complexes stabilized by scaffold proteins.
- Scaffold proteins associate different kinases within a signaling pathway, preventing accidental phosphorylation of inappropriate substrates.
- This allows kinases from one pathway to interact with each other while preventing cross-talk with kinases in other pathways.
Insulin and Protein Kinase B (PKB)
- Insulin binds to the insulin receptor (RTK), activating it.
- The activated insulin receptor can:
- Phosphorylate effector proteins.
- Initiate a signaling cascade involving PI3 kinase, PDK1, and PKB.
- PKB phosphorylates downstream targets, regulating glucose uptake, glycogen synthesis, and other metabolic processes.
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Explore the major classes of cell-surface receptors and their roles in signal transduction pathways. This quiz covers the mechanisms of TGFβ signaling and its importance in developmental processes and gene regulation. Test your understanding of how these receptors influence cellular activities and interactions.
