Molecular architecture of the chick vestibular hair bundle

Jung Bum Shin, Jocelyn F. Krey, Ahmed Hassan, Zoltan Metlagel, Andrew N. Tauscher, James M. Pagana, Nicholas E. Sherman, Erin D. Jeffery, Kateri J. Spinelli, Hongyu Zhao, Phillip Wilmarth, Dongseok Choi, Larry David, Manfred Auer, Peter Barr-Gillespie

Research output: Contribution to journalArticle

80 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)365-374
Number of pages10
JournalNature Neuroscience
Volume16
Issue number3
DOIs
StatePublished - Mar 2013

Fingerprint

Actins
Mass Spectrometry
Proteins
Electron Microscope Tomography
Stereocilia
Three-Dimensional Imaging
Inner Ear
Cytoskeleton
Energy Metabolism
Phospholipids
Membranes
radixin

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Shin, J. B., Krey, J. F., Hassan, A., Metlagel, Z., Tauscher, A. N., Pagana, J. M., ... Barr-Gillespie, P. (2013). Molecular architecture of the chick vestibular hair bundle. Nature Neuroscience, 16(3), 365-374. https://doi.org/10.1038/nn.3312

Molecular architecture of the chick vestibular hair bundle. / Shin, Jung Bum; Krey, Jocelyn F.; Hassan, Ahmed; Metlagel, Zoltan; Tauscher, Andrew N.; Pagana, James M.; Sherman, Nicholas E.; Jeffery, Erin D.; Spinelli, Kateri J.; Zhao, Hongyu; Wilmarth, Phillip; Choi, Dongseok; David, Larry; Auer, Manfred; Barr-Gillespie, Peter.

In: Nature Neuroscience, Vol. 16, No. 3, 03.2013, p. 365-374.

Research output: Contribution to journalArticle

Shin, JB, Krey, JF, Hassan, A, Metlagel, Z, Tauscher, AN, Pagana, JM, Sherman, NE, Jeffery, ED, Spinelli, KJ, Zhao, H, Wilmarth, P, Choi, D, David, L, Auer, M & Barr-Gillespie, P 2013, 'Molecular architecture of the chick vestibular hair bundle', Nature Neuroscience, vol. 16, no. 3, pp. 365-374. https://doi.org/10.1038/nn.3312
Shin JB, Krey JF, Hassan A, Metlagel Z, Tauscher AN, Pagana JM et al. Molecular architecture of the chick vestibular hair bundle. Nature Neuroscience. 2013 Mar;16(3):365-374. https://doi.org/10.1038/nn.3312
Shin, Jung Bum ; Krey, Jocelyn F. ; Hassan, Ahmed ; Metlagel, Zoltan ; Tauscher, Andrew N. ; Pagana, James M. ; Sherman, Nicholas E. ; Jeffery, Erin D. ; Spinelli, Kateri J. ; Zhao, Hongyu ; Wilmarth, Phillip ; Choi, Dongseok ; David, Larry ; Auer, Manfred ; Barr-Gillespie, Peter. / Molecular architecture of the chick vestibular hair bundle. In: Nature Neuroscience. 2013 ; Vol. 16, No. 3. pp. 365-374.
@article{281522f83ed94994821b5e87e92335d0,
title = "Molecular architecture of the chick vestibular hair bundle",
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.",
author = "Shin, {Jung Bum} and Krey, {Jocelyn F.} and Ahmed Hassan and Zoltan Metlagel and Tauscher, {Andrew N.} and Pagana, {James M.} and Sherman, {Nicholas E.} and Jeffery, {Erin D.} and Spinelli, {Kateri J.} and Hongyu Zhao and Phillip Wilmarth and Dongseok Choi and Larry David and Manfred Auer and Peter Barr-Gillespie",
year = "2013",
month = "3",
doi = "10.1038/nn.3312",
language = "English (US)",
volume = "16",
pages = "365--374",
journal = "Nature Neuroscience",
issn = "1097-6256",
publisher = "Nature Publishing Group",
number = "3",

}

TY - JOUR

T1 - Molecular architecture of the chick vestibular hair bundle

AU - Shin, Jung Bum

AU - Krey, Jocelyn F.

AU - Hassan, Ahmed

AU - Metlagel, Zoltan

AU - Tauscher, Andrew N.

AU - Pagana, James M.

AU - Sherman, Nicholas E.

AU - Jeffery, Erin D.

AU - Spinelli, Kateri J.

AU - Zhao, Hongyu

AU - Wilmarth, Phillip

AU - Choi, Dongseok

AU - David, Larry

AU - Auer, Manfred

AU - Barr-Gillespie, Peter

PY - 2013/3

Y1 - 2013/3

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84875890050&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84875890050&partnerID=8YFLogxK

U2 - 10.1038/nn.3312

DO - 10.1038/nn.3312

M3 - Article

VL - 16

SP - 365

EP - 374

JO - Nature Neuroscience

JF - Nature Neuroscience

SN - 1097-6256

IS - 3

ER -