Cargando…
General and specific promotion of flagellar assembly by a flagellar nucleoside diphosphate kinase
Nucleoside diphosphate kinases (NDKs) play a central role in diverse cellular processes using the canonical NDK activity or alternative mechanisms that remain poorly defined. Our study of dimeric NDK5 in a flagellar motility control complex, the radial spoke (RS), has revealed new modalities. The fl...
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/PMC5662260/ https://www.ncbi.nlm.nih.gov/pubmed/28877983 http://dx.doi.org/10.1091/mbc.E17-03-0156 |
_version_ | 1783274601435889664 |
---|---|
author | Zhu, Xiaoyan Poghosyan, Emiliya Gopal, Radhika Liu, Yi Ciruelas, Kristine S. Maizy, Yousif Diener, Dennis R. King, Stephen M. Ishikawa, Takashi Yang, Pinfen |
author_facet | Zhu, Xiaoyan Poghosyan, Emiliya Gopal, Radhika Liu, Yi Ciruelas, Kristine S. Maizy, Yousif Diener, Dennis R. King, Stephen M. Ishikawa, Takashi Yang, Pinfen |
author_sort | Zhu, Xiaoyan |
collection | PubMed |
description | Nucleoside diphosphate kinases (NDKs) play a central role in diverse cellular processes using the canonical NDK activity or alternative mechanisms that remain poorly defined. Our study of dimeric NDK5 in a flagellar motility control complex, the radial spoke (RS), has revealed new modalities. The flagella in Chlamydomonas ndk5 mutant were paralyzed, albeit only deficient in three RS subunits. RS morphology appeared severely changed in averaged cryo-electron tomograms, suggesting that NDK5 is crucial for the intact spokehead formation as well as RS structural stability. Intriguingly, ndk5’s flagella were also short, resembling those of an allelic spoke-less mutant. All ndk5’s phenotypes were rescued by expressions of NDK5 or a mutated NDK5 lacking the canonical kinase activity. Importantly, the mutated NDK5 that appeared fully functional in ndk5 cells elicited a dominant-negative effect in wild-type cells, causing paralyzed short flagella with hypophosphorylated, less abundant, but intact RSs, and accumulated hypophosphorylated NDK5 in the cell body. We propose that NDK5 dimer is an RS structural subunit with an additional mechanism that uses cross-talk between the two NDK monomers to accelerate phosphorylation-related assembly of RSs and entire flagella. |
format | Online Article Text |
id | pubmed-5662260 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-56622602018-01-16 General and specific promotion of flagellar assembly by a flagellar nucleoside diphosphate kinase Zhu, Xiaoyan Poghosyan, Emiliya Gopal, Radhika Liu, Yi Ciruelas, Kristine S. Maizy, Yousif Diener, Dennis R. King, Stephen M. Ishikawa, Takashi Yang, Pinfen Mol Biol Cell Articles Nucleoside diphosphate kinases (NDKs) play a central role in diverse cellular processes using the canonical NDK activity or alternative mechanisms that remain poorly defined. Our study of dimeric NDK5 in a flagellar motility control complex, the radial spoke (RS), has revealed new modalities. The flagella in Chlamydomonas ndk5 mutant were paralyzed, albeit only deficient in three RS subunits. RS morphology appeared severely changed in averaged cryo-electron tomograms, suggesting that NDK5 is crucial for the intact spokehead formation as well as RS structural stability. Intriguingly, ndk5’s flagella were also short, resembling those of an allelic spoke-less mutant. All ndk5’s phenotypes were rescued by expressions of NDK5 or a mutated NDK5 lacking the canonical kinase activity. Importantly, the mutated NDK5 that appeared fully functional in ndk5 cells elicited a dominant-negative effect in wild-type cells, causing paralyzed short flagella with hypophosphorylated, less abundant, but intact RSs, and accumulated hypophosphorylated NDK5 in the cell body. We propose that NDK5 dimer is an RS structural subunit with an additional mechanism that uses cross-talk between the two NDK monomers to accelerate phosphorylation-related assembly of RSs and entire flagella. The American Society for Cell Biology 2017-11-01 /pmc/articles/PMC5662260/ /pubmed/28877983 http://dx.doi.org/10.1091/mbc.E17-03-0156 Text en © 2017 Zhu 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 Zhu, Xiaoyan Poghosyan, Emiliya Gopal, Radhika Liu, Yi Ciruelas, Kristine S. Maizy, Yousif Diener, Dennis R. King, Stephen M. Ishikawa, Takashi Yang, Pinfen General and specific promotion of flagellar assembly by a flagellar nucleoside diphosphate kinase |
title | General and specific promotion of flagellar assembly by a flagellar nucleoside diphosphate kinase |
title_full | General and specific promotion of flagellar assembly by a flagellar nucleoside diphosphate kinase |
title_fullStr | General and specific promotion of flagellar assembly by a flagellar nucleoside diphosphate kinase |
title_full_unstemmed | General and specific promotion of flagellar assembly by a flagellar nucleoside diphosphate kinase |
title_short | General and specific promotion of flagellar assembly by a flagellar nucleoside diphosphate kinase |
title_sort | general and specific promotion of flagellar assembly by a flagellar nucleoside diphosphate kinase |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5662260/ https://www.ncbi.nlm.nih.gov/pubmed/28877983 http://dx.doi.org/10.1091/mbc.E17-03-0156 |
work_keys_str_mv | AT zhuxiaoyan generalandspecificpromotionofflagellarassemblybyaflagellarnucleosidediphosphatekinase AT poghosyanemiliya generalandspecificpromotionofflagellarassemblybyaflagellarnucleosidediphosphatekinase AT gopalradhika generalandspecificpromotionofflagellarassemblybyaflagellarnucleosidediphosphatekinase AT liuyi generalandspecificpromotionofflagellarassemblybyaflagellarnucleosidediphosphatekinase AT ciruelaskristines generalandspecificpromotionofflagellarassemblybyaflagellarnucleosidediphosphatekinase AT maizyyousif generalandspecificpromotionofflagellarassemblybyaflagellarnucleosidediphosphatekinase AT dienerdennisr generalandspecificpromotionofflagellarassemblybyaflagellarnucleosidediphosphatekinase AT kingstephenm generalandspecificpromotionofflagellarassemblybyaflagellarnucleosidediphosphatekinase AT ishikawatakashi generalandspecificpromotionofflagellarassemblybyaflagellarnucleosidediphosphatekinase AT yangpinfen generalandspecificpromotionofflagellarassemblybyaflagellarnucleosidediphosphatekinase |