Branchial cilia and sperm flagella recruit distinct axonemal components.
Eukaryotic cilia and flagella have highly conserved 9 + 2 structures. They are functionally diverged to play cell-type-specific roles even in a multicellular organism. Although their structural components are therefore believed to be common, few studies have investigated the molecular diversity of t...
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doaj-f5bf0ad2c09d4ebd98992403ce8c42f62020-11-25T02:23:37ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01105e012600510.1371/journal.pone.0126005Branchial cilia and sperm flagella recruit distinct axonemal components.Alu KonnoKogiku ShibaChunhua CaiKazuo InabaEukaryotic cilia and flagella have highly conserved 9 + 2 structures. They are functionally diverged to play cell-type-specific roles even in a multicellular organism. Although their structural components are therefore believed to be common, few studies have investigated the molecular diversity of the protein components of the cilia and flagella in a single organism. Here we carried out a proteomic analysis and compared protein components between branchial cilia and sperm flagella in a marine invertebrate chordate, Ciona intestinalis. Distinct feature of protein recruitment in branchial cilia and sperm flagella has been clarified; (1) Isoforms of α- and β-tubulins as well as those of actins are distinctly used in branchial cilia or sperm flagella. (2) Structural components, such as dynein docking complex, tektins and an outer dense fiber protein, are used differently by the cilia and flagella. (3) Sperm flagella are specialized for the cAMP- and Ca2+-dependent regulation of outer arm dynein and for energy metabolism by glycolytic enzymes. Our present study clearly demonstrates that flagellar or ciliary proteins are properly recruited according to their function and stability, despite their apparent structural resemblance and conservation.http://europepmc.org/articles/PMC4427456?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Alu Konno Kogiku Shiba Chunhua Cai Kazuo Inaba |
spellingShingle |
Alu Konno Kogiku Shiba Chunhua Cai Kazuo Inaba Branchial cilia and sperm flagella recruit distinct axonemal components. PLoS ONE |
author_facet |
Alu Konno Kogiku Shiba Chunhua Cai Kazuo Inaba |
author_sort |
Alu Konno |
title |
Branchial cilia and sperm flagella recruit distinct axonemal components. |
title_short |
Branchial cilia and sperm flagella recruit distinct axonemal components. |
title_full |
Branchial cilia and sperm flagella recruit distinct axonemal components. |
title_fullStr |
Branchial cilia and sperm flagella recruit distinct axonemal components. |
title_full_unstemmed |
Branchial cilia and sperm flagella recruit distinct axonemal components. |
title_sort |
branchial cilia and sperm flagella recruit distinct axonemal components. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2015-01-01 |
description |
Eukaryotic cilia and flagella have highly conserved 9 + 2 structures. They are functionally diverged to play cell-type-specific roles even in a multicellular organism. Although their structural components are therefore believed to be common, few studies have investigated the molecular diversity of the protein components of the cilia and flagella in a single organism. Here we carried out a proteomic analysis and compared protein components between branchial cilia and sperm flagella in a marine invertebrate chordate, Ciona intestinalis. Distinct feature of protein recruitment in branchial cilia and sperm flagella has been clarified; (1) Isoforms of α- and β-tubulins as well as those of actins are distinctly used in branchial cilia or sperm flagella. (2) Structural components, such as dynein docking complex, tektins and an outer dense fiber protein, are used differently by the cilia and flagella. (3) Sperm flagella are specialized for the cAMP- and Ca2+-dependent regulation of outer arm dynein and for energy metabolism by glycolytic enzymes. Our present study clearly demonstrates that flagellar or ciliary proteins are properly recruited according to their function and stability, despite their apparent structural resemblance and conservation. |
url |
http://europepmc.org/articles/PMC4427456?pdf=render |
work_keys_str_mv |
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