MITOSIS IN DUNALIELLA BIOCULATA (CHLOROPHYTA): CENTRIN BUT NOT BASAL BODIES ARE AT THE SPINDLE POLES

2001 ◽  
Vol 37 (6) ◽  
pp. 1030-1043 ◽  
Author(s):  
Andrea Grunow ◽  
Karl‐Ferdinand Lechtreck
Keyword(s):  
Basal Bodies ◽  
Spindle Poles

scholarly journals Human 76p

1999 ◽  
Vol 147 (4) ◽  
pp. 857-868 ◽  
Author(s):  
Fabienne Fava ◽  
Brigitte Raynaud-Messina ◽  
Jeanne Leung-Tack ◽  
Laurent Mazzolini ◽  
Min Li ◽  
...  
Keyword(s):  
Molecular Level ◽  
Basal Bodies ◽  
Microtubule Nucleation ◽  
Higher Plant ◽  
Spindle Poles ◽  
Mammalian Tissues ◽  
Associated Proteins ◽  
Centrosomal Proteins ◽  
Polypeptide Band

The role of the centrosomes in microtubule nucleation remains largely unknown at the molecular level. γ-Tubulin and the two associated proteins h103p (hGCP2) and h104p (hGCP3) are essential. These proteins are also present in soluble complexes containing additional polypeptides. Partial sequencing of a 76- kD polypeptide band from these complexes allowed the isolation of a cDNA encoding for a new protein (h76p = hGCP4) expressed ubiquitously in mammalian tissues. Orthologues of h76p have been characterized in Drosophila and in the higher plant Medicago. Several pieces of evidence indicate that h76p is involved in microtubule nucleation. (1) h76p is localized at the centrosome as demonstrated by immunofluorescence. (2) h76p and γ-tubulin are associated in the γ-tubulin complexes. (3) γ-tubulin complexes containing h76p bind to microtubules. (4) h76p is recruited to the spindle poles and to Xenopus sperm basal bodies. (5) h76p is necessary for aster nucleation by sperm basal bodies and recombinant h76p partially replaces endogenous 76p in oocyte extracts. Surprisingly, h76p shares partial sequence identity with human centrosomal proteins h103p and h104p, suggesting a common protein core. Hence, human γ-tubulin appears associated with at least three evolutionary related centrosomal proteins, raising new questions about their functions at the molecular level.

scholarly journals Regulating the transition from centriole to basal body

2011 ◽  
Vol 193 (3) ◽  
pp. 435-444 ◽  
Author(s):  
Tetsuo Kobayashi ◽  
Brian D. Dynlacht
Keyword(s):  
Cell Cycle ◽  
Basal Body ◽  
Primary Cilia ◽  
Molecular Mechanisms ◽  
Basal Bodies ◽  
Spindle Poles ◽  
Shed Light

The role of centrioles changes as a function of the cell cycle. Centrioles promote formation of spindle poles in mitosis and act as basal bodies to assemble primary cilia in interphase. Stringent regulations govern conversion between these two states. Although the molecular mechanisms have not been fully elucidated, recent findings have begun to shed light on pathways that regulate the conversion of centrioles to basal bodies and vice versa. Emerging studies also provide insights into how defects in the balance between centrosome and cilia function could promote ciliopathies and cancer.

scholarly journals MORN1 Has a Conserved Role in Asexual and Sexual Development across the Apicomplexa

2008 ◽  
Vol 7 (4) ◽  
pp. 698-711 ◽  
Author(s):  
David J. P. Ferguson ◽  
Nivedita Sahoo ◽  
Robert A. Pinches ◽  
Janene M. Bumstead ◽  
Fiona M. Tomley ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Sexual Development ◽  
Asexual Development ◽  
Basal Bodies ◽  
Gene Encoding ◽  
Membrane Complex ◽  
Spindle Poles ◽  
Sexual Stages ◽  
Inner Membrane Complex ◽  
Posterior Ring

ABSTRACT The gene encoding the membrane occupation and recognition nexus protein MORN1 is conserved across the Apicomplexa. In Toxoplasma gondii, MORN1 is associated with the spindle poles, the anterior and posterior rings of the inner membrane complex (IMC). The present study examines the localization of MORN1 during the coccidian development of T. gondii and three Eimeria species (in the definitive host) and erythrocytic schizogony of Plasmodium falciparum. During asexual proliferation, MORN1 is associated with the posterior ring of the IMCs of the multiple daughters forming during T. gondii endopolygeny and schizogony in Eimeria and P. falciparum. Furthermore, the expression of P. falciparum MORN1 protein peaked in late schizogony. These data fit a model with a conserved role for MORN1 during IMC assembly in all variations of asexual development. An important new observation is the reactivity of MORN1 antibody with certain sexual stages in T. gondii and Eimeria species. Here MORN1 is organized as a ring-like structure where the microgametes bud from the microgametocyte while in mature microgametes it is present near the flagellar basal bodies and mitochondrion. These observations suggest a conserved role for MORN1 in both asexual and sexual development across the Apicomplexa.

