Dimerization deficiency of enigmatic retinitis pigmentosa-linked rhodopsin mutants

Retinitis pigmentosa is often caused by mutations that affect the activity or transport of rhodopsin, but some mutations cause disease even though an apparently functional protein is produced. Here the authors show that three such enigmatic mutants retain scramblase activity but are unable to dimeri...

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Main Authors: Birgit Ploier, Lydia N. Caro, Takefumi Morizumi, Kalpana Pandey, Jillian N. Pearring, Michael A. Goren, Silvia C. Finnemann, Johannes Graumann, Vadim Y. Arshavsky, Jeremy S. Dittman, Oliver P. Ernst, Anant K. Menon
Format: Article
Language:English
Published: Nature Publishing Group 2016-10-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms12832
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spelling doaj-94c82e6657484b44baee46822dc7c91b2021-05-11T10:34:51ZengNature Publishing GroupNature Communications2041-17232016-10-017111110.1038/ncomms12832Dimerization deficiency of enigmatic retinitis pigmentosa-linked rhodopsin mutantsBirgit Ploier0Lydia N. Caro1Takefumi Morizumi2Kalpana Pandey3Jillian N. Pearring4Michael A. Goren5Silvia C. Finnemann6Johannes Graumann7Vadim Y. Arshavsky8Jeremy S. Dittman9Oliver P. Ernst10Anant K. Menon11Department of Biochemistry, Weill Cornell Medical CollegeDepartment of Biochemistry, University of TorontoDepartment of Biochemistry, University of TorontoDepartment of Biochemistry, Weill Cornell Medical CollegeDepartment of Ophthalmology, Duke University Medical CenterDepartment of Biochemistry, Weill Cornell Medical CollegeDepartment of Biological Sciences, Center for Cancer, Genetic Diseases and Gene Regulation, Fordham UniversityDepartment of Biochemistry, Weill Cornell Medical CollegeDepartment of Ophthalmology, Duke University Medical CenterDepartment of Biochemistry, Weill Cornell Medical CollegeDepartment of Biochemistry, University of TorontoDepartment of Biochemistry, Weill Cornell Medical CollegeRetinitis pigmentosa is often caused by mutations that affect the activity or transport of rhodopsin, but some mutations cause disease even though an apparently functional protein is produced. Here the authors show that three such enigmatic mutants retain scramblase activity but are unable to dimerize.https://doi.org/10.1038/ncomms12832
collection DOAJ
language English
format Article
sources DOAJ
author Birgit Ploier
Lydia N. Caro
Takefumi Morizumi
Kalpana Pandey
Jillian N. Pearring
Michael A. Goren
Silvia C. Finnemann
Johannes Graumann
Vadim Y. Arshavsky
Jeremy S. Dittman
Oliver P. Ernst
Anant K. Menon
spellingShingle Birgit Ploier
Lydia N. Caro
Takefumi Morizumi
Kalpana Pandey
Jillian N. Pearring
Michael A. Goren
Silvia C. Finnemann
Johannes Graumann
Vadim Y. Arshavsky
Jeremy S. Dittman
Oliver P. Ernst
Anant K. Menon
Dimerization deficiency of enigmatic retinitis pigmentosa-linked rhodopsin mutants
Nature Communications
author_facet Birgit Ploier
Lydia N. Caro
Takefumi Morizumi
Kalpana Pandey
Jillian N. Pearring
Michael A. Goren
Silvia C. Finnemann
Johannes Graumann
Vadim Y. Arshavsky
Jeremy S. Dittman
Oliver P. Ernst
Anant K. Menon
author_sort Birgit Ploier
title Dimerization deficiency of enigmatic retinitis pigmentosa-linked rhodopsin mutants
title_short Dimerization deficiency of enigmatic retinitis pigmentosa-linked rhodopsin mutants
title_full Dimerization deficiency of enigmatic retinitis pigmentosa-linked rhodopsin mutants
title_fullStr Dimerization deficiency of enigmatic retinitis pigmentosa-linked rhodopsin mutants
title_full_unstemmed Dimerization deficiency of enigmatic retinitis pigmentosa-linked rhodopsin mutants
title_sort dimerization deficiency of enigmatic retinitis pigmentosa-linked rhodopsin mutants
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2016-10-01
description Retinitis pigmentosa is often caused by mutations that affect the activity or transport of rhodopsin, but some mutations cause disease even though an apparently functional protein is produced. Here the authors show that three such enigmatic mutants retain scramblase activity but are unable to dimerize.
url https://doi.org/10.1038/ncomms12832
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