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Reduced tubulin polyglutamylation suppresses flagellar shortness in Chlamydomonas
Ciliary length control is an incompletely understood process essential for normal ciliary function. The flagella of Chlamydomonas mutants lacking multiple axonemal dyneins are shorter than normal; previously it was shown that this shortness can be suppressed by the mutation suppressor of shortness 1...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571340/ https://www.ncbi.nlm.nih.gov/pubmed/26085508 http://dx.doi.org/10.1091/mbc.E15-03-0182 |
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author | Kubo, Tomohiro Hirono, Masafumi Aikawa, Takumi Kamiya, Ritsu Witman, George B. |
author_facet | Kubo, Tomohiro Hirono, Masafumi Aikawa, Takumi Kamiya, Ritsu Witman, George B. |
author_sort | Kubo, Tomohiro |
collection | PubMed |
description | Ciliary length control is an incompletely understood process essential for normal ciliary function. The flagella of Chlamydomonas mutants lacking multiple axonemal dyneins are shorter than normal; previously it was shown that this shortness can be suppressed by the mutation suppressor of shortness 1 (ssh1) via an unknown mechanism. To elucidate this mechanism, we carried out genetic analysis of ssh1 and found that it is a new allele of TPG2 (hereafter tpg2-3), which encodes FAP234 functioning in tubulin polyglutamylation in the axoneme. Similar to the polyglutamylation-deficient mutants tpg1 and tpg2-1, tpg2-3 axonemal tubulin has a greatly reduced level of long polyglutamate side chains. We found that tpg1 and tpg2-1 mutations also promote flagellar elongation in short-flagella mutants, consistent with a polyglutamylation-dependent mechanism of suppression. Double mutants of tpg1 or tpg2-1 and fla10-1, a temperature-sensitive mutant of intraflagellar transport, underwent slower flagellar shortening than fla10-1 at restrictive temperatures, indicating that the rate of tubulin disassembly is decreased in the polyglutamylation-deficient flagella. Moreover, α-tubulin incorporation into the flagellar tips in temporary dikaryons was retarded in polyglutamylation-deficient flagella. These results show that polyglutamylation deficiency stabilizes axonemal microtubules, decelerating axonemal disassembly at the flagellar tip and shifting the axonemal assembly/disassembly balance toward assembly. |
format | Online Article Text |
id | pubmed-4571340 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-45713402015-10-16 Reduced tubulin polyglutamylation suppresses flagellar shortness in Chlamydomonas Kubo, Tomohiro Hirono, Masafumi Aikawa, Takumi Kamiya, Ritsu Witman, George B. Mol Biol Cell Articles Ciliary length control is an incompletely understood process essential for normal ciliary function. The flagella of Chlamydomonas mutants lacking multiple axonemal dyneins are shorter than normal; previously it was shown that this shortness can be suppressed by the mutation suppressor of shortness 1 (ssh1) via an unknown mechanism. To elucidate this mechanism, we carried out genetic analysis of ssh1 and found that it is a new allele of TPG2 (hereafter tpg2-3), which encodes FAP234 functioning in tubulin polyglutamylation in the axoneme. Similar to the polyglutamylation-deficient mutants tpg1 and tpg2-1, tpg2-3 axonemal tubulin has a greatly reduced level of long polyglutamate side chains. We found that tpg1 and tpg2-1 mutations also promote flagellar elongation in short-flagella mutants, consistent with a polyglutamylation-dependent mechanism of suppression. Double mutants of tpg1 or tpg2-1 and fla10-1, a temperature-sensitive mutant of intraflagellar transport, underwent slower flagellar shortening than fla10-1 at restrictive temperatures, indicating that the rate of tubulin disassembly is decreased in the polyglutamylation-deficient flagella. Moreover, α-tubulin incorporation into the flagellar tips in temporary dikaryons was retarded in polyglutamylation-deficient flagella. These results show that polyglutamylation deficiency stabilizes axonemal microtubules, decelerating axonemal disassembly at the flagellar tip and shifting the axonemal assembly/disassembly balance toward assembly. The American Society for Cell Biology 2015-08-01 /pmc/articles/PMC4571340/ /pubmed/26085508 http://dx.doi.org/10.1091/mbc.E15-03-0182 Text en © 2015 Kubo 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 Kubo, Tomohiro Hirono, Masafumi Aikawa, Takumi Kamiya, Ritsu Witman, George B. Reduced tubulin polyglutamylation suppresses flagellar shortness in Chlamydomonas |
title | Reduced tubulin polyglutamylation suppresses flagellar shortness in Chlamydomonas |
title_full | Reduced tubulin polyglutamylation suppresses flagellar shortness in Chlamydomonas |
title_fullStr | Reduced tubulin polyglutamylation suppresses flagellar shortness in Chlamydomonas |
title_full_unstemmed | Reduced tubulin polyglutamylation suppresses flagellar shortness in Chlamydomonas |
title_short | Reduced tubulin polyglutamylation suppresses flagellar shortness in Chlamydomonas |
title_sort | reduced tubulin polyglutamylation suppresses flagellar shortness in chlamydomonas |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571340/ https://www.ncbi.nlm.nih.gov/pubmed/26085508 http://dx.doi.org/10.1091/mbc.E15-03-0182 |
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