scholarly journals Two proteins isolated from sea urchin sperm flagella: structural components common to the stable microtubules of axonemes and centrioles

1998 ◽  
Vol 111 (5) ◽  
pp. 585-595 ◽  
Author(s):  
E.H. Hinchcliffe ◽  
R.W. Linck
Keyword(s):  
Sea Urchin ◽  
Cho Cells ◽  
Mammalian Cells ◽  
Sea Urchins ◽  
Polyclonal Antibodies ◽  
Chinese Hamster ◽  
Basal Bodies ◽  
Spindle Poles ◽  
Biochemical Fractionation ◽  
Sea Urchin Sperm

Biochemical fractionation of axonemal microtubules yields the protofilament ribbon (pf-ribbon), an insoluble structure of 3–4 longitudinal protofilaments composed primarily of alpha/beta tubulin, tektins A, B and C, and two previously uncharacterized polypeptides of 77 kDa and 83 kDa. We have isolated the 77/83 kDa polypeptides (termed Sp77 and Sp83) from sperm flagella of the sea urchin Stronglyocentrotus purpuratus and raised polyclonal antibodies against them. Sp77 and Sp83 copurify exclusively with the pf-ribbon. Both the anti-Sp77 and anti-Sp83 antibodies detected the nine outer doublets and the basal bodies of sea urchin sperm by immunofluorescence microscopy. In addition, the anti-Sp83 antibody, but not the anti-Sp77 antibody, detected a single 83 kDa polypeptide on immunoblots of unfertilized sea urchin egg cytoplasm, and a single polypeptide of 80 kDa on blots of isolated mitotic spindles from Chinese hamster ovary (CHO) cells. Previous studies have shown that tektins are present in the basal bodies and centrosomes/centrioles of cells ranging from clam to human. We found that anti-Sp83 decorates the spindle poles in sea urchin zygotes, and the interphase centrosome and spindle poles in CHO cells. In CHO cells arrested in S phase with aphidicolin, anti-Sp83 detects multiple centrosomes. The staining of the centrosome was not disrupted by prolonged nocodazole treatment, suggesting that the 80 kDa polypeptide is associated with the centrioles themselves. Our observations demonstrate that, like tektins, Sp77 and Sp83 are structural proteins associated with stable doublet microtubules, and may be components of basal bodies and centrioles of sea urchins and mammalian cells.

scholarly journals Production of Basal Bodies in bulk for dense multicilia formation

F1000Research ◽  
2016 ◽  
Vol 5 ◽  
pp. 1533 ◽  
Author(s):  
Xiumin Yan ◽  
Huijie Zhao ◽  
Xueliang Zhu
Keyword(s):  
Electron Microscopy ◽  
Mitotic Spindle ◽  
Molecular Mechanisms ◽  
Basal Bodies ◽  
Tight Control ◽  
Independent Manner ◽  
Spindle Poles ◽  
Multiciliated Cells ◽  
Mother Centriole ◽  
Daughter Centriole

Centriole number is normally under tight control and is directly linked to ciliogenesis. In cells that use centrosomes as mitotic spindle poles, one pre-existing mother centriole is allowed to duplicate only one daughter centriole per cell cycle. In multiciliated cells, however, many centrioles are generated to serve as basal bodies of the cilia. Although deuterosomes were observed more than 40 years ago using electron microscopy and are believed to produce most of the basal bodies in a mother centriole-independent manner, the underlying molecular mechanisms have remained unknown until recently. From these findings arise more questions and a call for clarifications that will require multidisciplinary efforts.

