The Ubiquitin Conjugation System Is Involved in the Disassembly of Cilia and Flagella

The disassembly of cilia and flagella is linked to the cell cycle and environmental cues. We have found that ubiquitination of flageliar proteins is an integral part of flageliar disassembly. Free ubiquitin and the ubiquitin-conjugating enzyme CrUbc13 are detected in flagella, and several proteins a...

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Published inThe Journal of cell biology Vol. 186; no. 4; pp. 601 - 613
Main Authors Huang, Kaiyao, Diener, Dennis R., Rosenbaum, Joel L.
Format Journal Article
LanguageEnglish
Published United States Rockefeller University Press 24.08.2009
The Rockefeller University Press
Subjects
Adenosine triphosphatase
Animals
Antibodies
Biochemistry
Cell cycle
Cells
Chlamydomonas reinhardtii - cytology
Chlamydomonas reinhardtii - metabolism
Cilia
Cilia - metabolism
Cilia - ultrastructure
Enzymes
Epithelial cells
Flagella
Flagella - metabolism
Flagella - ultrastructure
Humans
Microtubules
Proteins
Protozoan Proteins - genetics
Protozoan Proteins - metabolism
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Signal Transduction - physiology
Ubiquitin - metabolism
Ubiquitin-Conjugating Enzymes - genetics
Ubiquitin-Conjugating Enzymes - metabolism
Ubiquitins
Online AccessGet full text

