A stomatin-domain protein essential for touch sensation in the mouse.
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A stomatin-domain protein essential for touch sensation in the mouse. / Wetzel, Christiane; Hu, Jing; Riethmacher, Dieter; Benckendorff, Anne; Harder, Lena; Eilers, Andreas; Moshourab, Rabih; Kozlenkov, Alexey; Labuz, Dominika; Caspani, Ombretta; Erdmann, Bettina; Machelska, Halina; Heppenstall, Paul A; Lewin, Gary R.
in: NATURE, Jahrgang 445, Nr. 7124, 7124, 2007, S. 206-209.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - A stomatin-domain protein essential for touch sensation in the mouse.
AU - Wetzel, Christiane
AU - Hu, Jing
AU - Riethmacher, Dieter
AU - Benckendorff, Anne
AU - Harder, Lena
AU - Eilers, Andreas
AU - Moshourab, Rabih
AU - Kozlenkov, Alexey
AU - Labuz, Dominika
AU - Caspani, Ombretta
AU - Erdmann, Bettina
AU - Machelska, Halina
AU - Heppenstall, Paul A
AU - Lewin, Gary R
PY - 2007
Y1 - 2007
N2 - Touch and mechanical pain are first detected at our largest sensory surface, the skin. The cell bodies of sensory neurons that detect such stimuli are located in the dorsal root ganglia, and subtypes of these neurons are specialized to detect specific modalities of mechanical stimuli. Molecules have been identified that are necessary for mechanosensation in invertebrates but so far not in mammals. In Caenorhabditis elegans, mec-2 is one of several genes identified in a screen for touch insensitivity and encodes an integral membrane protein with a stomatin homology domain. Here we show that about 35% of skin mechanoreceptors do not respond to mechanical stimuli in mice with a mutation in stomatin-like protein 3 (SLP3, also called Stoml3), a mammalian mec-2 homologue that is expressed in sensory neurons. In addition, mechanosensitive ion channels found in many sensory neurons do not function without SLP3. Tactile-driven behaviours are also impaired in SLP3 mutant mice, including touch-evoked pain caused by neuropathic injury. SLP3 is therefore indispensable for the function of a subset of cutaneous mechanoreceptors, and our data support the idea that this protein is an essential subunit of a mammalian mechanotransducer.
AB - Touch and mechanical pain are first detected at our largest sensory surface, the skin. The cell bodies of sensory neurons that detect such stimuli are located in the dorsal root ganglia, and subtypes of these neurons are specialized to detect specific modalities of mechanical stimuli. Molecules have been identified that are necessary for mechanosensation in invertebrates but so far not in mammals. In Caenorhabditis elegans, mec-2 is one of several genes identified in a screen for touch insensitivity and encodes an integral membrane protein with a stomatin homology domain. Here we show that about 35% of skin mechanoreceptors do not respond to mechanical stimuli in mice with a mutation in stomatin-like protein 3 (SLP3, also called Stoml3), a mammalian mec-2 homologue that is expressed in sensory neurons. In addition, mechanosensitive ion channels found in many sensory neurons do not function without SLP3. Tactile-driven behaviours are also impaired in SLP3 mutant mice, including touch-evoked pain caused by neuropathic injury. SLP3 is therefore indispensable for the function of a subset of cutaneous mechanoreceptors, and our data support the idea that this protein is an essential subunit of a mammalian mechanotransducer.
M3 - SCORING: Zeitschriftenaufsatz
VL - 445
SP - 206
EP - 209
JO - NATURE
JF - NATURE
SN - 0028-0836
IS - 7124
M1 - 7124
ER -