Swarna Maseneni
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The study investigated the molecular mechanisms of TGF-β-induced activation of TAK1. It found that TGF-β causes lysine-63 linked polyubiquitylation of TAK1, activating it independently of TGF-β receptor kinase activity. The TGF-β type I receptor engages TRAF6, an E3 ubiquitin ligase, to ubiquitylate and activate TAK1 in a kinase-independent manner. This suggests TGF-β activates TAK1 by promoting lysine-63 linked polyubiquitylation through the interaction between its type I receptor and TRAF6.
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abstract
Monocytes and macrophages play an important role in both innate and acquired immunity. Cytokines like interleukin-4 (IL-4) produced by T-cells and mast cells can influence monocyte and macrophage actions. A previous study showed that IL-4 stimulation leads to over 2000-fold up-regulation of the MAO-A enzyme in U937 cells, but not the MAO-B isoform. This study examines transcriptional regulation of MAO-A by IL-4. Electrophoretic mobility shift assays revealed that the transcription factor SP1 binds to probes from the MAO-A promoter region, especially in cells stimulated with IL-4 for 3 days. This suggests SP1 plays a role in upregulating
Tgf β signalling from cell
TGF-β signals from the cell membrane to the nucleus through SMAD proteins. Pathway-restricted SMADs are phosphorylated by cell surface receptors with kinase activity, then oligomerize with Smad4 and translocate to the nucleus to direct transcription in response to TGF-β. Inhibitory SMADs block the activation of pathway-restricted SMADs.
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- They interact with G-protein alpha subunits to trigger downstream signaling cascades involving cAMP and phospholipase C.
- Ligands that bind GPCRs can be agonists, partial agonists, inverse agonists, or antagonists depending on their effects on receptor activation.
- Repeated receptor activation leads to desensitization through phosphorylation by kinases.
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abstract
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- Repeated receptor activation leads to desensitization through phosphorylation by kinases.
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Chapter 2
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Chapter 3
Surveying: Object Principles & Types of Surveying; Site Plans, Plans & Maps; Scales & Unit of different Measurements.
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Swarna Maseneni
- 1. The type I TGF-β receptor engages TRAF6 to activate TAK1 in a receptor kinase independent manner By Sorrentino.A .et al. Nature cell biology, 2008 Presented by Swarna Maseneni
- 4. Elucidate the molecular mechanisms for TGF-β-induced activation of TAK1
- 6. Is nature of ubiquitin-linked chains important for TAK1 activation ?
- 7. In vivo Ubiquitylation Assay
- 8. TGF- β causes lys-63 linked polyubiquitylation of TAK1 activation Importance of T βR1 kinase activity for the ubiquitylation and activation of TAK 1
- 9. T βR1 kinase activity Kinase activity is not required for activation of TAK1 and p38
- 10. TGF- β activates TAK1 by promoting Lys63 linked ubiqutylation Whether T βR1 interacts with TRAF6?
- 13. Consensus binding motifs TGF- β induced TAk1 activation which is correlated with Lys63 linked polyubiquitylaion of TAK1 and with the association of TRAF6 to ALK5
- 14. Biological significance of TRAF6 E3 activity on TGF- β induced ubiquitylation of TAK1