Cryo-EM of retinoschisin branched networks suggests an intercellular adhesive scaffold in the retina
Identifieur interne : 002072 ( Ncbi/Merge ); précédent : 002071; suivant : 002073Cryo-EM of retinoschisin branched networks suggests an intercellular adhesive scaffold in the retina
Auteurs : J. Bernard Heymann ; Camasamudram Vijayasarathy ; Rick K. Huang ; Altaira D. Dearborn ; Paul A. Sieving ; Alasdair C. StevenSource :
- The Journal of Cell Biology [ 0021-9525 ] ; 2019.
Descripteurs français
- KwdFr :
- Cellules HEK293, Cryomicroscopie électronique, Humains, Mutation, Mâle, Protéines de l'oeil (génétique), Protéines de l'oeil (métabolisme), Rétine (métabolisme), Rétine (ultrastructure), Rétinoschisis (anatomopathologie), Rétinoschisis (génétique), Rétinoschisis (métabolisme), Structure secondaire des protéines.
- MESH :
- anatomopathologie : Rétinoschisis.
- génétique : Protéines de l'oeil, Rétinoschisis.
- métabolisme : Protéines de l'oeil, Rétine, Rétinoschisis.
- ultrastructure : Cellules HEK293, Cryomicroscopie électronique, Humains, Mutation, Mâle, Rétine, Structure secondaire des protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Eye Proteins.
- chemical , metabolism : Eye Proteins.
- genetics : Retinoschisis.
- metabolism : Retina, Retinoschisis.
- pathology : Retinoschisis.
- ultrastructure : Retina.
- Cryoelectron Microscopy, HEK293 Cells, Humans, Male, Mutation, Protein Structure, Secondary.
Abstract
Mutations in the essential retinal protein retinoschisin (RS1) cause a form of macular degeneration. Heymann et al. use cryo-EM to show that RS1 assembles into branched networks that may play a stabilizing role in maintaining the integrity of the retina.
Url:
DOI: 10.1083/jcb.201806148
PubMed: 30630865
PubMed Central: 6400569
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PMC:6400569Le document en format XML
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<front><div type="abstract" xml:lang="en"><p>Mutations in the essential retinal protein retinoschisin (RS1) cause a form of macular degeneration. Heymann et al. use cryo-EM to show that RS1 assembles into branched networks that may play a stabilizing role in maintaining the integrity of the retina.</p>
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<double pmid="30630865"><pmc><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Cryo-EM of retinoschisin branched networks suggests an intercellular adhesive scaffold in the retina</title>
<author><name sortKey="Heymann, J Bernard" sort="Heymann, J Bernard" uniqKey="Heymann J" first="J. Bernard" last="Heymann">J. Bernard Heymann</name>
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<author><name sortKey="Vijayasarathy, Camasamudram" sort="Vijayasarathy, Camasamudram" uniqKey="Vijayasarathy C" first="Camasamudram" last="Vijayasarathy">Camasamudram Vijayasarathy</name>
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<author><name sortKey="Huang, Rick K" sort="Huang, Rick K" uniqKey="Huang R" first="Rick K." last="Huang">Rick K. Huang</name>
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<author><name sortKey="Sieving, Paul A" sort="Sieving, Paul A" uniqKey="Sieving P" first="Paul A." last="Sieving">Paul A. Sieving</name>
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<author><name sortKey="Steven, Alasdair C" sort="Steven, Alasdair C" uniqKey="Steven A" first="Alasdair C." last="Steven">Alasdair C. Steven</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Cryo-EM of retinoschisin branched networks suggests an intercellular adhesive scaffold in the retina</title>
<author><name sortKey="Heymann, J Bernard" sort="Heymann, J Bernard" uniqKey="Heymann J" first="J. Bernard" last="Heymann">J. Bernard Heymann</name>
<affiliation><nlm:aff id="aff1"><institution>Laboratory for Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD</institution>
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<series><title level="j">The Journal of Cell Biology</title>
<idno type="ISSN">0021-9525</idno>
<idno type="eISSN">1540-8140</idno>
<imprint><date when="2019">2019</date>
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<front><div type="abstract" xml:lang="en"><p>Mutations in the essential retinal protein retinoschisin (RS1) cause a form of macular degeneration. Heymann et al. use cryo-EM to show that RS1 assembles into branched networks that may play a stabilizing role in maintaining the integrity of the retina.</p>
</div>
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<placeName><region type="state">Maryland</region>
</placeName>
<wicri:cityArea>Section on Translational Research for Retinal and Macular Degeneration, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Huang, Rick K" sort="Huang, Rick K" uniqKey="Huang R" first="Rick K" last="Huang">Rick K. Huang</name>
<affiliation wicri:level="2"><nlm:affiliation>Cryo-Electron Microscopy Facility, Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Virginie</region>
