Trk receptor

Trk receptor
Identifiers
SymbolTrk
InterProIPR020777
Membranome1342

Trk receptors are a family of tyrosine kinases that regulates synaptic strength and plasticity in the mammalian nervous system.[1][2] Trk receptors affect neuronal survival and differentiation through several signaling cascades. However, the activation of these receptors also has significant effects on functional properties of neurons.

The common ligands of trk receptors are neurotrophins, a family of growth factors critical to the functioning of the nervous system.[3] The binding of these molecules is highly specific. Each type of neurotrophin has different binding affinity toward its corresponding Trk receptor. The activation of Trk receptors by neurotrophin binding may lead to activation of signal cascades resulting in promoting survival and other functional regulation of cells.

  1. ^ Malenka RC, Nestler EJ, Hyman SE (2009). "Chapter 8: Atypical neurotransmitters". In Sydor A, Brown RY (eds.). Molecular Neuropharmacology: A Foundation for Clinical Neuroscience (2nd ed.). New York: McGraw-Hill Medical. ISBN 9780071481274. Another common feature of neurotrophins is that they produce their physiologic effects by means of the tropomyosin receptor kinase (Trk) receptor family (also known as the tyrosine receptor kinase family). ...
    Trk receptors
    All neurotrophins bind to a class of highly homologous receptor tyrosine kinases known as Trk receptors, of which three types are known: TrkA, TrkB, and TrkC. These transmembrane receptors are glycoproteins whose molecular masses range from 140 to 145 kDa. Each type of Trk receptor tends to bind specific neurotrophins: TrkA is the receptor for NGF, TrkB the receptor for BDNF and NT-4, and TrkC the receptor for NT-3.However, some overlap in the specificity of these receptors has been noted.
  2. ^ Huang EJ, Reichardt LF (2003). "Trk receptors: roles in neuronal signal transduction". Annual Review of Biochemistry. 72: 609–42. doi:10.1146/annurev.biochem.72.121801.161629. PMID 12676795.
  3. ^ Segal RA (2003). "Selectivity in neurotrophin signaling: theme and variations". Annual Review of Neuroscience. 26: 299–330. doi:10.1146/annurev.neuro.26.041002.131421. PMID 12598680.