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Abstract The disassembly of cilia and flagella is linked to the cell cycle and environmental cues. We have found that ubiquitination of flageliar proteins is an integral part of flageliar disassembly. Free ubiquitin and the ubiquitin-conjugating enzyme CrUbc13 are detected in flagella, and several proteins are ubiquitinated in isolated flagella when exogenous ubiquitin and adenosine triphosphatase are added, suggesting that the ubiquitin conjugation system operates in flagella. Levels of ubiquitinated flageliar proteins increase during flageliar résorption, especially in intraflagellar transport (lFF) mutants, suggesting that disassembly products are labeled with ubiquitin and transported to the cell body by lFT. Substrates of the ubiquitin conjugation system include α-tubulin (but not ß-tubulin), a dynein subunit (lC2), two signaling proteins involved in the mating process, cyclic guanosine monophosphate-dependent kinase, and the cation channel polycystic kidney disease 2. Ubiquitination of flageliar proteins is enhanced early in mating, suggesting that ubiquitination also plays an active role in regulating signaling pathways in flagella.
AbstractList The disassembly of cilia and flagella is linked to the cell cycle and environmental cues. We have found that ubiquitination of flagellar proteins is an integral part of flagellar disassembly. Free ubiquitin and the ubiquitin-conjugating enzyme CrUbc13 are detected in flagella, and several proteins are ubiquitinated in isolated flagella when exogenous ubiquitin and adenosine triphosphatase are added, suggesting that the ubiquitin conjugation system operates in flagella. Levels of ubiquitinated flagellar proteins increase during flagellar resorption, especially in intraflagellar transport (IFT) mutants, suggesting that disassembly products are labeled with ubiquitin and transported to the cell body by IFT. Substrates of the ubiquitin conjugation system include α-tubulin (but not β-tubulin), a dynein subunit (IC2), two signaling proteins involved in the mating process, cyclic guanosine monophosphate-dependent kinase, and the cation channel polycystic kidney disease 2. Ubiquitination of flagellar proteins is enhanced early in mating, suggesting that ubiquitination also plays an active role in regulating signaling pathways in flagella. [PUBLICATION ABSTRACT]
The disassembly of cilia and flagella is linked to the cell cycle and environmental cues. We have found that ubiquitination of flagellar proteins is an integral part of flagellar disassembly. Free ubiquitin and the ubiquitin-conjugating enzyme CrUbc13 are detected in flagella, and several proteins are ubiquitinated in isolated flagella when exogenous ubiquitin and adenosine triphosphatase are added, suggesting that the ubiquitin conjugation system operates in flagella. Levels of ubiquitinated flagellar proteins increase during flagellar resorption, especially in intraflagellar transport (IFT) mutants, suggesting that disassembly products are labeled with ubiquitin and transported to the cell body by IFT. Substrates of the ubiquitin conjugation system include α-tubulin (but not β-tubulin), a dynein subunit (IC2), two signaling proteins involved in the mating process, cyclic guanosine monophosphate–dependent kinase, and the cation channel polycystic kidney disease 2. Ubiquitination of flagellar proteins is enhanced early in mating, suggesting that ubiquitination also plays an active role in regulating signaling pathways in flagella.
The disassembly of cilia and flagella is linked to the cell cycle and environmental cues. We have found that ubiquitination of flagellar proteins is an integral part of flagellar disassembly. Free ubiquitin and the ubiquitin-conjugating enzyme CrUbc13 are detected in flagella, and several proteins are ubiquitinated in isolated flagella when exogenous ubiquitin and adenosine triphosphatase are added, suggesting that the ubiquitin conjugation system operates in flagella. Levels of ubiquitinated flagellar proteins increase during flagellar resorption, especially in intraflagellar transport (IFT) mutants, suggesting that disassembly products are labeled with ubiquitin and transported to the cell body by IFT. Substrates of the ubiquitin conjugation system include alpha-tubulin (but not beta-tubulin), a dynein subunit (IC2), two signaling proteins involved in the mating process, cyclic guanosine monophosphate-dependent kinase, and the cation channel polycystic kidney disease 2. Ubiquitination of flagellar proteins is enhanced early in mating, suggesting that ubiquitination also plays an active role in regulating signaling pathways in flagella.
The disassembly of cilia and flagella is linked to the cell cycle and environmental cues. We have found that ubiquitination of flageliar proteins is an integral part of flageliar disassembly. Free ubiquitin and the ubiquitin-conjugating enzyme CrUbc13 are detected in flagella, and several proteins are ubiquitinated in isolated flagella when exogenous ubiquitin and adenosine triphosphatase are added, suggesting that the ubiquitin conjugation system operates in flagella. Levels of ubiquitinated flageliar proteins increase during flageliar résorption, especially in intraflagellar transport (lFF) mutants, suggesting that disassembly products are labeled with ubiquitin and transported to the cell body by lFT. Substrates of the ubiquitin conjugation system include α-tubulin (but not ß-tubulin), a dynein subunit (lC2), two signaling proteins involved in the mating process, cyclic guanosine monophosphate-dependent kinase, and the cation channel polycystic kidney disease 2. Ubiquitination of flageliar proteins is enhanced early in mating, suggesting that ubiquitination also plays an active role in regulating signaling pathways in flagella.
Author Rosenbaum, Joel L.
Huang, Kaiyao
Diener, Dennis R.
AuthorAffiliation Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520
AuthorAffiliation_xml – name: Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520
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  givenname: Kaiyao
  surname: Huang
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  givenname: Dennis R.
  surname: Diener
  fullname: Diener, Dennis R.
– sequence: 3
  givenname: Joel L.
  surname: Rosenbaum
  fullname: Rosenbaum, Joel L.
BackLink https://www.ncbi.nlm.nih.gov/pubmed/19704024$$D View this record in MEDLINE/PubMed
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Snippet The disassembly of cilia and flagella is linked to the cell cycle and environmental cues. We have found that ubiquitination of flageliar proteins is an...
The disassembly of cilia and flagella is linked to the cell cycle and environmental cues. We have found that ubiquitination of flagellar proteins is an...
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SubjectTerms Adenosine triphosphatase
Animals
Antibodies
Biochemistry
Cell cycle
Cells
Chlamydomonas reinhardtii - cytology
Chlamydomonas reinhardtii - metabolism
Cilia
Cilia - metabolism
Cilia - ultrastructure
Enzymes
Epithelial cells
Flagella
Flagella - metabolism
Flagella - ultrastructure
Humans
Microtubules
Proteins
Protozoan Proteins - genetics
Protozoan Proteins - metabolism
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Signal Transduction - physiology
Ubiquitin - metabolism
Ubiquitin-Conjugating Enzymes - genetics
Ubiquitin-Conjugating Enzymes - metabolism
Ubiquitins
Title The Ubiquitin Conjugation System Is Involved in the Disassembly of Cilia and Flagella
URI https://www.jstor.org/stable/40384092
https://www.ncbi.nlm.nih.gov/pubmed/19704024
https://www.proquest.com/docview/217111913
https://search.proquest.com/docview/67597752
https://pubmed.ncbi.nlm.nih.gov/PMC2733750
Volume 186
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