</placeName>
<wicri:cityArea>Cryo-Electron Microscopy Facility, Janelia Research Campus, Howard Hughes Medical Institute, Ashburn</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Dearborn, Altaira D" sort="Dearborn, Altaira D" uniqKey="Dearborn A" first="Altaira D" last="Dearborn">Altaira D. Dearborn</name>
<affiliation wicri:level="2"><nlm:affiliation>Laboratory for Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Maryland</region>
</placeName>
<wicri:cityArea>Laboratory for Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Sieving, Paul A" sort="Sieving, Paul A" uniqKey="Sieving P" first="Paul A" last="Sieving">Paul A. Sieving</name>
<affiliation wicri:level="2"><nlm:affiliation>Section on Translational Research for Retinal and Macular Degeneration, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Maryland</region>
</placeName>
<wicri:cityArea>Section on Translational Research for Retinal and Macular Degeneration, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Steven, Alasdair C" sort="Steven, Alasdair C" uniqKey="Steven A" first="Alasdair C" last="Steven">Alasdair C. Steven</name>
<affiliation wicri:level="2"><nlm:affiliation>Laboratory for Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Maryland</region>
</placeName>
<wicri:cityArea>Laboratory for Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda</wicri:cityArea>
</affiliation>
</author>
</analytic>
<series><title level="j">The Journal of cell biology</title>
<idno type="eISSN">1540-8140</idno>
<imprint><date when="2019" type="published">2019</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cryoelectron Microscopy</term>
<term>Eye Proteins (genetics)</term>
<term>Eye Proteins (metabolism)</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Male</term>
<term>Mutation</term>
<term>Protein Structure, Secondary</term>
<term>Retina (metabolism)</term>
<term>Retina (ultrastructure)</term>
<term>Retinoschisis (genetics)</term>
<term>Retinoschisis (metabolism)</term>
<term>Retinoschisis (pathology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HEK293</term>
<term>Cryomicroscopie électronique</term>
<term>Humains</term>
<term>Mutation</term>
<term>Mâle</term>
<term>Protéines de l'oeil (génétique)</term>
<term>Protéines de l'oeil (métabolisme)</term>
<term>Rétine (métabolisme)</term>
<term>Rétine (ultrastructure)</term>
<term>Rétinoschisis (anatomopathologie)</term>
<term>Rétinoschisis (génétique)</term>
<term>Rétinoschisis (métabolisme)</term>
<term>Structure secondaire des protéines</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Eye Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Eye Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Rétinoschisis</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Retinoschisis</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de l'oeil</term>
<term>Rétinoschisis</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Retina</term>
<term>Retinoschisis</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines de l'oeil</term>
<term>Rétine</term>
<term>Rétinoschisis</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Retinoschisis</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Retina</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Cryoelectron Microscopy</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Male</term>
<term>Mutation</term>
<term>Protein Structure, Secondary</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Cellules HEK293</term>
<term>Cryomicroscopie électronique</term>
<term>Humains</term>
<term>Mutation</term>
<term>Mâle</term>
<term>Rétine</term>
<term>Structure secondaire des protéines</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Mutations in the retinal protein retinoschisin (RS1) cause progressive loss of vision in young males, a form of macular degeneration called X-linked retinoschisis (XLRS). We previously solved the structure of RS1, a 16-mer composed of paired back-to-back octameric rings. Here, we show by cryo-electron microscopy that RS1 16-mers can assemble into extensive branched networks. We classified the different configurations, finding four types of interaction between the RS1 molecules. The predominant configuration is a linear strand with a wavy appearance. Three less frequent types constitute the branch points of the network. In all cases, the "spikes" around the periphery of the double rings are involved in these interactions. In the linear strand, a loop (usually referred to as spike 1) occurs on both sides of the interface between neighboring molecules. Mutations in this loop suppress secretion, indicating the possibility of intracellular higher-order assembly. These observations suggest that branched networks of RS1 may play a stabilizing role in maintaining the integrity of the retina.</div>
</front>
</TEI>
</pubmed>
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