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Dynein Modifiers in C. elegans: Light Chains Suppress Conditional Heavy Chain Mutants

Cytoplasmic dynein is a microtubule-dependent motor protein that functions in mitotic cells during centrosome separation, metaphase chromosome congression, anaphase spindle elongation, and chromosome segregation. Dynein is also utilized during interphase for vesicle transport and organelle positioni...

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Autores principales: O'Rourke, Sean M, Dorfman, Marc D, Carter, J. Clayton, Bowerman, Bruce
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1937013/
https://www.ncbi.nlm.nih.gov/pubmed/17676955
http://dx.doi.org/10.1371/journal.pgen.0030128
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author O'Rourke, Sean M
Dorfman, Marc D
Carter, J. Clayton
Bowerman, Bruce
author_facet O'Rourke, Sean M
Dorfman, Marc D
Carter, J. Clayton
Bowerman, Bruce
author_sort O'Rourke, Sean M
collection PubMed
description Cytoplasmic dynein is a microtubule-dependent motor protein that functions in mitotic cells during centrosome separation, metaphase chromosome congression, anaphase spindle elongation, and chromosome segregation. Dynein is also utilized during interphase for vesicle transport and organelle positioning. While numerous cellular processes require cytoplasmic dynein, the mechanisms that target and regulate this microtubule motor remain largely unknown. By screening a conditional Caenorhabditis elegans cytoplasmic dynein heavy chain mutant at a semipermissive temperature with a genome-wide RNA interference library to reduce gene functions, we have isolated and characterized twenty dynein-specific suppressor genes. When reduced in function, these genes suppress dynein mutants but not other conditionally mutant loci, and twelve of the 20 specific suppressors do not exhibit sterile or lethal phenotypes when their function is reduced in wild-type worms. Many of the suppressor proteins, including two dynein light chains, localize to subcellular sites that overlap with those reported by others for the dynein heavy chain. Furthermore, knocking down any one of four putative dynein accessory chains suppresses the conditional heavy chain mutants, suggesting that some accessory chains negatively regulate heavy chain function. We also identified 29 additional genes that, when reduced in function, suppress conditional mutations not only in dynein but also in loci required for unrelated essential processes. In conclusion, we have identified twenty genes that in many cases are not essential themselves but are conserved and when reduced in function can suppress conditionally lethal C. elegans cytoplasmic dynein heavy chain mutants. We conclude that conserved but nonessential genes contribute to dynein function during the essential process of mitosis.
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spelling pubmed-19370132007-08-03 Dynein Modifiers in C. elegans: Light Chains Suppress Conditional Heavy Chain Mutants O'Rourke, Sean M Dorfman, Marc D Carter, J. Clayton Bowerman, Bruce PLoS Genet Research Article Cytoplasmic dynein is a microtubule-dependent motor protein that functions in mitotic cells during centrosome separation, metaphase chromosome congression, anaphase spindle elongation, and chromosome segregation. Dynein is also utilized during interphase for vesicle transport and organelle positioning. While numerous cellular processes require cytoplasmic dynein, the mechanisms that target and regulate this microtubule motor remain largely unknown. By screening a conditional Caenorhabditis elegans cytoplasmic dynein heavy chain mutant at a semipermissive temperature with a genome-wide RNA interference library to reduce gene functions, we have isolated and characterized twenty dynein-specific suppressor genes. When reduced in function, these genes suppress dynein mutants but not other conditionally mutant loci, and twelve of the 20 specific suppressors do not exhibit sterile or lethal phenotypes when their function is reduced in wild-type worms. Many of the suppressor proteins, including two dynein light chains, localize to subcellular sites that overlap with those reported by others for the dynein heavy chain. Furthermore, knocking down any one of four putative dynein accessory chains suppresses the conditional heavy chain mutants, suggesting that some accessory chains negatively regulate heavy chain function. We also identified 29 additional genes that, when reduced in function, suppress conditional mutations not only in dynein but also in loci required for unrelated essential processes. In conclusion, we have identified twenty genes that in many cases are not essential themselves but are conserved and when reduced in function can suppress conditionally lethal C. elegans cytoplasmic dynein heavy chain mutants. We conclude that conserved but nonessential genes contribute to dynein function during the essential process of mitosis. Public Library of Science 2007-08 2007-08-03 /pmc/articles/PMC1937013/ /pubmed/17676955 http://dx.doi.org/10.1371/journal.pgen.0030128 Text en © 2007 O'Rourke et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
O'Rourke, Sean M
Dorfman, Marc D
Carter, J. Clayton
Bowerman, Bruce
Dynein Modifiers in C. elegans: Light Chains Suppress Conditional Heavy Chain Mutants
title Dynein Modifiers in C. elegans: Light Chains Suppress Conditional Heavy Chain Mutants
title_full Dynein Modifiers in C. elegans: Light Chains Suppress Conditional Heavy Chain Mutants
title_fullStr Dynein Modifiers in C. elegans: Light Chains Suppress Conditional Heavy Chain Mutants
title_full_unstemmed Dynein Modifiers in C. elegans: Light Chains Suppress Conditional Heavy Chain Mutants
title_short Dynein Modifiers in C. elegans: Light Chains Suppress Conditional Heavy Chain Mutants
title_sort dynein modifiers in c. elegans: light chains suppress conditional heavy chain mutants
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1937013/
https://www.ncbi.nlm.nih.gov/pubmed/17676955
http://dx.doi.org/10.1371/journal.pgen.0030128
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