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Article ; Online: Cellular interpretation of the long-range gradient of Four-jointed activity in the Drosophila wing.

Hale, Rosalind / Brittle, Amy L / Fisher, Katherine H / Monk, Nicholas A M / Strutt, David

2015 Volume 4

Abstract: To understand how long-range patterning gradients are interpreted at the cellular level, we investigate how a gradient of expression of the Four-jointed kinase specifies planar polarised distributions of the cadherins Fat and Dachsous in the Drosophila ... ...

Abstract	To understand how long-range patterning gradients are interpreted at the cellular level, we investigate how a gradient of expression of the Four-jointed kinase specifies planar polarised distributions of the cadherins Fat and Dachsous in the Drosophila wing. We use computational modelling to test different scenarios for how Four-jointed might act and test the model predictions by employing fluorescence recovery after photobleaching as an in vivo assay to measure the influence of Four-jointed on Fat-Dachsous binding. We demonstrate that in vivo, Four-jointed acts both on Fat to promote its binding to Dachsous and on Dachsous to inhibit its binding to Fat, with a bias towards a stronger effect on Fat. Overall, we show that opposing gradients of Fat and Dachsous phosphorylation are sufficient to explain the observed pattern of Fat-Dachsous binding and planar polarisation across the wing, and thus demonstrate the mechanism by which a long-range gradient is interpreted.
MeSH term(s)	Animals ; Dimerization ; Drosophila/anatomy & histology ; Drosophila Proteins/physiology ; Humans ; Membrane Glycoproteins/physiology ; Phosphorylation
Chemical Substances	Drosophila Proteins ; Membrane Glycoproteins ; fj protein, Drosophila
Language	English
Publishing date	2015-02-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.05789
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Centrosome maturation: Aurora lights the way to the poles.

Brittle, Amy L / Ohkura, Hiroyuki

Current biology : CB

2005 Volume 15, Issue 21, Page(s) R880–2

Abstract: The centrosome is the main microtubule organising centre in the cell. During mitosis, centrosomes dramatically increase microtubule nucleating activity, enabling them to form a mitotic spindle. Recent studies show that Aurora A kinase promotes ... ...

Abstract	The centrosome is the main microtubule organising centre in the cell. During mitosis, centrosomes dramatically increase microtubule nucleating activity, enabling them to form a mitotic spindle. Recent studies show that Aurora A kinase promotes microtubule assembly from centrosomes through the phosphorylation of the conserved centrosomal protein TACC.
MeSH term(s)	Aurora Kinases ; Centrosome/physiology ; Drosophila Proteins/genetics ; Drosophila Proteins/physiology ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/physiology ; Microtubules/physiology ; Mitosis/physiology ; Models, Biological ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; Spindle Apparatus/physiology
Chemical Substances	Drosophila Proteins ; Microtubule-Associated Proteins ; TACC protein, Drosophila ; Aurora Kinases (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2005-11-08
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2005.10.022
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Article: Mini spindles, the XMAP215 homologue, suppresses pausing of interphase microtubules in Drosophila.

Brittle, Amy L / Ohkura, Hiroyuki

The EMBO journal

2005 Volume 24, Issue 7, Page(s) 1387–1396

Abstract: Drosophila Mini spindles (Msps) protein belongs to a conserved family of microtubule-associated proteins (MAPs). Intriguingly, this family of MAPs, including Xenopus XMAP215, was reported to have both microtubule stabilising and destabilising activities. ...