Ciliary coordination in newt lung cells requires microtubule-based linkages between basal bodies: A correlative light and EM study

1992 ◽  
Vol 50 (1) ◽  
pp. 570-571
Author(s):  
Robert Hard ◽  
Gerald Rupp ◽  
Matthew L. Withiam-Leitch ◽  
Lisa Cardamone
Keyword(s):  
Basal Body ◽  
Untreated Control ◽  
Beat Frequency ◽  
Primary Cultures ◽  
Living Cells ◽  
Power Stroke ◽  
Ultrastructural Changes ◽  
Lung Cells ◽  
Basal Bodies ◽  
Ciliated Cells

In a coordinated field of beating cilia, the direction of the power stroke is correlated with the orientation of basal body appendages, called basal feet. In newt lung ciliated cells, adjacent basal feet are interconnected by cold-stable microtubules (basal MTs). In the present study, we investigate the hypothesis that these basal MTs stabilize ciliary distribution and alignment. To accomplish this, newt lung primary cultures were treated with the microtubule disrupting agent, Colcemid. In newt lung cultures, cilia normally disperse in a characteristic fashion as the mucociliary epithelium migrates from the tissue explant. Four arbitrary, but progressive stages of dispersion were defined and used to monitor this redistribution process. Ciliaiy beat frequency, coordination, and dispersion were assessed for 91 hrs in untreated (control) and treated cultures. When compared to controls, cilia dispersed more rapidly and ciliary coordination decreased markedly in cultures treated with Colcemid (2 mM). Correlative LM/EM was used to assess whether these effects of Colcemid were coupled to ultrastructural changes. Living cells were defined as having coordinated or uncoordinated cilia and then were processed for transmission EM.

scholarly journals The mitotic spindle mediates inheritance of the Golgi ribbon structure

2009 ◽  
Vol 184 (3) ◽  
pp. 391-397 ◽  
Author(s):  
Jen-Hsuan Wei ◽  
Joachim Seemann
Keyword(s):  
Mitotic Spindle ◽  
Daughter Cell ◽  
Daughter Cells ◽  
Spindle Poles ◽  
Golgi Membranes ◽  
Ribbon Structure ◽  
Golgi Ribbon

The mammalian Golgi ribbon disassembles during mitosis and reforms in both daughter cells after division. Mitotic Golgi membranes concentrate around the spindle poles, suggesting that the spindle may control Golgi partitioning. To test this, cells were induced to divide asymmetrically with the entire spindle segregated into only one daughter cell. A ribbon reforms in the nucleated karyoplasts, whereas the Golgi stacks in the cytoplasts are scattered. However, the scattered Golgi stacks are polarized and transport cargo. Microinjection of Golgi extract together with tubulin or incorporation of spindle materials rescues Golgi ribbon formation. Therefore, the factors required for postmitotic Golgi ribbon assembly are transferred by the spindle, but the constituents of functional stacks are partitioned independently, suggesting that Golgi inheritance is regulated by two distinct mechanisms.

scholarly journals Functional Redundancy of the B9 Proteins and Nephrocystins in Caenorhabditis elegans Ciliogenesis

2008 ◽  
Vol 19 (5) ◽  
pp. 2154-2168 ◽  
Author(s):  
Corey L. Williams ◽  
Marlene E. Winkelbauer ◽  
Jenny C. Schafer ◽  
Edward J. Michaud ◽  
Bradley K. Yoder
Keyword(s):  
Caenorhabditis Elegans ◽  
Joubert Syndrome ◽  
Cystic Kidney ◽  
Basal Bodies ◽  
The Novel ◽  
C Elegans ◽  
Human Genes ◽  
Cilia Formation ◽  
Strong Candidate ◽  
Candidate Loci

Meckel-Gruber syndrome (MKS), nephronophthisis (NPHP), and Joubert syndrome (JBTS) are a group of heterogeneous cystic kidney disorders with partially overlapping loci. Many of the proteins associated with these diseases interact and localize to cilia and/or basal bodies. One of these proteins is MKS1, which is disrupted in some MKS patients and contains a B9 motif of unknown function that is found in two other mammalian proteins, B9D2 and B9D1. Caenorhabditis elegans also has three B9 proteins: XBX-7 (MKS1), TZA-1 (B9D2), and TZA-2 (B9D1). Herein, we report that the C. elegans B9 proteins form a complex that localizes to the base of cilia. Mutations in the B9 genes do not overtly affect cilia formation unless they are in combination with a mutation in nph-1 or nph-4, the homologues of human genes (NPHP1 and NPHP4, respectively) that are mutated in some NPHP patients. Our data indicate that the B9 proteins function redundantly with the nephrocystins to regulate the formation and/or maintenance of cilia and dendrites in the amphid and phasmid ciliated sensory neurons. Together, these data suggest that the human homologues of the novel B9 genes B9D2 and B9D1 will be strong candidate loci for pathologies in human MKS, NPHP, and JBTS.

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