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...
Autores principales: | , , , , , |
---|---|
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 |