Abstract	Drosophila Mini spindles (Msps) protein belongs to a conserved family of microtubule-associated proteins (MAPs). Intriguingly, this family of MAPs, including Xenopus XMAP215, was reported to have both microtubule stabilising and destabilising activities. While they are shown to regulate various aspects of microtubules, the role in regulating interphase microtubules in animal cells has yet to be established. Here, we show that the depletion or mutation of Msps prevents interphase microtubules from extending to the cell periphery and leads to the formation of stable microtubule bundles. The effect is independent of known Msps regulator or effector proteins, kinesin-13/KinI homologues or D-TACC. Real-time analysis revealed that the depletion of Msps results in a dramatic increase of microtubule pausing with little or no growth. Our study provides the first direct evidence to support a hypothesis that this family of MAPs acts as an antipausing factor to exhibit both microtubule stabilising and destabilising activities.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cells, Cultured ; Drosophila/genetics ; Drosophila/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Fluorescence Recovery After Photobleaching ; Green Fluorescent Proteins ; Immunoblotting ; Interphase/physiology ; Microscopy, Fluorescence ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Microtubules/physiology ; Molecular Sequence Data ; RNA Interference ; Sequence Alignment
Chemical Substances	Drosophila Proteins ; Microtubule-Associated Proteins ; msps protein, Drosophila ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2005-03-17
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.1038/sj.emboj.7600629
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Article ; Online: Cellular interpretation of the long-range gradient of Four-jointed activity in the Drosophila wing

Rosalind Hale / Amy L Brittle / Katherine H Fisher / Nicholas A M Monk / David Strutt

eLife, Vol

2015 Volume 4

Abstract	To understand how long-range patterning gradients are interpreted at the cellular level, we investigate how a gradient of expression of the Four-jointed kinase specifies planar polarised distributions of the cadherins Fat and Dachsous in the Drosophila wing. We use computational modelling to test different scenarios for how Four-jointed might act and test the model predictions by employing fluorescence recovery after photobleaching as an in vivo assay to measure the influence of Four-jointed on Fat-Dachsous binding. We demonstrate that in vivo, Four-jointed acts both on Fat to promote its binding to Dachsous and on Dachsous to inhibit its binding to Fat, with a bias towards a stronger effect on Fat. Overall, we show that opposing gradients of Fat and Dachsous phosphorylation are sufficient to explain the observed pattern of Fat–Dachsous binding and planar polarisation across the wing, and thus demonstrate the mechanism by which a long-range gradient is interpreted.
Keywords	PCP ; planar polarity ; gradients ; Four-jointed ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2015-02-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Concerted action of Aurora B, Polo and NHK-1 kinases in centromere-specific histone 2A phosphorylation.

Brittle, Amy L / Nanba, Yasuaki / Ito, Takashi / Ohkura, Hiroyuki

Experimental cell research

2007 Volume 313, Issue 13, Page(s) 2780–2785

Abstract: The spatial and temporal control of histone modifications is crucial for precise regulation of chromatin structure and function. Here we report that phosphorylation of H2A at threonine 119 (T119) is enriched at centromere regions in Drosophila mitosis. ... ...

Abstract	The spatial and temporal control of histone modifications is crucial for precise regulation of chromatin structure and function. Here we report that phosphorylation of H2A at threonine 119 (T119) is enriched at centromere regions in Drosophila mitosis. We found that the Aurora B kinase complex is essential for this phosphorylation at centromeres, while Polo kinase is required to down-regulate H2A phosphorylation on chromosome arms in mitosis. Cyclin B degradation triggers loss of centromeric H2A phosphorylation at anaphase onset. Epistasis analysis indicated that Polo functions upstream of the H2A kinase NHK-1 but parallel to Aurora B. Therefore, multiple mitotic kinases work together to specify the spatial and temporal pattern of H2A T119 phosphorylation.
MeSH term(s)	Animals ; Aurora Kinases ; Centromere/chemistry ; Centromere/metabolism ; Drosophila/cytology ; Drosophila/genetics ; Drosophila/physiology ; Drosophila Proteins/antagonists & inhibitors ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Histones/analysis ; Histones/metabolism ; Mitosis ; Phosphorylation ; Protamine Kinase/antagonists & inhibitors ; Protamine Kinase/genetics ; Protamine Kinase/metabolism ; Protein-Serine-Threonine Kinases/antagonists & inhibitors ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism
Chemical Substances	Drosophila Proteins ; Histones ; polo protein, Drosophila (EC 2.7.11.-) ; Aurora Kinases (EC 2.7.11.1) ; Ball protein, Drosophila (EC 2.7.11.1) ; Protamine Kinase (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2007-05-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1016/j.yexcr.2007.04.038
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Article ; Online: Four-jointed modulates growth and planar polarity by reducing the affinity of dachsous for fat.

