scholarly journals CHE-3, a Cytosolic Dynein Heavy Chain, Is Required for Sensory Cilia Structure and Function in Caenorhabditis elegans

2000 ◽  
Vol 221 (2) ◽  
pp. 295-307 ◽  
Author(s):  
Stephen R. Wicks ◽  
Corry J. de Vries ◽  
Henri G.A.M. van Luenen ◽  
Ronald H.A. Plasterk
Keyword(s):  
Caenorhabditis Elegans ◽  
Heavy Chain ◽  
Structure And Function ◽  
Dynein Heavy Chain ◽  
Sensory Cilia ◽  
And Function

scholarly journals Maybe repressed mRNAs are not stored in the chromatoid body in mammalian spermatids

Reproduction ◽  
2011 ◽  
Vol 142 (3) ◽  
pp. 383-388 ◽  
Author(s):  
Kenneth C Kleene ◽  
Danielle L Cullinane
Keyword(s):  
Caenorhabditis Elegans ◽  
Mrna Translation ◽  
Mrna Localization ◽  
Structure And Function ◽  
Convincing Evidence ◽  
Chromatoid Body ◽  
P Granules ◽  
Accurate Indication ◽  
And Function ◽  
Translational Apparatus

The chromatoid body is a dynamic organelle that is thought to coordinate the cytoplasmic regulation of mRNA translation and degradation in mammalian spermatids. The chromatoid body is also postulated to function in repression of mRNA translation by sequestering dormant mRNAs where they are inaccessible to the translational apparatus. This review finds no convincing evidence that dormant mRNAs are localized exclusively in the chromatoid body. This discrepancy can be explained by two hypotheses. First, experimental artifacts, possibly related to peculiarities of the structure and function of the chromatoid body, preclude obtaining an accurate indication of mRNA localization. Second, mRNA is not stored in the chromatoid body, because, like perinuclear P granules in Caenorhabditis elegans, the chromatoid body functions as a center for mRNP remodeling and export to other cytoplasmic sites.

Age-related changes of mitochondrial structure and function in Caenorhabditis elegans

2006 ◽  
Vol 127 (10) ◽  
pp. 763-770 ◽  
Author(s):  
Kayo Yasuda ◽  
Takamasa Ishii ◽  
Hitoshi Suda ◽  
Akira Akatsuka ◽  
Philip S. Hartman ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Structure And Function ◽  
Mitochondrial Structure ◽  
Age Related ◽  
And Function ◽  
Age Related Changes

Motile cilia structure and function in patients with mutations in the outer dynein arm heavy chain DNAH9

2018 ◽  
Author(s):  
Amelia Shoemark ◽  
Mahmoud R Fassad ◽  
Farheen Daudvohra ◽  
Tom Burgoyne ◽  
Robert A Hirst ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Structure And Function ◽  
Motile Cilia ◽  
And Function

scholarly journals Caenorhabditis elegans DYF-2, an Orthologue of Human WDR19, Is a Component of the Intraflagellar Transport Machinery in Sensory Cilia

2006 ◽  
Vol 17 (11) ◽  
pp. 4801-4811 ◽  
Author(s):  
Evgeni Efimenko ◽  
Oliver E. Blacque ◽  
Guangshuo Ou ◽  
Courtney J. Haycraft ◽  
Bradley K. Yoder ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Aspartic Acid ◽  
Critical Role ◽  
Intraflagellar Transport ◽  
Bardet Biedl Syndrome ◽  
Evolutionarily Conserved ◽  
Sensory Cilia ◽  
Mutant Phenotypes ◽  
And Function

The intraflagellar transport (IFT) machinery required to build functional cilia consists of a multisubunit complex whose molecular composition, organization, and function are poorly understood. Here, we describe a novel tryptophan-aspartic acid (WD) repeat (WDR) containing IFT protein from Caenorhabditis elegans, DYF-2, that plays a critical role in maintaining the structural and functional integrity of the IFT machinery. We determined the identity of the dyf-2 gene by transgenic rescue of mutant phenotypes and by sequencing of mutant alleles. Loss of DYF-2 function selectively affects the assembly and motility of different IFT components and leads to defects in cilia structure and chemosensation in the nematode. Based on these observations, and the analysis of DYF-2 movement in a Bardet–Biedl syndrome mutant with partially disrupted IFT particles, we conclude that DYF-2 can associate with IFT particle complex B. At the same time, mutations in dyf-2 can interfere with the function of complex A components, suggesting an important role of this protein in the assembly of the IFT particle as a whole. Importantly, the mouse orthologue of DYF-2, WDR19, also localizes to cilia, pointing to an important evolutionarily conserved role for this WDR protein in cilia development and function.

