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Article: Opsin is a phospholipid flippase

TitleOpsin is a phospholipid flippase
Authors
Issue Date2011
PublisherCell Press. The Journal's web site is located at http://www.current-biology.com/
Citation
Current Biology, 2011, v. 21 n. 2, p. 149-153 How to Cite?
AbstractPolar lipids must flip-flop rapidly across biological membranes to sustain cellular life [1, 2], but flipping is energetically costly [3] and its intrinsic rate is low. To overcome this problem, cells have membrane proteins that function as lipid transporters (flippases) to accelerate flipping to a physiologically relevant rate. Flippases that operate at the plasma membrane of eukaryotes, coupling ATP hydrolysis to unidirectional lipid flipping, have been defined at a molecular level [2]. On the other hand, ATP-independent bidirectional flippases that translocate lipids in biogenic compartments, e.g., the endoplasmic reticulum, and specialized membranes, e.g., photoreceptor discs [4, 5], have not been identified even though their activity has been recognized for more than 30 years [1]. Here, we demonstrate that opsin is the ATP-independent phospholipid flippase of photoreceptor discs. We show that reconstitution of opsin into large unilamellar vesicles promotes rapid (τ < 10 s) flipping of phospholipid probes across the vesicle membrane. This is the first molecular identification of an ATP-independent phospholipid flippase in any system. It reveals an unexpected activity for opsin and, in conjunction with recently available structural information on this G protein-coupled receptor [6, 7], significantly advances our understanding of the mechanism of ATP-independent lipid flip-flop. © 2011 Elsevier Ltd All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/188682
ISSN
2015 Impact Factor: 8.983
2015 SCImago Journal Rankings: 4.729
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMenon, Ien_US
dc.contributor.authorHuber, Ten_US
dc.contributor.authorSanyal, Sen_US
dc.contributor.authorBanerjee, Sen_US
dc.contributor.authorBarré, Pen_US
dc.contributor.authorCanis, Sen_US
dc.contributor.authorWarren, JDen_US
dc.contributor.authorHwa, Jen_US
dc.contributor.authorSakmar, TPen_US
dc.contributor.authorMenon, AKen_US
dc.date.accessioned2013-09-03T04:12:45Z-
dc.date.available2013-09-03T04:12:45Z-
dc.date.issued2011en_US
dc.identifier.citationCurrent Biology, 2011, v. 21 n. 2, p. 149-153en_US
dc.identifier.issn0960-9822en_US
dc.identifier.urihttp://hdl.handle.net/10722/188682-
dc.description.abstractPolar lipids must flip-flop rapidly across biological membranes to sustain cellular life [1, 2], but flipping is energetically costly [3] and its intrinsic rate is low. To overcome this problem, cells have membrane proteins that function as lipid transporters (flippases) to accelerate flipping to a physiologically relevant rate. Flippases that operate at the plasma membrane of eukaryotes, coupling ATP hydrolysis to unidirectional lipid flipping, have been defined at a molecular level [2]. On the other hand, ATP-independent bidirectional flippases that translocate lipids in biogenic compartments, e.g., the endoplasmic reticulum, and specialized membranes, e.g., photoreceptor discs [4, 5], have not been identified even though their activity has been recognized for more than 30 years [1]. Here, we demonstrate that opsin is the ATP-independent phospholipid flippase of photoreceptor discs. We show that reconstitution of opsin into large unilamellar vesicles promotes rapid (τ < 10 s) flipping of phospholipid probes across the vesicle membrane. This is the first molecular identification of an ATP-independent phospholipid flippase in any system. It reveals an unexpected activity for opsin and, in conjunction with recently available structural information on this G protein-coupled receptor [6, 7], significantly advances our understanding of the mechanism of ATP-independent lipid flip-flop. © 2011 Elsevier Ltd All rights reserved.en_US
dc.languageengen_US
dc.publisherCell Press. The Journal's web site is located at http://www.current-biology.com/en_US
dc.relation.ispartofCurrent Biologyen_US
dc.subject.meshAdenosine Triphosphate - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCattleen_US
dc.subject.meshGene Expression Regulationen_US
dc.subject.meshHek293 Cellsen_US
dc.subject.meshHumansen_US
dc.subject.meshMembrane Proteins - Genetics - Metabolismen_US
dc.subject.meshOpsins - Chemistry - Metabolismen_US
dc.subject.meshPhospholipids - Metabolismen_US
dc.subject.meshPhotoreceptor Cells, Vertebrateen_US
dc.titleOpsin is a phospholipid flippaseen_US
dc.typeArticleen_US
dc.identifier.emailSanyal, S: sumana@wi.mit.eduen_US
dc.identifier.authoritySanyal, S=rp01794en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.cub.2010.12.031en_US
dc.identifier.pmid21236677-
dc.identifier.scopuseid_2-s2.0-79151482289en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79151482289&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume21en_US
dc.identifier.issue2en_US
dc.identifier.spage149en_US
dc.identifier.epage153en_US
dc.identifier.isiWOS:000286680800026-
dc.publisher.placeUnited Statesen_US
dc.identifier.f10008602956-
dc.identifier.scopusauthoridMenon, I=7006011410en_US
dc.identifier.scopusauthoridHuber, T=7103351925en_US
dc.identifier.scopusauthoridSanyal, S=16069600000en_US
dc.identifier.scopusauthoridBanerjee, S=55477349600en_US
dc.identifier.scopusauthoridBarré, P=36974210100en_US
dc.identifier.scopusauthoridCanis, S=36738796200en_US
dc.identifier.scopusauthoridWarren, JD=7402212370en_US
dc.identifier.scopusauthoridHwa, J=7005878922en_US
dc.identifier.scopusauthoridSakmar, TP=7005991922en_US
dc.identifier.scopusauthoridMenon, AK=7202324192en_US

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