Brittle, Amy L / Repiso, Ada / Casal, José / Lawrence, Peter A / Strutt, David

Current biology : CB

2010 Volume 20, Issue 9, Page(s) 803–810

Abstract: The Drosophila genes fat (ft) and dachsous (ds) encode large atypical cadherins that collaborate to coordinately polarize cells in the plane of the epithelium (planar cell polarity) and to affect growth via the Warts/Hippo pathway. Ft and Ds form ... ...

Abstract	The Drosophila genes fat (ft) and dachsous (ds) encode large atypical cadherins that collaborate to coordinately polarize cells in the plane of the epithelium (planar cell polarity) and to affect growth via the Warts/Hippo pathway. Ft and Ds form heterodimeric bridges that convey polarity information from cell to cell. four-jointed (fj) is a modulator of Ft/Ds activity that acts in a graded fashion in the abdomen, eye, and wing. Genetic evidence indicates that Fj acts via Ds and/or Ft, and here we demonstrate that Fj can act independently on Ds and on Ft. It has been reported that Fj has kinase activity and can phosphorylate a subset of cadherin domains of both Ft and Ds in vitro. We have used both cell and in vitro assays to measure binding between Ft and Ds. We find that phosphorylation of Ds reduces its affinity for Ft in both of these assays. By expressing forms of Ds that lack the defined phosphorylation sites or have phosphomimetic amino acids at these positions, we demonstrate that effects of Fj on wing size and planar polarity can be explained by Fj phosphorylating these sites.
MeSH term(s)	Animals ; Binding Sites/genetics ; Binding Sites/physiology ; Blotting, Western ; Body Patterning/genetics ; Body Patterning/physiology ; Cadherins/genetics ; Cadherins/physiology ; Cell Adhesion Molecules/genetics ; Cell Adhesion Molecules/physiology ; Cells, Cultured ; Drosophila Proteins/genetics ; Drosophila Proteins/physiology ; Drosophila melanogaster/genetics ; Drosophila melanogaster/growth & development ; Gene Expression Regulation, Developmental/genetics ; Gene Expression Regulation, Developmental/physiology ; Genes, Developmental/genetics ; Genes, Developmental/physiology ; Immunoprecipitation ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/physiology ; Phosphorylation ; Point Mutation/genetics ; Wings, Animal/growth & development
Chemical Substances	Cadherins ; Cell Adhesion Molecules ; Drosophila Proteins ; Membrane Glycoproteins ; ds protein, Drosophila ; fj protein, Drosophila ; ft protein, Drosophila
Language	English
Publishing date	2010-04-29
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2010.03.056
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Article: The conserved kinase NHK-1 is essential for mitotic progression and unifying acentrosomal meiotic spindles in Drosophila melanogaster.

Cullen, C Fiona / Brittle, Amy L / Ito, Takashi / Ohkura, Hiroyuki

The Journal of cell biology

2005 Volume 171, Issue 4, Page(s) 593–602

Abstract: Conventional centrosomes are absent from the spindle in female meiosis in many species, but it is not clear how multiple chromosomes form one shared bipolar spindle without centrosomes. We identified a female sterile mutant in which each bivalent ... ...

Abstract	Conventional centrosomes are absent from the spindle in female meiosis in many species, but it is not clear how multiple chromosomes form one shared bipolar spindle without centrosomes. We identified a female sterile mutant in which each bivalent chromosome often forms a separate bipolar metaphase I spindle. Unlike wild type, prophase I chromosomes fail to form a single compact structure within the oocyte nucleus, although the integrity of metaphase I chromosomes appears to be normal. Molecular analysis indicates that the mutant is defective in the conserved kinase nucleosomal histone kinase-1 (NHK-1). Isolation of further alleles and RNA interference in S2 cells demonstrated that NHK-1 is also required for mitotic progression. NHK-1 itself is phosphorylated in mitosis and female meiosis, suggesting that this kinase is part of the regulatory system coordinating progression of mitosis and meiosis.
MeSH term(s)	Alleles ; Animals ; Cell Cycle ; Cell Line ; Cell Nucleus/metabolism ; Centrosome/ultrastructure ; Chromosomes/ultrastructure ; Drosophila Proteins/chemistry ; Drosophila melanogaster/physiology ; Female ; Meiosis ; Mitosis ; Models, Biological ; Models, Genetic ; Mutation ; Oocytes/metabolism ; Phenotype ; Phosphorylation ; Protamine Kinase/genetics ; Protamine Kinase/physiology ; Spindle Apparatus
Chemical Substances	Drosophila Proteins ; Ball protein, Drosophila (EC 2.7.11.1) ; Protamine Kinase (EC 2.7.11.1)
Language	English
Publishing date	2005-11-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.200508127
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Article: Dual roles of Incenp crucial to the assembly of the acentrosomal metaphase spindle in female meiosis.

