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Oregon Health and Science University, University of Virginia

Nat. Neurosci., 16,365–374, (March 2013) | doi:10.1038/nn.3312 Molecular architecture of the chick vestibular hair bundle

Abstract

Jung-Bum Shin^1,2,8, Jocelyn F Krey^2,8, Ahmed Hassan³, Zoltan Metlagel³, Andrew N Tauscher³, James M Pagana^1,2, Nicholas E Sherman⁴, Erin D Jeffery⁴, Kateri J Spinelli², Hongyu Zhao², Phillip A Wilmarth⁵, Dongseok Choi⁶, Larry L David⁵, Manfred Auer³ & Peter G Barr-Gillespie^2,7,*

¹Department of Neuroscience, University of Virginia, Charlottesville, Virginia, USA. ²Oregon Hearing Research Center, Oregon Health & Science University, Portland, Oregon, USA. ³Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California, USA. ⁴W.M. Keck Biomedical Mass Spectrometry Laboratory, University of Virginia, Charlottesville, Virginia, USA. ⁵Department of Biochemistry & Molecular Biology, Oregon Health & Science University, Portland, Oregon, USA. ⁶Department of Public Health & Preventive Medicine, Oregon Health & Science University, Portland, Oregon, USA. ⁷Vollum Institute, Oregon Health & Science University, Portland, Oregon, USA. ⁸These authors contributed equally to this work.

^*Correspondence to: Peter G Barr-Gillespie

Abstract
Hair bundles of the inner ear have a specialized structure and protein composition that underlies their sensitivity to mechanical stimulation. Using mass spectrometry, we identified and quantified >1,100 proteins, present from a few to 400,000 copies per stereocilium, from purified chick bundles; 336 of these were significantly enriched in bundles. Bundle proteins that we detected have been shown to regulate cytoskeleton structure and dynamics, energy metabolism, phospholipid synthesis and cell signaling. Three-dimensional imaging using electron tomography allowed us to count the number of actin-actin cross-linkers and actin-membrane connectors; these values compared well to those obtained from mass spectrometry. Network analysis revealed several hub proteins, including RDX (radixin) and SLC9A3R2 (NHERF2), which interact with many bundle proteins and may perform functions essential for bundle structure and function. The quantitative mass spectrometry of bundle proteins reported here establishes a framework for future characterization of dynamic processes that shape bundle structure and function.

논문정보

형식Research article
게재일2013년 03월 (BRIC 등록일 2013-03-12)
연구진국외 연구진
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