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Originally published In Press as doi:10.1074/jbc.M205202200 on August 28, 2002

J. Biol. Chem., Vol. 277, Issue 45, 43160-43167, November 8, 2002
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Regulation of TRKB Surface Expression by Brain-derived Neurotrophic Factor and Truncated TRKB Isoforms*

Annakaisa HaapasaloDagger §, Ilkka SipolaDagger , Kim LarssonDagger , Karl E. O. ÅkermanDagger , Peter Stoilov, Stefan Stamm, Garry WongDagger , and Eero CastrénDagger ||**

From the Dagger  Department of Neurobiology, A. I. Virtanen Institute and || Department of Psychiatry, University of Kuopio, P. O. Box 1627, 70211 Kuopio, Finland and  Universiteat Erlangen, Institute of Biochemistry, Fahrstrasse 17, 91054 Erlangen, Germany

Brain-derived neurotrophic factor (BDNF) signaling through its receptor TRKB modulates survival, differentiation, and activity of neurons. BDNF activates TRKB on the cell surface, which leads to the initiation of intracellular signaling cascades and different biological responses in neurons. Neuronal activity has been shown to regulate TRKB levels on the plasma membrane of neurons, but little is known about other factors affecting TRKB surface expression levels. We report here that BDNF regulates the cell surface levels of transfected or endogenously expressed full-length TRKB, depending on the exposure time in neuroblastoma cells and primary hippocampal neurons. BDNF rapidly increases TRKB surface expression levels in seconds, whereas treatment of cells with BDNF for a longer time (minutes to hours) leads to decreased TRKB surface levels. Coexpression of the full-length TRKB together with the truncated TRKB.T1 isoform results in decreased levels of full-length TRKB on the cell surface. This effect is specific to the T1 isoform, because coexpression of a kinase-dead TRKB mutant or another kinase domain-lacking TRKB form, truncated T-Shc, leads to increased TRKB surface levels. Our results suggest that regulation of TRKB surface expression levels by different factors is tightly controlled by complex mechanisms in active neurons.

* This work was supported by the Academy of Finland, the Sigrid Juselius Foundation, and the European Union.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Ph.D. student of the Finnish Graduate School of Neuroscience.

** To whom correspondence should be addressed: Dept. of Neurobiology, A. I. Virtanen Institute, University of Kuopio, P. O. Box 1627, 70211, Kuopio, Finland. Tel.: 358-17-162084; Fax: 358-17-163030; E-mail: Eero.Castren@uku.fi.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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