Dynamics and mechanism of a light-driven chloride pump

Mous, S.; Gotthard, Guillaume; Ehrenberg, D.; Sen, Saumik; Weinert, T.; Johnson, Philip J. M.; James, Daniel; Nass, Karol; Furrer, Antonia; Kekilli, D.; Ma, Pikyee; Brünle, Steffen; Casadei, Cecilia M.; Martiel, Isabelle; Dworkowski, Florian; Gashi, Dardan; Skopintsev, Petr; Wranik, Maximilian; Knopp, G.; Panepucci, Ezequiel; Panneels, Valérie; Cirelli, Claudio; Ozerov, Dmitry; Schertler, G.F.X.; Wang, Meitian; Milne, Chris; Standfuss, Joerg; Schapiro, Igor; Heberle, Joachim; Nogly, Przemyslaw

doi:10.1126/science.abj6663

Cited by 49 publications

(36 citation statements)

References 76 publications

(72 reference statements)

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“…Thereby, kinetic information is retrieved on the temporal sequence of structural changes in mechanosensitive channels. Time-resolved crystallographic techniques can track these structural changes at utmost temporal and spatial resolution ( Skopintsev et al, 2020 ; Mous et al, 2022 ), once the mechanosensing protein is co-crystalized with AzoPC. Finally, these experiments will derive an atomic picture of the lipid/protein coupling and resolve the gating mechanism of these channels.…”

Section: Discussionmentioning

confidence: 99%

Photoactivation of a Mechanosensitive Channel

Crea

Vorkas

Redlich

et al. 2022

Front. Mol. Biosci.

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Optogenetics in the conventional sense, i.e. the use of engineered proteins that gain their light sensitivity from naturally abundant chromophores, represents an exciting means to trigger and control biological activity by light. As an alternate approach, photopharmacology controls biological activity with the help of synthetic photoswitches. Here, we used an azobenzene-derived lipid analogue to optically activate the transmembrane mechanosensitive channel MscL which responds to changes in the lateral pressure of the lipid bilayer. In this work, MscL has been reconstituted in nanodiscs, which provide a native-like environment to the protein and a physical constraint to membrane expansion. We characterized this photomechanical system by FTIR spectroscopy and assigned the vibrational bands of the light-induced FTIR difference spectra of the trans and cis states of the azobenzene photolipid by DFT calculations. Differences in the amide I range indicated reversible conformational changes in MscL as a direct consequence of light switching. With the mediation of nanodiscs, we inserted the transmembrane protein in a free standing photoswitchable lipid bilayer, where electrophysiological recordings confirmed that the ion channel could be set to one of its sub-conducting states upon light illumination. In conclusion, a novel approach is presented to photoactivate and control cellular processes as complex and intricate as gravitropism and turgor sensing in plants, contractility of the heart, as well as sensing pain, hearing, and touch in animals.

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Section: Discussionmentioning

confidence: 99%

Photoactivation of a Mechanosensitive Channel

Crea

Vorkas

Redlich

et al. 2022

Front. Mol. Biosci.

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“…Following chromophore isomerization the chloride ion first dissociates from the protonated Schiff base and then starts to diffuse away. Additional molecular details of the interactions and trajectory of the chloride ion are provided by recent ps up to ms studies using time-resolved serial crystallography in combination with spectral and theoretical analysis ( Hosaka et al, 2022 ; Mous et al, 2022 ). An XFEL study of the channelrhodopsin chimera C1C2, that photochemically behaves like ChR1, investigated the photo-induced conformational changes from 1 µs to 4 ms ( Oda et al, 2021 ).…”

Section: Photochemical Propertiesmentioning

confidence: 99%

Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering

Grip

Ganapathy

2022

Front. Chem.

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The first member and eponym of the rhodopsin family was identified in the 1930s as the visual pigment of the rod photoreceptor cell in the animal retina. It was found to be a membrane protein, owing its photosensitivity to the presence of a covalently bound chromophoric group. This group, derived from vitamin A, was appropriately dubbed retinal. In the 1970s a microbial counterpart of this species was discovered in an archaeon, being a membrane protein also harbouring retinal as a chromophore, and named bacteriorhodopsin. Since their discovery a photogenic panorama unfolded, where up to date new members and subspecies with a variety of light-driven functionality have been added to this family. The animal branch, meanwhile categorized as type-2 rhodopsins, turned out to form a large subclass in the superfamily of G protein-coupled receptors and are essential to multiple elements of light-dependent animal sensory physiology. The microbial branch, the type-1 rhodopsins, largely function as light-driven ion pumps or channels, but also contain sensory-active and enzyme-sustaining subspecies. In this review we will follow the development of this exciting membrane protein panorama in a representative number of highlights and will present a prospect of their extraordinary future potential.

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“…As a widely distributed energy, visible light has the advantages of no pollution and no harm, and is widely applied in various stimulus-responsive functional materials ( Xu & Wang, 2022 ). Moreover, the natural light-responsive ionic nanochannels of rhodopsin are regulated by visible light and realized the conduction of visual nerve signals ( Mous et al, 2022 ). Therefore, the construction of visible light-responsive ionic transport nanochannels is conducive to deepening the understanding of similar biological processes.…”

Section: Photoresponsive Host–guest System-assembled Nanochannelsmentioning

confidence: 99%

Light-responsive nanochannels based on the supramolecular host–guest system

Quan

Guo

et al. 2022

Front. Chem.

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The light-responsive nanochannel of rhodopsin gained wider research interest from its crucial roles in light-induced biological functions, such as visual signal transduction and energy conversion, though its poor stability and susceptibility to inactivation in vitro have limited its exploration. However, the fabrication of artificial nanochannels with the properties of physical stability, controllable structure, and easy functional modification becomes a biomimetic system to study the stimulus-responsive gating properties. Typically, light-responsive molecules of azobenzene (Azo), retinal, and spiropyran were introduced into nanochannels as photo-switches, which can change the inner surface wettability of nanochannels under the influence of light; this ultimately results in the photoresponsive nature of biomimetic nanochannels. Furthermore, the fine-tuning of their stimulus-responsive properties can be achieved through the introduction of host–guest systems generally combined with a non-covalent bond, and the assembling process is reversible. These host–guest systems have been introduced into the nanochannels to form different functions. Based on the host–guest system of light-responsive reversible interaction, it can not only change the internal surface properties of the nanochannel and control the recognition and transmission behaviors but also realize the controlled release of a specific host or guest molecules in the nanochannel. At present, macrocyclic host molecules have been introduced into nanochannels including pillararenes, cyclodextrin (CD), and metal–organic frameworks (MOFs). They are introduced into the nanochannel through chemical modification or host–guest assemble methods. Based on the changes in the light-responsive structure of azobenzene, spiropyran, retinal, and others with macrocycle host molecules, the surface charge and hydrophilic and hydrophobic properties of the nanochannel were changed to regulate the ionic and molecular transport. In this study, the development of photoresponsive host and guest-assembled nanochannel systems from design to application is reviewed, and the research prospects and problems of this photo-responsive nanochannel membrane are presented.

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Dynamics and mechanism of a light-driven chloride pump

Cited by 49 publications

References 76 publications

Photoactivation of a Mechanosensitive Channel

Photoactivation of a Mechanosensitive Channel

Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering

Light-responsive nanochannels based on the supramolecular host–guest system

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