Association of the Src family tyrosine kinase Fyn with TrkB
- PMID: 9648856
- DOI: 10.1046/j.1471-4159.1998.71010106.x
Association of the Src family tyrosine kinase Fyn with TrkB
Abstract
Fyn tyrosine kinase, a member of the Src family, was recently reported to be present in neurons and glia cells. We investigated whether Fyn is involved in the Trk-dependent signal transduction pathways of neurotrophin. The Fyn-Src homology domain 2 (SH2) was observed to associate in vitro with the intracellular domain of TrkB (ICD-TrkB). This association was dependent on the autophosphorylation of ICD-TrkB. The Fyn-SH2 domains bound to phosphorylated ICD-TrkB (pICD-TrkB) with an affinity similar to the binding of phospholipase Cgamma (PLCgamma)-SH2 domains to its autophosphorylation site in TrkB. The Src-SH2 domains showed substantially lower affinity with pICD-TrkB, suggesting that the association between Fyn-SH2 and pICD-TrkB is not due to nonspecific interactions of SH2 domains with phosphorylated tyrosine residues. This is further supported by the observation that Fyn-SH2 was able to trap phosphorylated TrkB in cell lysate prepared from primary rat cortical neurons stimulated with brain-derived neurotrophic factor (BDNF). In contrast, endogenous Fyn was coprecipitated with TrkB from cortical neurons without BDNF stimulation. This basal association showed a threefold increase on BDNF stimulation, probably due to the SH2/phosphotyrosine interaction that was observed in the cell-free system. All these data suggest the involvement of Fyn in the neurotrophin signal transduction pathways downstream of TrkB.
Similar articles
-
Inhibition of phosphorylation of TrkB and TrkC and their signal transduction by alpha2-macroglobulin.J Neurochem. 1998 Jul;71(1):213-20. doi: 10.1046/j.1471-4159.1998.71010213.x. J Neurochem. 1998. PMID: 9648868
-
Association of p59(fyn) with the T lymphocyte costimulatory receptor CD2. Binding of the Fyn Src homology (SH) 3 domain is regulated by the Fyn SH2 domain.J Biol Chem. 1998 Jul 31;273(31):19914-21. doi: 10.1074/jbc.273.31.19914. J Biol Chem. 1998. PMID: 9677430
-
Specific binding of Fyn and phosphatidylinositol 3-kinase to the B cell surface glycoprotein CD19 through their src homology 2 domains.Eur J Immunol. 1995 Oct;25(10):2978-84. doi: 10.1002/eji.1830251040. Eur J Immunol. 1995. PMID: 7589101
-
Regulation and targets of receptor tyrosine kinases.Eur J Cancer. 2002 Sep;38 Suppl 5:S3-10. doi: 10.1016/s0959-8049(02)80597-4. Eur J Cancer. 2002. PMID: 12528767 Review.
-
SH2 and PTB domain interactions in tyrosine kinase signal transduction.Curr Opin Chem Biol. 1997 Aug;1(2):227-34. doi: 10.1016/s1367-5931(97)80014-2. Curr Opin Chem Biol. 1997. PMID: 9667855 Review.
Cited by
-
Fyn kinase contributes to tyrosine phosphorylation of the GABA(A) receptor gamma2 subunit.Mol Cell Neurosci. 2010 Jun;44(2):129-34. doi: 10.1016/j.mcn.2010.03.002. Epub 2010 Mar 15. Mol Cell Neurosci. 2010. PMID: 20233604 Free PMC article.
-
Postsynaptic action of brain-derived neurotrophic factor attenuates alpha7 nicotinic acetylcholine receptor-mediated responses in hippocampal interneurons.J Neurosci. 2008 May 21;28(21):5611-8. doi: 10.1523/JNEUROSCI.5378-07.2008. J Neurosci. 2008. PMID: 18495895 Free PMC article.
-
Role of Src Family Kinases in BDNF-Mediated Suppression of Cocaine-Seeking and Prevention of Cocaine-Induced ERK, GluN2A, and GluN2B Dephosphorylation in the Prelimbic Cortex.Neuropsychopharmacology. 2017 Sep;42(10):1972-1980. doi: 10.1038/npp.2017.114. Epub 2017 Jun 6. Neuropsychopharmacology. 2017. PMID: 28585567 Free PMC article.
-
The Insula and Taste Learning.Front Mol Neurosci. 2017 Nov 3;10:335. doi: 10.3389/fnmol.2017.00335. eCollection 2017. Front Mol Neurosci. 2017. PMID: 29163022 Free PMC article. Review.
-
Fyn Tyrosine Kinase as Harmonizing Factor in Neuronal Functions and Dysfunctions.Int J Mol Sci. 2020 Jun 22;21(12):4444. doi: 10.3390/ijms21124444. Int J Mol Sci. 2020. PMID: 32580508 Free PMC article. Review.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous
