A
            <i>Drosophila</i>
            Mechanosensory Transduction Channel

Walker, Richard G.; Willingham, Aarron; Zuker, Charles S.

doi:10.1126/science.287.5461.2229

Cited by 632 publications

(561 citation statements)

References 32 publications

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“…Moreover, hydrogen bonding between the hydroxyl group of Thr and the imidazole ring of His contributes to the stability of AR motif and global AR proteins (16) (Figure 1c). The Val/IleVal-Xxx (hydrophilic)-Leu/Val-Leu-Leu motif (positions [17][18][19][20][21][22] is the central piece of the second R-helix of an AR motif, and it functions to form intra-and inter-AR hydrophobic networks to stabilize the global sketch of an AR protein (5,8). In addition, glycine residues are conserved at positions 13 and 25, which terminate the helices and provide the freedom for a loop to link both helices (5).…”

Section: Structurementioning

confidence: 99%

Ankyrin Repeat: A Unique Motif Mediating Protein−Protein Interactions

2006

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Ankyrin repeat, one of the most widely existing protein motifs in nature, consists of 30−34 amino acid residues and exclusively functions to mediate protein−protein interactions, some of which are directly involved in the development of human cancer and other diseases. Each ankyrin repeat exhibits a helix−turn−helix conformation, and strings of such tandem repeats are packed in a nearly linear array to form helix−turn−helix bundles with relatively flexible loops. The global structure of an ankyrin repeat protein is mainly stabilized by intra- and inter-repeat hydrophobic and hydrogen bonding interactions. The repetitive and elongated nature of ankyrin repeat proteins provides the molecular bases of the unique characteristics of ankyrin repeat proteins in protein stability, folding and unfolding, and binding specificity. Recent studies have demonstrated that ankyrin repeat proteins do not recognize specific sequences, and interacting residues are discontinuously dispersed into the whole molecules of both the ankyrin repeat protein and its partner. In addition, the availability of thousands of ankyrin repeat sequences has made it feasible to use rational design to modify the specificity and stability of physiologically important ankyrin repeat proteins and even to generate ankyrin repeat proteins with novel functions through combinatorial chemistry approaches.

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Section: Structurementioning

confidence: 99%

Ankyrin Repeat: A Unique Motif Mediating Protein−Protein Interactions

2006

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“…These neurons express the TRPN channel TRP-4 [48]. The trp-4 gene is an ortholog of the fruitfly and zebrafish nompC genes [74,88]. Because trp-4 mutants do not slow on entering a bacterial lawn [48], TRP-4 may have a role in transducing textural stimuli.…”

Section: Other Mechanosensory Behaviorsmentioning

confidence: 99%

“…One such gene is trp-4 [48]. As previously mentioned, TRP-4 is expressed in the dopaminergic neurons required for food-mediated slowing, but it is also expressed in the DVA interneuron [88]. The DVA cell body is located in the head, but it sends a process that extends for the entire length of the ventral cord [91].…”

Section: Other Mechanosensory Behaviorsmentioning

confidence: 99%

Touch sensitivity in Caenorhabditis elegans

Bounoutas

Chalfie

2007

Pflugers Arch - Eur J Physiol

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The nematode Caenorhabditis elegans was the first organism for which touch insensitive mutants were obtained. The study of the genes defective in these mutants has led to the identification of components of a mechanosensory complex needed for specific cells to sense gentle touch to the body. Multiple approaches using genetics, cell biology, biochemistry, and electrophysiology have characterized a channel complex, containing two DEG/ENaC pore-forming subunits and several other proteins, that transduces the touch response. Other mechanical responses, sensed by other cells using a variety of other components, are less well understood in C. elegans. Many of these other senses may use TRP channels, although DEG/ENaC channels have also been implicated.

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“…Trp is now a large family that encompasses channels of diverse functions from the receptors of heat, vanilloid, and menthol to possibly the store-operated channels (4). Among Trp-family channels, Osm9 (5), no mechanoreceptor potential C (nompC) (6), stretch inhibitable channel (SIC) (7), polycystin-2 (PC2) (8), and vanilloid receptor-related osmotically activated channel (VR-OAC) (9) are associated with mechanosensitivity in different animals. In prokaryotes, the MS channels MscL and MscS have been cloned, expressed, and crystallized (10)(11)(12)(13).…”

mentioning

confidence: 99%

The transient receptor potential channel on the yeast vacuole is mechanosensitive

Zhou

Batiza²,

Loukin³

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

144

123

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Ca 2؉ is released from the vacuole into the yeast cytoplasm on an osmotic upshock, but how this upshock is perceived was unknown. We found the vacuolar channel, Yvc1p, to be mechanosensitive, showing that the Ca 2؉ conduit is also the sensing molecule. Although fragile, the yeast vacuole allows limited direct mechanical examination. Pressures at tens of millimeters of Hg (1 mmHg ‫؍‬ 133 Pa) activate the 400-pS Yvc1p conductance in whole-vacuole recording mode as well as in the excised cytoplasmic-side-out mode. Raising the bath osmolarity activates this channel and causes vacuolar shrinkage and deformation. It appears that, on upshock, a transient osmotic force activates Yvc1p to release Ca 2؉ from the vacuole. Mechanical activation of Yvc1p occurs regardless of Ca 2؉ concentration and is apparently independent of its known Ca 2؉ activation, which we now propose to be an amplification mechanism (Ca 2؉ -induced Ca 2؉ release). Yvc1p is a member of the transient receptor potential-family channels, several of which have been associated with mechanosensation in animals. The possible use of Yvc1p as a molecular model to study mechanosensation in general is discussed.

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A Drosophila Mechanosensory Transduction Channel

Cited by 632 publications

References 32 publications

Ankyrin Repeat: A Unique Motif Mediating Protein−Protein Interactions

Ankyrin Repeat: A Unique Motif Mediating Protein−Protein Interactions

Touch sensitivity in Caenorhabditis elegans

The transient receptor potential channel on the yeast vacuole is mechanosensitive

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