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  • Dynein
  • Springer  (6)
  • Cell Press  (1)
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  • 1
    Publication Date: 2022-10-27
    Description: © The Author(s), 2020. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Meaders, J. L., de Matos, S. N., & Burgess, D. R. A pushing mechanism for microtubule aster positioning in a large cell type. Cell Reports, 33(1), (2020): 108213, doi:10.1016/j.celrep.2020.108213.
    Description: After fertilization, microtubule (MT) sperm asters undergo long-range migration to accurately position pronuclei. Due to the large sizes of zygotes, the forces driving aster migration are considered to be from pulling on the astral MTs by dynein, with no significant contribution from pushing forces. Here, we re-investigate the forces responsible for sperm aster centration in sea urchin zygotes. Our quantifications of aster geometry and MT density preclude a pulling mechanism. Manipulation of aster radial lengths and growth rates, combined with quantitative tracking of aster migration dynamics, indicates that aster migration is equal to the length of rear aster radii, supporting a pushing model for centration. We find that dynein inhibition causes an increase in aster migration rates. Finally, ablation of rear astral MTs halts migration, whereas front and side ablations do not. Collectively, our data indicate that a pushing mechanism can drive the migration of asters in a large cell type.
    Description: We would like to thank Dr. Jesse Gatlin for sending us the Tau-mCherry fusion protein for imaging live MTs. We would also like to thank Dr. Timothy Mitchison, Dr. Christine Field, and Dr. James Pelletier for supplying us with CA4, p150-CC1, and EB1-GFP peptides, as well as for fruitful discussions. Finally, we would like to thank Dr. Charles Shuster and Leslie Toledo-Jacobo for constructive feedback when preparing the manuscript. We thank Bret Judson and the Boston College Imaging Core for infrastructure and support. This material is based upon work supported by NSF grant no. 124425 to D.R.B.
    Keywords: Dynein ; Aster ; Microtubule ; Centrosome ; Pronucleus ; Fertilization ; Aster position
    Repository Name: Woods Hole Open Access Server
    Type: Article
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Sexual plant reproduction 9 (1996), S. 312-317 
    ISSN: 1432-2145
    Keywords: Pollen tube ; Nicotiana tabacum ; Ginkgo biloba ; Dynein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Microtubules in pollen tubes are evident within the vegetative and generative cell cytoplasm. This observation led to the formulation of several hypotheses regarding the role of microtubules in cytoplasmic movement and the migration of the vegetative nucleus/generative cell along the pollen tube. The study of microtubular motor proteins in pollen tubes followed the discovery and characterization of an immunoreactive homolog of mammalian kinesin in tobacco pollen tubes. Recent identification of dynein-related polypeptides in pollen tubes ofNicotiana tabacum and pollen ofGinkgo biloba is a significant step in the definition of the role of microtubule function within pollen and pollen tubes.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Sexual plant reproduction 9 (1996), S. 312-317 
    ISSN: 1432-2145
    Keywords: Key words Pollen tube ; Nicotiana tabacum ; Ginkgo biloba ; Dynein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Microtubules in pollen tubes are evident within the vegetative and generative cell cytoplasm. This observation led to the formulation of several hypotheses regarding the role of microtubules in cytoplasmic movement and the migration of the vegetative nucleus/generative cell along the pollen tube. The study of microtubular motor proteins in pollen tubes followed the discovery and characterization of an immunoreactive homolog of mammalian kinesin in tobacco pollen tubes. Recent identification of dynein-related polypeptides in pollen tubes of Nicotiana tabacum and pollen of Ginkgo biloba is a significant step in the definition of the role of microtubule function within pollen and pollen tubes.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1617-4623
    Keywords: Key words Saccharomyces cerevisiae ; Dynein ; Gene disruption ; cin8
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Cytoplasmic dynein is a multisubunit, microtubule-dependent motor enzyme that has been proposed to function in a variety of intracellular movements. As part of an effort to understand the evolution and the biological roles of cytoplasmic dynein, we have identified the first non-metazoan dynein light chain 1, SLC1, in the yeast Saccharomyces cerevisiae. The amino acid sequence of the SLC1 protein is similar to those of the human, Drosophila and Caenorhabditis cytoplasmic dynein light chains 1. The SLC1 gene lies adjacent to the YAP2 (=CAD1) transcription unit. The SLC1 coding sequence is split by two introns and its mRNA is detectable throughout the cell cycle. Tetrad analysis of heterozygotes harboring a TRP insertion in the SLC1 coding region indicate that SLC1 function is not essential for cell viability. Furthermore, we demonstrate that double mutants, defective for SLC1 and the kinesin-related CIN8 genes are non-lethal. The redundancy of SLC1 function in yeast contrasts with the cell death caused by loss-of-function mutations in the dynein light chain 1 gene in Drosophila melanogaster.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 206 (1999), S. 245-248 
