Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants

Arrestins constitute a family of small cytoplasmic proteins that mediate deactivation of G-protein-coupled receptors (GPCRs) and are known to be essential for cascade inactivation and receptor desensitization. Alternative splicing produces an array of arrestin gene products that have widely differen...

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Autores: Burns, Marie E., Méndez Zunzunegui, Ana, Chen, Ching-Kang, Almuete, Aileen, Quillinan, Nidia, Simon, Melvin I., Baylor, Denis A., Chen, Jeannie
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2006
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/175910
Acceso en línea:https://hdl.handle.net/2445/175910
Access Level:acceso abierto
Palabra clave:Fisiologia
Genètica
Metabolisme
Physiology
Genetics
Metabolism
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spelling Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variantsBurns, Marie E.Méndez Zunzunegui, AnaChen, Ching-KangAlmuete, AileenQuillinan, NidiaSimon, Melvin I.Baylor, Denis A.Chen, JeannieFisiologiaGenèticaMetabolismePhysiologyGeneticsMetabolismArrestins constitute a family of small cytoplasmic proteins that mediate deactivation of G-protein-coupled receptors (GPCRs) and are known to be essential for cascade inactivation and receptor desensitization. Alternative splicing produces an array of arrestin gene products that have widely different specificities for their cognate receptors in vitro, but the differential functions of these splice variants in vivo are essentially unknown. Bovine rod photoreceptors express two splice variants of visual arrestin (p44 and p48) that display different affinities for the GPCR rhodopsin. To determine the functions of these splice variants in intact cells, we expressed a transgene encoding either a truncated form of murine arrestin (mArr(1-369), or m44) or the long (p48) isoform in mouse rods lacking endogenous arrestin (Arr-/-). Morphological analysis showed that expression of either variant attenuated the light-induced degeneration that is thought to result from excessive cascade activity in Arr-/-rods. Suction electrode recordings from individual rods indicated that the expression of either m44 or p48 splice variants could restore normal kinetics to Arr-/- dim flash responses, indicating that both isoforms can bind to and quench phosphorylated rhodopsin rapidly. To our surprise, only the full-length variant was able to alter the kinetics of responses in rods lacking both arrestin and rhodopsin kinase, indicating that p48 can also quench the activity of nonphosphorylated rhodopsin.The Society for Neuroscience2006info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/175910Articles publicats en revistes (Ciències Fisiològiques)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.1523/JNEUROSCI.3301-05.2006Journal of Neuroscience, 2006, vol. 26, num. 3, p. 1036-1044https://doi.org/10.1523/JNEUROSCI.3301-05.2006cc-by-nc-sa (c) Burns, Marie E. et al., 2006http://creativecommons.org/licenses/by-nc-sa/3.0/esinfo:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1759102026-05-27T06:46:51Z
dc.title.none.fl_str_mv Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants
title Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants
spellingShingle Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants
Burns, Marie E.
Fisiologia
Genètica
Metabolisme
Physiology
Genetics
Metabolism
title_short Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants
title_full Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants
title_fullStr Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants
title_full_unstemmed Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants
title_sort Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants
dc.creator.none.fl_str_mv Burns, Marie E.
Méndez Zunzunegui, Ana
Chen, Ching-Kang
Almuete, Aileen
Quillinan, Nidia
Simon, Melvin I.
Baylor, Denis A.
Chen, Jeannie
author Burns, Marie E.
author_facet Burns, Marie E.
Méndez Zunzunegui, Ana
Chen, Ching-Kang
Almuete, Aileen
Quillinan, Nidia
Simon, Melvin I.
Baylor, Denis A.
Chen, Jeannie
author_role author
author2 Méndez Zunzunegui, Ana
Chen, Ching-Kang
Almuete, Aileen
Quillinan, Nidia
Simon, Melvin I.
Baylor, Denis A.
Chen, Jeannie
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Fisiologia
Genètica
Metabolisme
Physiology
Genetics
Metabolism
topic Fisiologia
Genètica
Metabolisme
Physiology
Genetics
Metabolism
description Arrestins constitute a family of small cytoplasmic proteins that mediate deactivation of G-protein-coupled receptors (GPCRs) and are known to be essential for cascade inactivation and receptor desensitization. Alternative splicing produces an array of arrestin gene products that have widely different specificities for their cognate receptors in vitro, but the differential functions of these splice variants in vivo are essentially unknown. Bovine rod photoreceptors express two splice variants of visual arrestin (p44 and p48) that display different affinities for the GPCR rhodopsin. To determine the functions of these splice variants in intact cells, we expressed a transgene encoding either a truncated form of murine arrestin (mArr(1-369), or m44) or the long (p48) isoform in mouse rods lacking endogenous arrestin (Arr-/-). Morphological analysis showed that expression of either variant attenuated the light-induced degeneration that is thought to result from excessive cascade activity in Arr-/-rods. Suction electrode recordings from individual rods indicated that the expression of either m44 or p48 splice variants could restore normal kinetics to Arr-/- dim flash responses, indicating that both isoforms can bind to and quench phosphorylated rhodopsin rapidly. To our surprise, only the full-length variant was able to alter the kinetics of responses in rods lacking both arrestin and rhodopsin kinase, indicating that p48 can also quench the activity of nonphosphorylated rhodopsin.
publishDate 2006
dc.date.none.fl_str_mv 2006
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/175910
url https://hdl.handle.net/2445/175910
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.1523/JNEUROSCI.3301-05.2006
Journal of Neuroscience, 2006, vol. 26, num. 3, p. 1036-1044
https://doi.org/10.1523/JNEUROSCI.3301-05.2006
dc.rights.none.fl_str_mv cc-by-nc-sa (c) Burns, Marie E. et al., 2006
http://creativecommons.org/licenses/by-nc-sa/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by-nc-sa (c) Burns, Marie E. et al., 2006
http://creativecommons.org/licenses/by-nc-sa/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv The Society for Neuroscience
publisher.none.fl_str_mv The Society for Neuroscience
dc.source.none.fl_str_mv Articles publicats en revistes (Ciències Fisiològiques)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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