Cryo-EM of retinoschisin branched networks suggests an intercellular adhesive scaffold in the retina
Identifieur interne : 000642 ( Main/Exploration ); précédent : 000641; suivant : 000643Cryo-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
Affiliations:
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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></nlm:aff></affiliation></author><author><name sortKey="Vijayasarathy, Camasamudram" sort="Vijayasarathy, Camasamudram" uniqKey="Vijayasarathy C" first="Camasamudram" last="Vijayasarathy">Camasamudram Vijayasarathy</name><affiliation><nlm:aff id="aff2"><institution>Section on Translational Research for Retinal and Macular Degeneration, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD</institution></nlm:aff></affiliation></author><author><name sortKey="Huang, Rick K" sort="Huang, Rick K" uniqKey="Huang R" first="Rick K." last="Huang">Rick K. 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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></nlm:aff></affiliation></author><author><name sortKey="Vijayasarathy, Camasamudram" sort="Vijayasarathy, Camasamudram" uniqKey="Vijayasarathy C" first="Camasamudram" last="Vijayasarathy">Camasamudram Vijayasarathy</name><affiliation><nlm:aff id="aff2"><institution>Section on Translational Research for Retinal and Macular Degeneration, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD</institution></nlm:aff></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><nlm:aff id="aff3"><institution>Cryo-Electron Microscopy Facility, Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA</institution></nlm:aff></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><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></nlm:aff></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><nlm:aff id="aff2"><institution>Section on Translational Research for Retinal and Macular Degeneration, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD</institution></nlm:aff></affiliation><affiliation><nlm:aff id="aff4"><institution>National Eye Institute, National Institutes of Health, Bethesda, MD</institution></nlm:aff></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><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></nlm:aff></affiliation></author></analytic><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></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"><p>Mutations in the essential retinal protein retinoschisin (RS1) cause a form of macular degeneration. 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Zrenner</name></author><author><name sortKey="Fischer, M D" uniqKey="Fischer M">M.D. Fischer</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Dearborn, Altaira D" sort="Dearborn, Altaira D" uniqKey="Dearborn A" first="Altaira D." last="Dearborn">Altaira D. Dearborn</name><name sortKey="Heymann, J Bernard" sort="Heymann, J Bernard" uniqKey="Heymann J" first="J. Bernard" last="Heymann">J. Bernard Heymann</name><name sortKey="Huang, Rick K" sort="Huang, Rick K" uniqKey="Huang R" first="Rick K." last="Huang">Rick K. Huang</name><name sortKey="Sieving, Paul A" sort="Sieving, Paul A" uniqKey="Sieving P" first="Paul A." last="Sieving">Paul A. Sieving</name><name sortKey="Steven, Alasdair C" sort="Steven, Alasdair C" uniqKey="Steven A" first="Alasdair C." last="Steven">Alasdair C. Steven</name><name sortKey="Vijayasarathy, Camasamudram" sort="Vijayasarathy, Camasamudram" uniqKey="Vijayasarathy C" first="Camasamudram" last="Vijayasarathy">Camasamudram Vijayasarathy</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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