    ISSN: 1615-6102
    Keywords: Cilia ; Dynein ; Epithelium ; Trachea ; Differentiation ; Cloning
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ciliated cells play an integral role in the defense mechanisms of the respiratory system. By the coordinated beating of their cilia they provide the force necessary to clear potentially harmful material from the airways. We have been investigating the regulation of ciliated-cell differentiation and gene expression. Using a culture system that allows us to positively or negatively regulate the development of the ciliated-cell phenotype, we have previously reported that the expression of axonemal dynein heavy chain mRNAs are regulated in parallel with the development of ciliated cells. To identify other genes important to the development or function of ciliated cells, differential display was used to compare mRNA isolated from cultures of ciliated or nonciliated rat tracheal epithelial cells. Two novel genes, KPL1 and KPL2, have been identified whose expression is increased in parallel with ciliated-cell differentiation. Two transcripts of KPL1 are expressed in a tissue-specific pattern; KPL1 is particularly highly expressed in brain. The sequence of KPL1 predicts a 188 or 223 amino acid protein which contains a pleckstrin homology domain. Pleckstrin homology domains have been shown to bind inositolphosphates and G-proteins and function as signal-dependent membrane adapters. KPL1 therefore may function in a signal transduction pathway important to the development or maintenance of the ciliated-cell phenotype. KPL2 shows more limited distribution and is predominantly expressed in tissues which contain axonemes. KPL2 is predicted to encode a 1744 amino acid protein which contains many functional motifs, including nuclear localization signals, an ATP-binding domain, a proline-rich region, and a calponin homology domain. KPL2 may thus be involved in transmitting signals to the nucleus during ciliated-cell differentiation.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Dynein ; Gene disruption ; cin8
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cytoplasmic dynein is a multisubunit, microtubule-dependent motor enzyme that has been proposed to function in a variety of intracellular movements. As part of an effort to understand the evolution and the biological roles of cytoplasmic dynein, we have identified the first non-metazoan dynein light chain 1, SLC1, in the yeastSaccharomyces cerevisiae. The amino acid sequence of the SLC1 protein is similar to those of the human,Drosophila andCaenorhabditis cytoplasmic dynein light chains 1. TheSLC1 gene lies adjacent to theYAP2 (CAD1) transcription unit. TheSLC1 coding sequence is split by two introns and its mRNA is detectable throughout the cell cycle. Tetrad analysis of heterozygotes harboring aTRP insertion in theSLC1 coding region indicate thatSLC1 function is not essential for cell viability. Furthermore, we demonstrate that double mutants, defective forSLC1 and the kinesin-relatedCIN8 genes are non-lethal. The redundancy ofSLC1 function in yeast contrasts with the cell death caused by loss-of-function mutations in the dynein light chain 1 gene inDrosophila melanogaster.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 206 (1999), S. 241-244 
    ISSN: 1615-6102
    Keywords: Cilia ; Dynein ; Protein phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ciliary beating is empowered by a mechanochemical enzyme, dynein, which appears as two rows of projections on doublet microtubules. While inner-arm dyneins modulate beat form, outer-arm dynein empowers ciliary beat and sets beat frequency. Beat frequency is controlled via phosphorylation of outer-arm dynein. UsingParamecium tetraurelia as model system, we have previously identified a regulatory light chain of outer-arm dynein (22S dynein), Mr29 (p29), whose phosphorylation is cAMP-dependent. The phosphorylation state of the p29 in 22 S dynein determines in vitro microtubule translocation velocity. Although in vitro phosphorylation of p29 takes place in a short time, the percent change ist significantly less than the percent change in dynein activation, or in ciliary beat frequency. A potential mechanism that explains how a few activated dyneins can change ciliary beating is discussed.
    Type of Medium: Electronic Resource
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