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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Bibliographic Details
Published in:PLoS genetics 2007-08, Vol.3 (8), p.e128-e128
Main Authors: O'Rourke, Sean M, Dorfman, Marc D, Carter, J Clayton, Bowerman, Bruce
Format: Article
Language:English
Subjects:
Animals
Animals, Genetically Modified
Caenorhabditis
Caenorhabditis elegans
Caenorhabditis elegans - genetics
Caenorhabditis elegans - physiology
Caenorhabditis elegans Proteins - antagonists & inhibitors
Caenorhabditis elegans Proteins - genetics
Caenorhabditis elegans Proteins - physiology
Carrier Proteins - genetics
Carrier Proteins - physiology
Cell Biology
Cell cycle
Cells
Cellular biology
Cytoplasm - enzymology
Cytoplasm - genetics
Cytoplasm - physiology
Cytoplasmic Dyneins
Drosophila Proteins - genetics
Drosophila Proteins - physiology
Dyneins - antagonists & inhibitors
Dyneins - genetics
Dyneins - physiology
Eukaryotes
Gene mutations
Genes
Genetic aspects
Genetics
Genetics and Genomics
Properties
Protein Subunits - genetics
Protein Subunits - physiology
Proteins
Repressor Proteins - genetics
Repressor Proteins - physiology
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Summary: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.
ISSN:1553-7404
1553-7390
1553-7404
DOI:10.1371/journal.pgen.0030128