Colombié, Nathalie / Cullen, C Fiona / Brittle, Amy L / Jang, Janet K / Earnshaw, William C / Carmena, Mar / McKim, Kim / Ohkura, Hiroyuki

Development (Cambridge, England)

2008 Volume 135, Issue 19, Page(s) 3239–3246

Abstract: Spindle formation in female meiosis differs from mitosis in many animals, as it takes place independently of centrosomes, and the molecular requirements of this pathway remain to be understood. Here, we report two crucial roles of Incenp, an essential ... ...

Abstract	Spindle formation in female meiosis differs from mitosis in many animals, as it takes place independently of centrosomes, and the molecular requirements of this pathway remain to be understood. Here, we report two crucial roles of Incenp, an essential subunit of the chromosomal passenger complex (the Aurora B complex), in centrosome-independent spindle formation in Drosophila female meiosis. First, the initial assembly of spindle microtubules is drastically delayed in an incenp mutant. This clearly demonstrates, for the first time, a crucial role for Incenp in chromosome-driven spindle microtubule assembly in living oocytes. Additionally, Incenp is necessary to stabilise the equatorial region of the metaphase I spindle, in contrast to mitosis, where the equivalent function becomes prominent after anaphase onset. Our analysis suggests that Subito, a kinesin-6 protein, cooperates with Incenp for this latter function, but not in microtubule assembly. We propose that the two functions of Incenp are part of the mechanisms that compensate for the lack of centrosomes during meiotic spindle formation.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Centrosome/physiology ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/physiology ; Drosophila/cytology ; Drosophila/genetics ; Drosophila/physiology ; Drosophila Proteins/genetics ; Drosophila Proteins/physiology ; Female ; Genes, Insect ; Kinesin/physiology ; Meiosis/genetics ; Meiosis/physiology ; Metaphase/genetics ; Metaphase/physiology ; Microtubules/physiology ; Mutation
Chemical Substances	Chromosomal Proteins, Non-Histone ; Drosophila Proteins ; Incenp protein, Drosophila ; SUB protein, Drosophila ; Kinesin (EC 3.6.4.4)
Language	English
Publishing date	2008-08-28
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.022624
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Article: The conserved kinase NHK-1 is essential for mitotic progression and unifying acentrosomal meiotic spindles in Drosophila melanogaster

Cullen, C. Fiona / Brittle, Amy L / Ito, Takashi / Ohkura, Hiroyuki

Journal of cell biology. 2005 Nov. 21, v. 171, no. 4

2005

Abstract	Conventional centrosomes are absent from the spindle in female meiosis in many species, but it is not clear how multiple chromosomes form one shared bipolar spindle without centrosomes. We identified a female sterile mutant in which each bivalent chromosome often forms a separate bipolar metaphase I spindle. Unlike wild type, prophase I chromosomes fail to form a single compact structure within the oocyte nucleus, although the integrity of metaphase I chromosomes appears to be normal. Molecular analysis indicates that the mutant is defective in the conserved kinase nucleosomal histone kinase-1 (NHK-1). Isolation of further alleles and RNA interference in S2 cells demonstrated that NHK-1 is also required for mitotic progression. NHK-1 itself is phosphorylated in mitosis and female meiosis, suggesting that this kinase is part of the regulatory system coordinating progression of mitosis and meiosis.
Language	English
Dates of publication	2005-1121
Size	p. 593-602.
Document type	Article
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
Database	NAL-Catalogue (AGRICOLA)

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