Touch sensitivity in Caenorhabditis elegans

Bounoutas, Alexander; Chalfie, Martin

doi:10.1007/s00424-006-0187-x

Cited by 80 publications

(77 citation statements)

References 100 publications

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“…This model and derivatives that propose that channels are linked to the ECM but not to 15pf microtubules (Emtage et al, 2004;Bounoutas and Chalfie, 2007) make specific predictions about the position of MeT channels in relation to MEC-5 and 15pf microtubule endpoints. We used serialsection immunoelectron microscopy and digital 3-D reconstruction methods to localize native MeT channels in C. elegans touch receptor neurons to establish the structural correlates of channel gating and to test these models.…”

Section: Discussionmentioning

confidence: 88%

Nanoscale Organization of the MEC-4 DEG/ENaC Sensory Mechanotransduction Channel inCaenorhabditis elegansTouch Receptor Neurons

Cueva¹,

Mulholland²,

Goodman³

2007

J. Neurosci.

141

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Hearing, touch and proprioception are thought to involve direct activation of mechano-electrical transduction (MeT) channels. In Caenorhabditis elegans touch receptor neurons (TRNs), such channels contain two pore-forming subunits (MEC-4 and MEC-10) and two auxiliary subunits (MEC-2 and MEC-6). MEC-4 and MEC-10 belong to a large superfamily of ion channel proteins (DEG/ENaCs) that form nonvoltage-gated, amiloride-sensitive Na ϩ channels. In TRNs, unique 15-protofilament microtubules and an electron-dense extracellular matrix have been proposed to serve as gating tethers critical for MeT channel activation. We combined high-pressure freezing and serial-section immunoelectron microscopy to determine the position of MeT channels relative to putative gating tethers. MeT channels were visualized using antibodies against MEC-4 and MEC-2. This nanometer-resolution view of a sensory MeT channel establishes structural constraints on the mechanics of channel gating. We show here that MEC-2 and MEC-5 collagen, a putative extracellular tether, occupy overlapping but distinct domains in TRN neurites. Although channels decorate all sides of TRN neurites; they are not associated with the distal endpoints of 15-protofilament microtubules hypothesized to be gating tethers. These specialized microtubules, which are unique to TRNs, assemble into a cross-linked bundle connected by a network of kinked filaments to the neurite membrane. We speculate that the microtubule bundle converts external point loads into membrane stretch which, in turn, facilitates MeT channel activation.

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Section: Discussionmentioning

confidence: 88%

Nanoscale Organization of the MEC-4 DEG/ENaC Sensory Mechanotransduction Channel inCaenorhabditis elegansTouch Receptor Neurons

Cueva¹,

Mulholland²,

Goodman³

2007

J. Neurosci.

141

View full text Add to dashboard Cite

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“…However, to date it is frequently difficult to discriminate between direct and indirect mechanosensitivity due to limitations of the technical resolution and the experimental designs chosen. However, it should be kept in mind that mechanosensory protein complexes may consist of several distinct components that are neatly orchestrated to sense and transduce mechanical signals (9). By this means, a given protein may not be mechanosensitive eo ipso but may still react to mechanical cues in conjunction with other proteins within macromolecular complexes.…”

Section: Criteria For Mechanosensitive Integral Membrane Proteinsmentioning

confidence: 99%

“…This kind of mechanosensitive protein complexes is best understood in Caenorhabditis elegans touch receptor neurons (9,28).…”

Section: Potential Mechanosensors Discussed So Farmentioning

confidence: 99%

G protein-mediated stretch reception

Storch¹,

Schnitzler

Gudermann

2012

American Journal of Physiology-Heart and Circulatory Physiology

154

136

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Mechanosensation and -transduction are important for physiological processes like the senses of touch, hearing, and balance. The mechanisms underlying the translation of mechanical stimuli into biochemical information by activating various signaling pathways play a fundamental role in physiology and pathophysiology but are only poorly understood. Recently, G protein-coupled receptors (GPCRs), which are essential for the conversion of light, olfactory and gustatory stimuli, as well as of primary messengers like hormones and neurotransmitters into cellular signals and which play distinct roles in inflammation, cell growth, and differentiation, have emerged as potential mechanosensors. The first candidate for a mechanosensitive GPCR was the angiotensin-II type-1 (AT 1) receptor. Agonist-independent mechanical receptor activation of AT 1 receptors induces an active receptor conformation that appears to differ from agonist-induced receptor conformations and entails the activation of G proteins. Mechanically induced AT 1 receptor activation plays an important role for myogenic vasoconstriction and for the initiation of cardiac hypertrophy. A growing body of evidence suggests that other GPCRs are involved in mechanosensation as well. These findings highlight physiologically relevant, ligand-independent functions of GPCRs and add yet another facet to the polymodal activation spectrum of this ubiquitous protein family. mechanosensation; G protein-coupled receptor; angiotensin-II type-1 receptor; agonist independent THIS ARTICLE is part of a collection on G Protein Kinase A Signaling in Cardiovascular Physiology and Disease. Other articles appearing in this collection, as well as a full archive of all collections, can be found online at http://ajpheart.physiology. org/.

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“…However, sensory cells which are specialized for the detection of mechanical stimuli (mechanoreceptors) can use elaborate protein complexes to transduce adequate mechanical stimuli, and to report a sensory signal to the central nervous system. How intricate the structure of such a transducer can be revealed by an extensive genetic screen of Caenorhabditis elegans mutants which took more than 25 years and brought to light a set of proteins that coassemble to form a mechanotransduction complex (O'Hagan and ChalWe 2006;Bianchi 2007;Bounoutas and ChalWe 2007). This multi-protein system works by pulling transduction channels open when the worm's cuticula moves (Fig.…”

Section: Mechanoreceptors: Tugging At Enigmatic Channelsmentioning

confidence: 99%

Primary processes in sensory cells: current advances

Frings

2008

J Comp Physiol A

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In the course of evolution, the strong and unremitting selective pressure on sensory performance has driven the acuity of sensory organs to its physical limits. As a consequence, the study of primary sensory processes illustrates impressively how far a physiological function can be improved if the survival of a species depends on it. Sensory cells that detect single-photons, single molecules, mechanical motions on a nanometer scale, or incredibly small Xuctuations of electromagnetic Welds have fascinated physiologists for a long time. It is a great challenge to understand the primary sensory processes on a molecular level. This review points out some important recent developments in the search for primary processes in sensory cells that mediate touch perception, hearing, vision, taste, olfaction, as well as the analysis of light polarization and the orientation in the Earth's magnetic Weld. The data are screened for common transduction strategies and common transduction molecules, an aspect that may be helpful for researchers in the Weld. Keywords

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Touch sensitivity in Caenorhabditis elegans

Cited by 80 publications

References 100 publications

Nanoscale Organization of the MEC-4 DEG/ENaC Sensory Mechanotransduction Channel inCaenorhabditis elegansTouch Receptor Neurons

Nanoscale Organization of the MEC-4 DEG/ENaC Sensory Mechanotransduction Channel inCaenorhabditis elegansTouch Receptor Neurons

G protein-mediated stretch reception

Primary processes in sensory cells: current advances

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