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This signaling pathway is antagonized by the action in the phospholipid phosphatases PTEN or SHIP2. Akt phosphorylates various substrates, which includes TSC2 (tuberous sclerosis complex, tuberin), which <a href="http://komiwiki.syktsu.ru/index.php?title=Les_and_reacting_to_its_atmosphere_and_neighboring_agents_accordingly._These">Les and reacting to its environment and neighboring agents accordingly. These</a> ultimately activates theFrontiers in Endocrinology | Neuroendocrine ScienceOctober 2014 | Volume five | Write-up 161 |Bl quez et al.Relationships among T2DM and ADFIGURE 2 | Transduction of signals and biological actions induced by insulin or IGF-1 through their receptor or by means of their hybrid receptors.mammalian target of rapamycin (mTOR) and provides a direct link among insulin si.Ral insulin receptor substrates (IRSs) (69), at the same time as other scaffold proteins (70), which initiate divergent signal transduction pathways (71). Likewise, following the binding of insulin, aggregated IRs are swiftly internalized in to the cell by a procedure that at least in aspect includes coated pits and vesicles (72). It has been suggested that aggregation or internalization could be vital for insulin signaling (73). The internalized IRs can then be degraded or recycled back to the cell membrane. Most insulin responses are mediated by IRS-1 and IRS-2. IRS-1 controls body development and peripheral insulin action, even though IRS2 regulates brain development, physique weight control, glucose homeostasis, and female fertility (74). IRS proteins are composed of an NH2 -terminal pleckstrin homology (PH) domain adjacent to a phosphotyrosine-binding (PTB) domain, and followed by a tail containing several tyrosine and Ser/Thr phosphorylation internet sites (75). The Tyr phosphorylation web-sites coordinate downstream signaling cascades by binding the SH2 domains present in popular effector proteins, like enzymes (the phosphoinositide 3-kinase, PI3K; the phosphatase SHP2; or the tyrosinekinase Fyn) or adapters (SOCS1, SOCS-3, GRB2, and other people) (70, 74). By contrast, the distinct serine phosphorylation of the IRS-1/2 by the c-Jun N-terminal kinase (JNK1) as well as other protein kinases inhibits insulin-stimulated tyrosine phosphorylation, which correlates closely with insulin resistance (76). Likewise, the ubiquitin-mediated degradation of IRS-1/2 also promotes insulin resistance (77). On the other hand, the agonists that enhance IRS-2 expression via cAMP production and CREB activation improve insulin signaling (78). The synapse will be the main locus of cell ell communication in the nervous method. It has been reported that IR was co-expressed with the insulin receptor tyrosine-kinase substrate p58/53 (IRSp53) inside the synapse-rich molecular layer and in the granule cell layer on the cerebellum, at the same time as inside the synapses from the cultured hippocampal neuron, which suggested that these molecules might be part of an insulin-dependent signaling pathway in the post-synaptic apparatus (79). IRSp53, which can be phosphorylated upon stimulation with insulin (80, 81), is often a important factor in cytoskeleton reorganization that mediates neurite outgrowth (82), being also involved in many neurodegenerative disorders (83), simply because IRSp53-deficient animals record cognitive deficits within the contextual fear-conditioning paradigm (84). The association of IRS proteins and PI3K triggers the activation of this enzyme, which phosphorylates an inositol phospholipid within the   plasma membrane, named PI (4,5)P2 , to PI (3,four,5)P3 , which recruits each the Ser/Thr kinase PDK (3-phosphatidylinositoldependent protein kinase) and protein kinase B (PKB or Akt) for the plasma membrane, where Akt is activated by PDK1- and PDK2-mediated phosphorylation (85).

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