scholarly journals Molecular characterization of centriole assembly in ciliated epithelial cells

2007 ◽  
Vol 178 (1) ◽  
pp. 31-42 ◽  
Author(s):  
Eszter K. Vladar ◽  
Tim Stearns
Keyword(s):  
Epithelial Cells ◽  
Mammalian Cells ◽  
Intraflagellar Transport ◽  
Proximal Region ◽  
Basal Bodies ◽  
Tracheal Epithelial Cells ◽  
Centriole Duplication ◽  
Centriole Assembly ◽  
Ciliated Epithelial Cells ◽  
Centrosomal Proteins

Ciliated epithelial cells have the unique ability to generate hundreds of centrioles during differentiation. We used centrosomal proteins as molecular markers in cultured mouse tracheal epithelial cells to understand this process. Most centrosomal proteins were up-regulated early in ciliogenesis, initially appearing in cytoplasmic foci and then incorporated into centrioles. Three candidate proteins were further characterized. The centrosomal component SAS-6 localized to basal bodies and the proximal region of the ciliary axoneme, and depletion of SAS-6 prevented centriole assembly. The intraflagellar transport component polaris localized to nascent centrioles before incorporation into cilia, and depletion of polaris blocked axoneme formation. The centriolar satellite component PCM-1 colocalized with centrosomal components in cytoplasmic granules surrounding nascent centrioles. Interfering with PCM-1 reduced the amount of centrosomal proteins at basal bodies but did not prevent centriole assembly. This system will help determine the mechanism of centriole formation in mammalian cells and how the limitation on centriole duplication is overcome in ciliated epithelial cells.

scholarly journals Cep120 is asymmetrically localized to the daughter centriole and is essential for centriole assembly

2010 ◽  
Vol 191 (2) ◽  
pp. 331-346 ◽  
Author(s):  
Moe R. Mahjoub ◽  
Zhigang Xie ◽  
Tim Stearns
Keyword(s):  
Basal Bodies ◽  
Animal Cells ◽  
Tracheal Epithelial Cells ◽  
Centriole Duplication ◽  
Photobleaching Recovery ◽  
Mother And Daughter ◽  
Tracheal Epithelial ◽  
Centriole Assembly ◽  
And Function ◽  
Daughter Centriole

Centrioles form the core of the centrosome in animal cells and function as basal bodies that nucleate and anchor cilia at the plasma membrane. In this paper, we report that Cep120 (Ccdc100), a protein previously shown to be involved in maintaining the neural progenitor pool in mouse brain, is associated with centriole structure and function. Cep120 is up-regulated sevenfold during differentiation of mouse tracheal epithelial cells (MTECs) and localizes to basal bodies. Cep120 localizes preferentially to the daughter centriole in cycling cells, and this asymmetry between mother and daughter centrioles is relieved coincident with new centriole assembly. Photobleaching recovery analysis identifies two pools of Cep120, differing in their halftime at the centriole. We find that Cep120 is required for centriole duplication in cycling cells, centriole amplification in MTECs, and centriole overduplication in S phase–arrested cells. We propose that Cep120 is required for centriole assembly and that the observed defect in neuronal migration might derive from a defect in this process.

scholarly journals Dishevelled controls apical docking and planar polarization of basal bodies in ciliated epithelial cells

2009 ◽  
Vol 331 (2) ◽  
pp. 486
Author(s):  
Philip B. Abitua ◽  
Tae Joo Park ◽  
Brian J. Mitchell ◽  
Chris Kintner ◽  
John B. Wallingford
Keyword(s):  
Epithelial Cells ◽  
Basal Bodies ◽  
Ciliated Epithelial Cells

scholarly journals Dishevelled controls apical docking and planar polarization of basal bodies in ciliated epithelial cells

2008 ◽  
Vol 40 (7) ◽  
pp. 871-879 ◽  
Author(s):  
Tae Joo Park ◽  
Brian J Mitchell ◽  
Philip B Abitua ◽  
Chris Kintner ◽  
John B Wallingford
Keyword(s):  
Epithelial Cells ◽  
Basal Bodies ◽  
Ciliated Epithelial Cells

Characterization of centrosomal proteins from ciliated epithelial cells in mammals

1995 ◽  
Vol 84 (1-2) ◽  
pp. 93-93
Author(s):  
Frédéric Tournier ◽  
Marie-Claude Gendron ◽  
Michel Bornens ◽  
Francelyne Marano
Keyword(s):  
Epithelial Cells ◽  
Ciliated Epithelial Cells ◽  
Centrosomal Proteins

scholarly journals Mycoplasma hyopneumoniae Increases Intracellular Calcium Release in Porcine Ciliated Tracheal Cells

2002 ◽  
Vol 70 (5) ◽  
pp. 2502-2506 ◽  
Author(s):  
Seung-Chun Park ◽  
Sirintorn Yibchok-Anun ◽  
Henrique Cheng ◽  
Theresa F. Young ◽  
Eileen L. Thacker ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Epithelial Cells ◽  
Phospholipase C ◽  
Pertussis Toxin ◽  
Calcium Release ◽  
Mycoplasma Hyopneumoniae ◽  
Tracheal Epithelial Cells ◽  
Tracheal Epithelial ◽  
Mycoplasma Flocculare ◽  
Ciliated Epithelial Cells

ABSTRACT We investigated the effects of intact pathogenic Mycoplasma hyopneumoniae, nonpathogenic M. hyopneumoniae, and Mycoplasma flocculare on intracellular free Ca2+ concentrations ([Ca2+]i) in porcine ciliated tracheal epithelial cells. The ciliated epithelial cells had basal [Ca2+]i of 103 ± 3 nM (n = 217 cells). The [Ca2+]i increased by 250 ± 19 nM (n = 47 cells) from the basal level within 100 s of the addition of pathogenic M. hyopneumoniae strain 91-3 (300 μg/ml), and this increase lasted ∼60 s. In contrast, nonpathogenic M. hyopneumoniae and M. flocculare at concentrations of 300 μg/ml failed to increase [Ca2+]i. In Ca2+-free medium, pathogenic M. hyopneumoniae still increased [Ca2+]i in tracheal cells. Pretreatment with thapsigargin (1 μM for 30 min), which depleted the Ca2+ store in the endoplasmic reticulum, abolished the effect of M. hyoneumoniae. Pretreatment with pertussis toxin (100 ng/ml for 3 h) or U-73122 (2 μM for 100 s), an inhibitor of phospholipase C, also abolished the effect of M. hyopneumoniae. The administration of mastoparan 7, an activator of pertussis toxin-sensitive proteins Gi and Go, increased [Ca2+]i in ciliated tracheal cells. These results suggest that pathogenic M. hyopneumoniae activates receptors that are coupled to Gi or Go, which in turn activates a phospholipase C pathway, thereby releasing Ca2+ from the endoplasmic reticulum. Thus, an increase in Ca2+ may serve as a signal for the pathogenesis of M. hyopneumoniae.

scholarly journals The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells

2014 ◽  
Vol 5 (1) ◽  
Author(s):  
Thibaut Eguether ◽  
Maria A. Ermolaeva ◽  
Yongge Zhao ◽  
Marion C. Bonnet ◽  
Ashish Jain ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Deubiquitinating Enzyme ◽  
Basal Bodies ◽  
Ciliated Epithelial Cells
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