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Molecular Microdomains in a Sensory Terminal, the Vestibular Calyx Ending

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Title: Molecular Microdomains in a Sensory Terminal, the Vestibular Calyx Ending
Author(s): Lysakowski, Anna; Gaboyard-Niay, Sophie; Calin-Jageman, Irina; Chatlani, Shilpa; Price, Steven D.; Eatock, Ruth Anne
Abstract: Many primary vestibular afferents form large cup-shaped postsynaptic terminals (calyces) that envelope the basolateral surfaces of type I hair cells. The calyceal terminals both respond to glutamate released from ribbon synapses in the type I cells and initiate spikes that propagate to the afferent’s central terminals in the brainstem. The combination of synaptic and spike initiation functions in these unique sensory endings distinguishes them from the axonal nodes of central neurons and peripheral nerves, such as the sciatic nerve, which have provided most of our information about nodal specializations. We show that rat vestibular calyces express an unusual mix of voltage-gatedNa and K channels and scaffolding, cell adhesion, and extracellular matrix proteins, which may hold the ion channels in place. Protein expression patterns form several microdomains within the calyx membrane: a synaptic domain facing the hair cell, the heminode abutting the first myelinated internode, and one or two intermediate domains. Differences in the expression and localization of proteins between afferent types and zones may contribute to known variations in afferent physiology.
Issue Date: 2011-07-06
Publisher: Society for Neuroscience
Citation Info: Lysakowski, A., Gaboyard-Niay, S., Calin-Jageman, I., Chatlani, S., Price, S. D., & Eatock, R. A. 2011. Molecular microdomains in a sensory terminal, the vestibular calyx ending. Journal of Neuroscience, 31(27): 10101-10114. DOI:10.1523/JNEUROSCI.0521-11.2011
Type: Article
Description: © 2011 Society for Neuroscience, Journal of Neuroscience DOI: 10.1523/JNEUROSCI.0521-11.2011
URI: http://hdl.handle.net/10027/8391
ISSN: 0270-6474
Sponsor: This study was supported by NIH Grants R01 DC-02521, R01 DC-02058, and R01 DC-02290. The Electron Microscopic Facility of the Research Resources Center of the University of Illinois at Chicago provided equipment and assistance to conduct this study.
Date Available in INDIGO: 2012-06-27
 

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