Research ArticleBiochemistry

The receptor tyrosine kinase TrkB signals without dimerization at the plasma membrane

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Sci. Signal.  08 May 2018:
Vol. 11, Issue 529, eaao4006
DOI: 10.1126/scisignal.aao4006

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RTKs on a new Trk

The conventional mechanism of receptor tyrosine kinase (RTK) activation is ligand-induced dimerization in the plasma membrane, upon which one monomer phosphorylates the other to initiate downstream, intracellular signaling and receptor internalization. However, using live-cell fluorescence imaging, Zahavi et al. found that the RTK TrkB in rodent neurons is internalized as a monomer. Only then in endosomes does TrkB dimerize, both independently of and (markedly more so) in response to the presence of its ligand BDNF in the endosome. The same behavior was observed when TrkB was expressed in a human cell line. These findings and future technological advances may challenge the generalized dogma of dimer-initiated RTK signaling.