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dc.contributor.authorSchmidt, Daniel
dc.contributor.authorTillberg, Paul W.
dc.contributor.authorChen, Fei
dc.contributor.authorBoyden, Edward Stuart
dc.date.accessioned2014-12-16T20:15:52Z
dc.date.available2014-12-16T20:15:52Z
dc.date.issued2014-01
dc.date.submitted2014-08
dc.identifier.issn2041-1723
dc.identifier.urihttp://hdl.handle.net/1721.1/92343
dc.description.abstractIon channels are among the most important proteins in biology, regulating the activity of excitable cells and changing in diseases. Ideally it would be possible to actuate endogenous ion channels, in a temporally precise and reversible manner, and without requiring chemical cofactors. Here we present a modular protein architecture for fully genetically encoded, light-modulated control of ligands that modulate ion channels of a targeted cell. Our reagent, which we call a lumitoxin, combines a photoswitch and an ion channel-blocking peptide toxin. Illumination causes the photoswitch to unfold, lowering the toxin’s local concentration near the cell surface, and enabling the ion channel to function. We explore lumitoxin modularity by showing operation with peptide toxins that target different voltage-dependent K+ channels. The lumitoxin architecture may represent a new kind of modular protein-engineering strategy for designing light-activated proteins, and thus may enable development of novel tools for modulating cellular physiology.en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (grant NIH 1DP2OD002002)en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (grant NIH 1R01DA029639)en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (grant NIH 1R01NS075421)en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (grant NIH 1RC1MH088182)en_US
dc.description.sponsorshipNational Science Foundation (U.S.) (NSF CAREER Award CBET 1053233)en_US
dc.description.sponsorshipUnited States. Defense Advanced Research Projects Agency (DARPA Living Foundries, Contract HR0011-12-C-0068)en_US
dc.description.sponsorshipNew York Stem Cell Foundation (Robertson Investigator Award)en_US
dc.description.sponsorshipDamon Runyon Cancer Research Foundation (DRG 2095-11)en_US
dc.description.sponsorshipFannie and John Hertz Foundationen_US
dc.description.sponsorshipNational Science Foundation (U.S.) (Graduate Research Fellowship under grant no. 1122374)en_US
dc.description.sponsorshipMassachusetts Institute of Technology. Synthetic Intelligence Laboratory (project)en_US
dc.language.isoen_US
dc.publisherNature Publishing Groupen_US
dc.relation.isversionofhttp://dx.doi.org/10.1038/ncomms4019en_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.rights.urien_US
dc.sourcePMCen_US
dc.titleA fully genetically encoded protein architecture for optical control of peptide ligand concentrationen_US
dc.typeArticleen_US
dc.identifier.citationSchmidt, Daniel, Paul W. Tillberg, Fei Chen, and Edward S. Boyden. “A Fully Genetically Encoded Protein Architecture for Optical Control of Peptide Ligand Concentration.” Nature Communications 5 (January 10, 2014).en_US
dc.contributor.departmentMassachusetts Institute of Technology. Materials Processing Centeren_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Brain and Cognitive Sciencesen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Electrical Engineering and Computer Scienceen_US
dc.contributor.departmentMcGovern Institute for Brain Research at MITen_US
dc.contributor.departmentProgram in Media Arts and Sciences (Massachusetts Institute of Technology)en_US
dc.contributor.mitauthorSchmidt, Danielen_US
dc.contributor.mitauthorChen, Feien_US
dc.contributor.mitauthorTillberg, Paul W.en_US
dc.contributor.mitauthorBoyden, Edward Stuarten_US
dc.relation.journalNature Communicationsen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsSchmidt, Daniel; Tillberg, Paul W.; Chen, Fei; Boyden, Edward S.en_US
dc.identifier.orcidhttps://orcid.org/0000-0003-3776-4605
dc.identifier.orcidhttps://orcid.org/0000-0003-0254-4741
dc.identifier.orcidhttps://orcid.org/0000-0002-0419-3351
mit.licensePUBLISHER_POLICYen_US


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