File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1016/j.cub.2010.12.031
- Scopus: eid_2-s2.0-79151482289
- PMID: 21236677
- WOS: WOS:000286680800026
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Opsin is a phospholipid flippase
Title | Opsin is a phospholipid flippase |
---|---|
Authors | |
Issue Date | 2011 |
Publisher | Cell 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? |
Abstract | Polar 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 Identifier | http://hdl.handle.net/10722/188682 |
ISSN | 2023 Impact Factor: 8.1 2023 SCImago Journal Rankings: 2.982 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Menon, I | en_US |
dc.contributor.author | Huber, T | en_US |
dc.contributor.author | Sanyal, S | en_US |
dc.contributor.author | Banerjee, S | en_US |
dc.contributor.author | Barré, P | en_US |
dc.contributor.author | Canis, S | en_US |
dc.contributor.author | Warren, JD | en_US |
dc.contributor.author | Hwa, J | en_US |
dc.contributor.author | Sakmar, TP | en_US |
dc.contributor.author | Menon, AK | en_US |
dc.date.accessioned | 2013-09-03T04:12:45Z | - |
dc.date.available | 2013-09-03T04:12:45Z | - |
dc.date.issued | 2011 | en_US |
dc.identifier.citation | Current Biology, 2011, v. 21 n. 2, p. 149-153 | en_US |
dc.identifier.issn | 0960-9822 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/188682 | - |
dc.description.abstract | Polar 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.language | eng | en_US |
dc.publisher | Cell Press. The Journal's web site is located at http://www.current-biology.com/ | en_US |
dc.relation.ispartof | Current Biology | en_US |
dc.subject.mesh | Adenosine Triphosphate - Metabolism | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Cattle | en_US |
dc.subject.mesh | Gene Expression Regulation | en_US |
dc.subject.mesh | Hek293 Cells | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Membrane Proteins - Genetics - Metabolism | en_US |
dc.subject.mesh | Opsins - Chemistry - Metabolism | en_US |
dc.subject.mesh | Phospholipids - Metabolism | en_US |
dc.subject.mesh | Photoreceptor Cells, Vertebrate | en_US |
dc.title | Opsin is a phospholipid flippase | en_US |
dc.type | Article | en_US |
dc.identifier.email | Sanyal, S: sumana@wi.mit.edu | en_US |
dc.identifier.authority | Sanyal, S=rp01794 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1016/j.cub.2010.12.031 | en_US |
dc.identifier.pmid | 21236677 | - |
dc.identifier.scopus | eid_2-s2.0-79151482289 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-79151482289&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 21 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.spage | 149 | en_US |
dc.identifier.epage | 153 | en_US |
dc.identifier.isi | WOS:000286680800026 | - |
dc.publisher.place | United States | en_US |
dc.identifier.f1000 | 8602956 | - |
dc.identifier.scopusauthorid | Menon, I=7006011410 | en_US |
dc.identifier.scopusauthorid | Huber, T=7103351925 | en_US |
dc.identifier.scopusauthorid | Sanyal, S=16069600000 | en_US |
dc.identifier.scopusauthorid | Banerjee, S=55477349600 | en_US |
dc.identifier.scopusauthorid | Barré, P=36974210100 | en_US |
dc.identifier.scopusauthorid | Canis, S=36738796200 | en_US |
dc.identifier.scopusauthorid | Warren, JD=7402212370 | en_US |
dc.identifier.scopusauthorid | Hwa, J=7005878922 | en_US |
dc.identifier.scopusauthorid | Sakmar, TP=7005991922 | en_US |
dc.identifier.scopusauthorid | Menon, AK=7202324192 | en_US |
dc.identifier.issnl | 0960-9822 | - |