Upstream and downstream (transduction) explained

The upstream signaling pathway is triggered by the binding of a signaling molecule, a ligand, to a receiving molecule, a receptor. Receptors and ligands exist in many different forms, and only recognize/bond to particular molecules. Upstream extracellular signaling transduce a variety of intracellular cascades.[1]

Receptors and ligands are common upstream signaling molecules that dictate the downstream elements of the signal pathway. A plethora of different factors affect which ligands bind to which receptors and the downstream cellular response that they initiate.

TGF-β

The extracellular type II and type I kinase receptors binding to the TGF-β ligands. Transforming growth factor-β (TGF-β) is a superfamily of cytokines that play a significant upstream role in regulating of morphogenesis, homeostasis, cell proliferation, and differentiation.[2] The significance of TGF-β is apparent with the human diseases that occur when TGF-β processes are disrupted, such as cancer, and skeletal, intestinal and cardiovascular diseases.[3] [4] TGF-β is pleiotropic and multifunctional, meaning they are able to act on a wide variety of cell types.[5]

Mechanism

The effects of transforming growth factor-β (TGF-β) are determined by cellular context. There are three kinds of contextual factors that determine the shape the TGF-β response: the signal transduction components, the transcriptional cofactors and the epigenetic state of the cell. The different ligands and receptors of TGF-β are significant as well in the composition signal transduction pathway.[2]

Upstream pathway

The type II receptors phosphorylate the type I receptors; the type I receptors are then enabled to phosphorylate cytoplasmic R-Smads, which then act as transcriptional regulators.[6] Signaling is initiated by the binding of TGF-β to its serine/threonine receptors. The serene/threonine receptors are the type II and type I receptors on the cell membrane. Binding of a TGF-β members induces assembly of a heterotetrameric complex of two type I and two type II receptors at the plasma membrane.[6] Individual members of the TGF-β family bind to a certain set of characteristic combination of these type I and type II receptors.[7] The type I receptors can be divided into two groups, which depends on the cytoplasmic R-Smads that they bind and phosphorylate. The first group of type I receptors (Alk1/2/3/6) bind and activate the R-Smads, Smad1/5/8. The second group of type I reactors (Alk4/5/7) act on the R-Smads, Smad2/3. The phosphorylated R-Smads then form complexes and the signals are funneled through two regulatory Smad (R-Smad) channels (Smad1/5/8 or Smad2/3). After the ligand-receptor complexes phosphorylate the cytoplasmic R-Smads, the signal is then sent through Smad 1/5/8 or Smad 2/3. This leads to the downstream signal cascade and cellular gene targeting.[6]

Downstream pathway

TGF-β regulates multiple downstream processes and cellular functions. The pathway is highly variable based on cellular context. TGF-β downstream signaling cascade includes regulation of cell growth, cell proliferation, cell differentiation, and apoptosis.[8]

See also

Notes and References

  1. Miller DS, Schmierer B, Hill CS . TGF-β family ligands exhibit distinct signalling dynamics that are driven by receptor localisation . Journal of Cell Science . 132 . 14 . July 2019 . jcs234039 . 31217285 . 6679586 . 10.1242/jcs.234039 .
  2. Massagué J . TGFβ signalling in context . Nature Reviews. Molecular Cell Biology . 13 . 10 . 616–30 . October 2012 . 22992590 . 4027049 . 10.1038/nrm3434 .
  3. Kashima R, Hata A . The role of TGF-β superfamily signaling in neurological disorders . Acta Biochimica et Biophysica Sinica . 50 . 1 . 106–120 . January 2018 . 29190314 . 5846707 . 10.1093/abbs/gmx124 .
  4. Huang T, Schor SL, Hinck AP . Biological activity differences between TGF-β1 and TGF-β3 correlate with differences in the rigidity and arrangement of their component monomers . Biochemistry . 53 . 36 . 5737–49 . September 2014 . 25153513 . 4165442 . 10.1021/bi500647d .
  5. Letterio JJ, Roberts AB . Regulation of immune responses by TGF-beta . Annual Review of Immunology . 16 . 1 . 137–61 . 1998-04-01 . 9597127 . 10.1146/annurev.immunol.16.1.137 .
  6. Vilar JM, Jansen R, Sander C . Signal processing in the TGF-beta superfamily ligand-receptor network . PLOS Computational Biology . 2 . 1 . e3 . January 2006 . 16446785 . 1356091 . 10.1371/journal.pcbi.0020003 . q-bio/0509016 . 2006PLSCB...2....3V . free .
  7. Heldin CH, Moustakas A . Signaling Receptors for TGF-β Family Members . Cold Spring Harbor Perspectives in Biology . 8 . 8 . a022053 . August 2016 . 27481709 . 4968163 . 10.1101/cshperspect.a022053 .
  8. Li N, Xie C, Lu NH . Transforming growth factor-β: an important mediator in Helicobacter pylori-associated pathogenesis . English . Frontiers in Cellular and Infection Microbiology . 5 . 77 . 2015 . 26583078 . 4632021 . 10.3389/fcimb.2015.00077 . free .