scholarly journals Functional Analysis of Cytoplasmic Dynein Heavy Chain in Caenorhabditis elegans with Fast-acting Temperature-sensitive Mutations

2005 ◽  
Vol 16 (3) ◽  
pp. 1200-1212 ◽  
Author(s):  
Diane J. Schmidt ◽  
Debra J. Rose ◽  
William M. Saxton ◽  
Susan Strome
Keyword(s):  
Caenorhabditis Elegans ◽  
Heavy Chain ◽  
Metaphase Plate ◽  
Cytoplasmic Dynein ◽  
Model Systems ◽  
Temperature Sensitive ◽  
Permissive Temperature ◽  
Timely Initiation ◽  
Dynein Heavy Chain ◽  
Dominant Temperature Sensitive

Cytoplasmic dynein, a minus-end–directed microtubule motor, has been implicated in many cellular and developmental processes. Identification of specific cellular processes that rely directly on dynein would be facilitated by a means to induce specific and rapid inhibition of its function. We have identified conditional variants of a Caenorhabditis elegans dynein heavy chain (DHC-1) that lose function within a minute of a modest temperature upshift. Mutant embryos generated at elevated temperature show defects in centrosome separation, pronuclear migration, rotation of the centrosome/nucleus complex, bipolar spindle assembly, anaphase chromosome segregation, and cytokinesis. Our analyses of mutant embryos generated at permissive temperature and then upshifted quickly just before events of interest indicate that DHC-1 is required specifically for rotation of the centrosome/nucleus complex, for chromosome congression to a well ordered metaphase plate, and for timely initiation of anaphase. Our results do not support the view that DHC-1 is required for anaphase B separation of spindle poles and chromosomes. A P-loop mutation identified in two independent dominant temperature-sensitive alleles of dhc-1, when engineered into the DHC1 gene of Saccharomyces cerevisiae, conferred a dominant temperature-sensitive dynein loss-of-function phenotype. This suggests that temperature-sensitive mutations can be created for time-resolved function analyses of dyneins and perhaps other P-loop proteins in a variety of model systems.

scholarly journals Cytoplasmic Dynein Heavy Chain 1b Is Required for Flagellar Assembly in Chlamydomonas

1999 ◽  
Vol 10 (3) ◽  
pp. 693-712 ◽  
Author(s):  
Mary E. Porter ◽  
Raqual Bower ◽  
Julie A. Knott ◽  
Pamela Byrd ◽  
William Dentler
Keyword(s):  
Caenorhabditis Elegans ◽  
Expression Pattern ◽  
Heavy Chain ◽  
Insertional Mutagenesis ◽  
Sea Urchins ◽  
Amorphous Material ◽  
Cytoplasmic Dynein ◽  
Genetic Approach ◽  
Dynein Heavy Chain ◽  
Flagellar Assembly

A second cytoplasmic dynein heavy chain (cDhc) has recently been identified in several organisms, and its expression pattern is consistent with a possible role in axoneme assembly. We have used a genetic approach to ask whether cDhc1b is involved in flagellar assembly in Chlamydomonas. Using a modified PCR protocol, we recovered two cDhc sequences distinct from the axonemal Dhc sequences identified previously. cDhc1a is closely related to the major cytoplasmic Dhc, whereas cDhc1b is closely related to the minor cDhc isoform identified in sea urchins, Caenorhabditis elegans, and Tetrahymena. TheChlamydomonas cDhc1b transcript is a low-abundance mRNA whose expression is enhanced by deflagellation. To determine its role in flagellar assembly, we screened a collection of stumpy flagellar (stf) mutants generated by insertional mutagenesis and identified two strains in which portions of the cDhc1bgene have been deleted. The two mutants assemble short flagellar stumps (<1–2 μm) filled with aberrant microtubules, raft-like particles, and other amorphous material. The results indicate that cDhc1b is involved in the transport of components required for flagellar assembly in Chlamydomonas.

