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First published online 11 August 2009
doi: 10.1242/jcs.047712

Journal of Cell Science 122, 3123-3136 (2009)
Published by The Company of Biologists 2009
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Research Article

Mechanism underlying activity-dependent insertion of TrkB into the neuronal surface

Ling Zhao1,*, Ai-Li Sheng1,*, Shu-Hong Huang1,*, Yu-Xia Yin1, Bing Chen1, Xue-Zhi Li1, Yun Zhang2 and Zhe-Yu Chen1,{ddagger}

1 Department of Neurobiology, Key Laboratory of Medical Neurobiology, School of Medicine, Shandong University, Jinan, Shandong 250012, P.R. China
2 Key Laboratory of Cardiovascular Remodeling and Function Research, Chinese Ministry of Education and Chinese Ministry of Health, Qilu Hospital, Shandong University, Jinan, Shandong 250012, P.R. China

{ddagger} Author for correspondence (zheyuchen{at}sdu.edu.cn)

Accepted 9 June 2009

Activity-dependent insertion of tyrosine kinase receptor type 2 (TrkB receptor) into the plasma membrane can explain, in part, the preferential effect of brain-derived neurotrophic factor (BDNF) on active neurons; however, the detailed cellular and molecular mechanisms underlying this process are still unclear. In our study, we developed a fluorescence ratiometric assay for surface TrkB receptors to investigate the mechanisms of recruitment of TrkB to the plasma membrane following chemical long-term potentiation (cLTP) induction. We found that, in hippocampal neurons, the effect of cLTP-induced TrkB surface-recruitment occurred predominantly on neurites with rapid kinetics (t1/2 of ~2.3 minutes) and was dependent on an intact cytoskeleton structure. Mutagenesis studies revealed that the juxtamembrane domain of TrkB is necessary and sufficient for its activity-dependent insertion into the plasma membrane. Moreover, we found that the phosphorylation of TrkB receptor at the Ser478 site by cyclin-dependent kinase 5 (Cdk5) is essential for cLTP-induced TrkB insertion into the neuronal surface. Finally, the degree of cLTP-induced TrkB surface-recruitment is higher in postsynaptic regions, which provides a potential mechanism for rapid enhancement of postsynaptic sensitivity to incoming BDNF signaling. Our studies provide new insights regarding neuronal activity-dependent surface delivery of TrkB receptor, which will advance our understanding of the modulatory role of TrkB in synaptic plasticity.

Key words: TrkB, Activity, cLTP, Neuron, Surface insertion, Juxtamembrane domain


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