Cargando…

RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly

Proteins localized to the basal body and the centrosome play crucial roles in ciliary assembly and function. Although RABL2 and CEP19 are conserved in ciliated organisms and have been implicated in ciliary/flagellar functions, their roles are poorly understood. Here we show that RABL2 interacts with...

Descripción completa

Detalles Bibliográficos
Autores principales: Nishijima, Yuya, Hagiya, Yohei, Kubo, Tomohiro, Takei, Ryota, Katoh, Yohei, Nakayama, Kazuhisa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5469608/
https://www.ncbi.nlm.nih.gov/pubmed/28428259
http://dx.doi.org/10.1091/mbc.E17-01-0017
_version_ 1783243609194102784
author Nishijima, Yuya
Hagiya, Yohei
Kubo, Tomohiro
Takei, Ryota
Katoh, Yohei
Nakayama, Kazuhisa
author_facet Nishijima, Yuya
Hagiya, Yohei
Kubo, Tomohiro
Takei, Ryota
Katoh, Yohei
Nakayama, Kazuhisa
author_sort Nishijima, Yuya
collection PubMed
description Proteins localized to the basal body and the centrosome play crucial roles in ciliary assembly and function. Although RABL2 and CEP19 are conserved in ciliated organisms and have been implicated in ciliary/flagellar functions, their roles are poorly understood. Here we show that RABL2 interacts with CEP19 and is recruited to the mother centriole and basal body in a CEP19-dependent manner and that CEP19 is recruited to the centriole probably via its binding to the centrosomal protein FGFR1OP. Disruption of the RABL2 gene in Chlamydomonas reinhardtii results in the nonflagellated phenotype, suggesting a crucial role of RABL2 in ciliary/flagellar assembly. We also show that RABL2 interacts, in its GTP-bound state, with the intraflagellar transport (IFT)-B complex via the IFT74–IFT81 heterodimer and that the interaction is disrupted by a mutation found in male infertile mice (Mot mice) with a sperm flagella motility defect. Intriguingly, RABL2 binds to CEP19 and the IFT74–IFT81 heterodimer in a mutually exclusive manner. Furthermore, exogenous expression of the GDP-locked or Mot-type RABL2 mutant in human cells results in mild defects in ciliary assembly. These results indicate that RABL2 localized to the basal body plays crucial roles in ciliary/flagellar assembly via its interaction with the IFT-B complex.
format Online
Article
Text
id pubmed-5469608
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher The American Society for Cell Biology
record_format MEDLINE/PubMed
spelling pubmed-54696082017-08-30 RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly Nishijima, Yuya Hagiya, Yohei Kubo, Tomohiro Takei, Ryota Katoh, Yohei Nakayama, Kazuhisa Mol Biol Cell Articles Proteins localized to the basal body and the centrosome play crucial roles in ciliary assembly and function. Although RABL2 and CEP19 are conserved in ciliated organisms and have been implicated in ciliary/flagellar functions, their roles are poorly understood. Here we show that RABL2 interacts with CEP19 and is recruited to the mother centriole and basal body in a CEP19-dependent manner and that CEP19 is recruited to the centriole probably via its binding to the centrosomal protein FGFR1OP. Disruption of the RABL2 gene in Chlamydomonas reinhardtii results in the nonflagellated phenotype, suggesting a crucial role of RABL2 in ciliary/flagellar assembly. We also show that RABL2 interacts, in its GTP-bound state, with the intraflagellar transport (IFT)-B complex via the IFT74–IFT81 heterodimer and that the interaction is disrupted by a mutation found in male infertile mice (Mot mice) with a sperm flagella motility defect. Intriguingly, RABL2 binds to CEP19 and the IFT74–IFT81 heterodimer in a mutually exclusive manner. Furthermore, exogenous expression of the GDP-locked or Mot-type RABL2 mutant in human cells results in mild defects in ciliary assembly. These results indicate that RABL2 localized to the basal body plays crucial roles in ciliary/flagellar assembly via its interaction with the IFT-B complex. The American Society for Cell Biology 2017-06-15 /pmc/articles/PMC5469608/ /pubmed/28428259 http://dx.doi.org/10.1091/mbc.E17-01-0017 Text en © 2017 Nishijima, Hagiya, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Nishijima, Yuya
Hagiya, Yohei
Kubo, Tomohiro
Takei, Ryota
Katoh, Yohei
Nakayama, Kazuhisa
RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly
title RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly
title_full RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly
title_fullStr RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly
title_full_unstemmed RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly
title_short RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly
title_sort rabl2 interacts with the intraflagellar transport-b complex and cep19 and participates in ciliary assembly
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5469608/
https://www.ncbi.nlm.nih.gov/pubmed/28428259
http://dx.doi.org/10.1091/mbc.E17-01-0017
work_keys_str_mv AT nishijimayuya rabl2interactswiththeintraflagellartransportbcomplexandcep19andparticipatesinciliaryassembly
AT hagiyayohei rabl2interactswiththeintraflagellartransportbcomplexandcep19andparticipatesinciliaryassembly
AT kubotomohiro rabl2interactswiththeintraflagellartransportbcomplexandcep19andparticipatesinciliaryassembly
AT takeiryota rabl2interactswiththeintraflagellartransportbcomplexandcep19andparticipatesinciliaryassembly
AT katohyohei rabl2interactswiththeintraflagellartransportbcomplexandcep19andparticipatesinciliaryassembly
AT nakayamakazuhisa rabl2interactswiththeintraflagellartransportbcomplexandcep19andparticipatesinciliaryassembly