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Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility
Light chain 1 (LC1) is a highly conserved leucine-rich repeat protein associated with the microtubule-binding domain of the Chlamydomonas outer–dynein arm γ heavy chain. LC1 mutations in humans and trypanosomes lead to motility defects, while its loss in oomycetes results in aciliate zoospores. Here...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10295483/ https://www.ncbi.nlm.nih.gov/pubmed/37133971 http://dx.doi.org/10.1091/mbc.E23-03-0104 |
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author | Sakato-Antoku, Miho King, Stephen M. |
author_facet | Sakato-Antoku, Miho King, Stephen M. |
author_sort | Sakato-Antoku, Miho |
collection | PubMed |
description | Light chain 1 (LC1) is a highly conserved leucine-rich repeat protein associated with the microtubule-binding domain of the Chlamydomonas outer–dynein arm γ heavy chain. LC1 mutations in humans and trypanosomes lead to motility defects, while its loss in oomycetes results in aciliate zoospores. Here we describe a Chlamydomonas LC1 null mutant (dlu1-1). This strain has reduced swimming velocity and beat frequency, can undergo waveform conversion, but often exhibits loss of hydrodynamic coupling between the cilia. Following deciliation, Chlamydomonas cells rapidly rebuild cytoplasmic stocks of axonemal dyneins. Loss of LC1 disrupts the kinetics of this cytoplasmic preassembly so that most outer-arm dynein heavy chains remain monomeric even after several hours. This suggests that association of LC1 with its heavy chain–binding site is a key step or checkpoint in the outer-arm dynein assembly process. Similarly to strains lacking the entire outer arm and inner arm I1/f, we found that loss of LC1 and I1/f in dlu1-1 ida1 double mutants resulted in cells unable to build cilia under normal conditions. Furthermore, dlu1-1 cells do not exhibit the usual ciliary extension in response to lithium treatment. Together, these observations suggest that LC1 plays an important role in the maintenance of axonemal stability. |
format | Online Article Text |
id | pubmed-10295483 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-102954832023-08-16 Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility Sakato-Antoku, Miho King, Stephen M. Mol Biol Cell Articles Light chain 1 (LC1) is a highly conserved leucine-rich repeat protein associated with the microtubule-binding domain of the Chlamydomonas outer–dynein arm γ heavy chain. LC1 mutations in humans and trypanosomes lead to motility defects, while its loss in oomycetes results in aciliate zoospores. Here we describe a Chlamydomonas LC1 null mutant (dlu1-1). This strain has reduced swimming velocity and beat frequency, can undergo waveform conversion, but often exhibits loss of hydrodynamic coupling between the cilia. Following deciliation, Chlamydomonas cells rapidly rebuild cytoplasmic stocks of axonemal dyneins. Loss of LC1 disrupts the kinetics of this cytoplasmic preassembly so that most outer-arm dynein heavy chains remain monomeric even after several hours. This suggests that association of LC1 with its heavy chain–binding site is a key step or checkpoint in the outer-arm dynein assembly process. Similarly to strains lacking the entire outer arm and inner arm I1/f, we found that loss of LC1 and I1/f in dlu1-1 ida1 double mutants resulted in cells unable to build cilia under normal conditions. Furthermore, dlu1-1 cells do not exhibit the usual ciliary extension in response to lithium treatment. Together, these observations suggest that LC1 plays an important role in the maintenance of axonemal stability. The American Society for Cell Biology 2023-06-01 /pmc/articles/PMC10295483/ /pubmed/37133971 http://dx.doi.org/10.1091/mbc.E23-03-0104 Text en © 2023 Sakato-Antoku and King. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. https://creativecommons.org/licenses/by-nc-sa/4.0/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 4.0 International Creative Commons License. |
spellingShingle | Articles Sakato-Antoku, Miho King, Stephen M. Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility |
title | Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility |
title_full | Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility |
title_fullStr | Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility |
title_full_unstemmed | Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility |
title_short | Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility |
title_sort | outer-arm dynein light chain lc1 is required for normal motor assembly kinetics, ciliary stability, and motility |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10295483/ https://www.ncbi.nlm.nih.gov/pubmed/37133971 http://dx.doi.org/10.1091/mbc.E23-03-0104 |
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