scholarly journals Optimal sidestepping of intraflagellar transport kinesins regulates structure and function of sensory cilia

2020 ◽  
Vol 39 (12) ◽  
Author(s):  
Chao Xie ◽  
Liuju Li ◽  
Ming Li ◽  
Wenxin Shao ◽  
Qingyu Zuo ◽  
...  
Keyword(s):  
Intraflagellar Transport ◽  
Structure And Function ◽  
Sensory Cilia ◽  
And Function

scholarly journals Crescerin uses a TOG domain array to regulate microtubules in the primary cilium

2015 ◽  
Vol 26 (23) ◽  
pp. 4248-4264 ◽  
Author(s):  
Alakananda Das ◽  
Daniel J. Dickinson ◽  
Cameron C. Wood ◽  
Bob Goldstein ◽  
Kevin C. Slep
Keyword(s):  
Crystal Structure ◽  
Binding Activity ◽  
Structure And Function ◽  
Sensory Disorders ◽  
Tubulin Binding ◽  
Sensory Cilia ◽  
And Function ◽  
Binding Determinants ◽  
Extracellular Environment

Eukaryotic cilia are cell-surface projections critical for sensing the extracellular environment. Defects in cilia structure and function result in a broad range of developmental and sensory disorders. However, mechanisms that regulate the microtubule (MT)-based scaffold forming the cilia core are poorly understood. TOG domain array–containing proteins ch-TOG and CLASP are key regulators of cytoplasmic MTs. Whether TOG array proteins also regulate ciliary MTs is unknown. Here we identify the conserved Crescerin protein family as a cilia-specific, TOG array-containing MT regulator. We present the crystal structure of mammalian Crescerin1 TOG2, revealing a canonical TOG fold with conserved tubulin-binding determinants. Crescerin1's TOG domains possess inherent MT-binding activity and promote MT polymerization in vitro. Using Cas9-triggered homologous recombination in Caenorhabditis elegans, we demonstrate that the worm Crescerin family member CHE-12 requires TOG domain–dependent tubulin-binding activity for sensory cilia development. Thus, Crescerin expands the TOG domain array–based MT regulatory paradigm beyond ch-TOG and CLASP, representing a distinct regulator of cilia structure.

scholarly journals Him-10 Is Required for Kinetochore Structure and Function on Caenorhabditis elegans Holocentric Chromosomes

2001 ◽  
Vol 153 (6) ◽  
pp. 1227-1238 ◽  
Author(s):  
Mary Howe ◽  
Kent L. McDonald ◽  
Donna G. Albertson ◽  
Barbara J. Meyer
Keyword(s):  
Caenorhabditis Elegans ◽  
Structure And Function ◽  
Holocentric Chromosomes ◽  
Molecular Architecture ◽  
Mitotic Chromosomes ◽  
C Elegans ◽  
Meiotic Chromosomes ◽  
Evolutionarily Conserved ◽  
And Function ◽  
Chromosome Nondisjunction

Macromolecular structures called kinetochores attach and move chromosomes within the spindle during chromosome segregation. Using electron microscopy, we identified a structure on the holocentric mitotic and meiotic chromosomes of Caenorhabditis elegans that resembles the mammalian kinetochore. This structure faces the poles on mitotic chromosomes but encircles meiotic chromosomes. Worm kinetochores require the evolutionarily conserved HIM-10 protein for their structure and function. HIM-10 localizes to the kinetochores and mediates attachment of chromosomes to the spindle. Depletion of HIM-10 disrupts kinetochore structure, causes a failure of bipolar spindle attachment, and results in chromosome nondisjunction. HIM-10 is related to the Nuf2 kinetochore proteins conserved from yeast to humans. Thus, the extended kinetochores characteristic of C. elegans holocentric chromosomes provide a guide to the structure, molecular architecture, and function of conventional kinetochores.

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