Regulated nuclear trafficking of rpL10A mediated by NIK1 represents a defense strategy of plant cells against virus.

The NSP-interacting kinase (NIK) receptor-mediated defense pathway has been identified recently as a virulence target of the geminivirus nuclear shuttle protein (NSP). However, the NIK1-NSP interaction does not fit into the elicitor-receptor model of resistance, and hence the molecular mechanism tha...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Claudine M Carvalho, Anésia A Santos, Silvana R Pires, Carolina S Rocha, Daniela I Saraiva, João Paulo B Machado, Eliciane C Mattos, Luciano G Fietto, Elizabeth P B Fontes
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2008
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/33cb0e004f2b4697bd08312d2c1ba945
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:33cb0e004f2b4697bd08312d2c1ba945
record_format	dspace
spelling	oai:doaj.org-article:33cb0e004f2b4697bd08312d2c1ba9452021-11-25T05:47:23ZRegulated nuclear trafficking of rpL10A mediated by NIK1 represents a defense strategy of plant cells against virus.1553-73661553-737410.1371/journal.ppat.1000247https://doaj.org/article/33cb0e004f2b4697bd08312d2c1ba9452008-12-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19112492/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The NSP-interacting kinase (NIK) receptor-mediated defense pathway has been identified recently as a virulence target of the geminivirus nuclear shuttle protein (NSP). However, the NIK1-NSP interaction does not fit into the elicitor-receptor model of resistance, and hence the molecular mechanism that links this antiviral response to receptor activation remains obscure. Here, we identified a ribosomal protein, rpL10A, as a specific partner and substrate of NIK1 that functions as an immediate downstream effector of NIK1-mediated response. Phosphorylation of cytosolic rpL10A by NIK1 redirects the protein to the nucleus where it may act to modulate viral infection. While ectopic expression of normal NIK1 or a hyperactive NIK1 mutant promotes the accumulation of phosphorylated rpL10A within the nuclei, an inactive NIK1 mutant fails to redirect the protein to the nuclei of co-transfected cells. Likewise, a mutant rpL10A defective for NIK1 phosphorylation is not redirected to the nucleus. Furthermore, loss of rpL10A function enhances susceptibility to geminivirus infection, resembling the phenotype of nik1 null alleles. We also provide evidence that geminivirus infection directly interferes with NIK1-mediated nuclear relocalization of rpL10A as a counterdefensive measure. However, the NIK1-mediated defense signaling neither activates RNA silencing nor promotes a hypersensitive response but inhibits plant growth and development. Although the virulence function of the particular geminivirus NSP studied here overcomes this layer of defense in Arabidopsis, the NIK1-mediated signaling response may be involved in restricting the host range of other viruses.Claudine M CarvalhoAnésia A SantosSilvana R PiresCarolina S RochaDaniela I SaraivaJoão Paulo B MachadoEliciane C MattosLuciano G FiettoElizabeth P B FontesPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 4, Iss 12, p e1000247 (2008)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Claudine M Carvalho Anésia A Santos Silvana R Pires Carolina S Rocha Daniela I Saraiva João Paulo B Machado Eliciane C Mattos Luciano G Fietto Elizabeth P B Fontes Regulated nuclear trafficking of rpL10A mediated by NIK1 represents a defense strategy of plant cells against virus.
description	The NSP-interacting kinase (NIK) receptor-mediated defense pathway has been identified recently as a virulence target of the geminivirus nuclear shuttle protein (NSP). However, the NIK1-NSP interaction does not fit into the elicitor-receptor model of resistance, and hence the molecular mechanism that links this antiviral response to receptor activation remains obscure. Here, we identified a ribosomal protein, rpL10A, as a specific partner and substrate of NIK1 that functions as an immediate downstream effector of NIK1-mediated response. Phosphorylation of cytosolic rpL10A by NIK1 redirects the protein to the nucleus where it may act to modulate viral infection. While ectopic expression of normal NIK1 or a hyperactive NIK1 mutant promotes the accumulation of phosphorylated rpL10A within the nuclei, an inactive NIK1 mutant fails to redirect the protein to the nuclei of co-transfected cells. Likewise, a mutant rpL10A defective for NIK1 phosphorylation is not redirected to the nucleus. Furthermore, loss of rpL10A function enhances susceptibility to geminivirus infection, resembling the phenotype of nik1 null alleles. We also provide evidence that geminivirus infection directly interferes with NIK1-mediated nuclear relocalization of rpL10A as a counterdefensive measure. However, the NIK1-mediated defense signaling neither activates RNA silencing nor promotes a hypersensitive response but inhibits plant growth and development. Although the virulence function of the particular geminivirus NSP studied here overcomes this layer of defense in Arabidopsis, the NIK1-mediated signaling response may be involved in restricting the host range of other viruses.
format	article
author	Claudine M Carvalho Anésia A Santos Silvana R Pires Carolina S Rocha Daniela I Saraiva João Paulo B Machado Eliciane C Mattos Luciano G Fietto Elizabeth P B Fontes
author_facet	Claudine M Carvalho Anésia A Santos Silvana R Pires Carolina S Rocha Daniela I Saraiva João Paulo B Machado Eliciane C Mattos Luciano G Fietto Elizabeth P B Fontes
author_sort	Claudine M Carvalho
title	Regulated nuclear trafficking of rpL10A mediated by NIK1 represents a defense strategy of plant cells against virus.
title_short	Regulated nuclear trafficking of rpL10A mediated by NIK1 represents a defense strategy of plant cells against virus.
title_full	Regulated nuclear trafficking of rpL10A mediated by NIK1 represents a defense strategy of plant cells against virus.
title_fullStr	Regulated nuclear trafficking of rpL10A mediated by NIK1 represents a defense strategy of plant cells against virus.
title_full_unstemmed	Regulated nuclear trafficking of rpL10A mediated by NIK1 represents a defense strategy of plant cells against virus.
title_sort	regulated nuclear trafficking of rpl10a mediated by nik1 represents a defense strategy of plant cells against virus.
publisher	Public Library of Science (PLoS)
publishDate	2008
url	https://doaj.org/article/33cb0e004f2b4697bd08312d2c1ba945
work_keys_str_mv	AT claudinemcarvalho regulatednucleartraffickingofrpl10amediatedbynik1representsadefensestrategyofplantcellsagainstvirus AT anesiaasantos regulatednucleartraffickingofrpl10amediatedbynik1representsadefensestrategyofplantcellsagainstvirus AT silvanarpires regulatednucleartraffickingofrpl10amediatedbynik1representsadefensestrategyofplantcellsagainstvirus AT carolinasrocha regulatednucleartraffickingofrpl10amediatedbynik1representsadefensestrategyofplantcellsagainstvirus AT danielaisaraiva regulatednucleartraffickingofrpl10amediatedbynik1representsadefensestrategyofplantcellsagainstvirus AT joaopaulobmachado regulatednucleartraffickingofrpl10amediatedbynik1representsadefensestrategyofplantcellsagainstvirus AT elicianecmattos regulatednucleartraffickingofrpl10amediatedbynik1representsadefensestrategyofplantcellsagainstvirus AT lucianogfietto regulatednucleartraffickingofrpl10amediatedbynik1representsadefensestrategyofplantcellsagainstvirus AT elizabethpbfontes regulatednucleartraffickingofrpl10amediatedbynik1representsadefensestrategyofplantcellsagainstvirus
_version_	1718414451557793792

Regulated nuclear trafficking of rpL10A mediated by NIK1 represents a defense strategy of plant cells against virus.

Ejemplares similares