scholarly journals Dictyostelium Aurora Kinase Has Properties of both Aurora A and Aurora B Kinases

2008 ◽  
Vol 7 (5) ◽  
pp. 894-905 ◽  
Author(s):  
Hui Li ◽  
Qian Chen ◽  
Markus Kaller ◽  
Wolfgang Nellen ◽  
Ralph Gräf ◽  
...  
Keyword(s):  
Myosin Ii ◽  
Aurora Kinase ◽  
Equatorial Region ◽  
Aurora B ◽  
Cleavage Furrow ◽  
Aurora A ◽  
Animal Cells ◽  
Aurora Kinases ◽  
Spindle Poles ◽  
Early Mitosis

ABSTRACT Aurora kinases are highly conserved proteins with important roles in mitosis. Metazoans contain two kinases, Aurora A and B, which contribute distinct functions at the spindle poles and the equatorial region respectively. It is not currently known whether the specialized functions of the two kinases arose after their duplication in animal cells or were already present in their ancestral kinase. We show that Dictyostelium discoideum contains a single Aurora kinase, DdAurora, that displays characteristics of both Aurora A and B. Like Aurora A, DdAurora has an extended N-terminal domain with an A-box sequence and localizes at the spindle poles during early mitosis. Like Aurora B, DdAurora binds to its partner DdINCENP and localizes on centromeres at metaphase, the central spindle during anaphase, and the cleavage furrow at the end of cytokinesis. DdAurora also has several unusual properties. DdAurora remains associated with centromeres in anaphase, and this association does not require an interaction with DdINCENP. DdAurora then localizes at the cleavage furrow, but only at the end of cytokinesis. This localization is dependent on DdINCENP and the motor proteins Kif12 and myosin II. Thus, DdAurora may represent the ancestral kinase that gave rise to the different Aurora kinases in animals and also those in other organisms.

scholarly journals Aurora A promotes chromosome congression by activating the condensin-dependent pool of KIF4A

2019 ◽  
Vol 219 (2) ◽  
Author(s):  
Elena Poser ◽  
Renaud Caous ◽  
Ulrike Gruneberg ◽  
Francis A. Barr
Keyword(s):  
Metaphase Plate ◽  
Aurora Kinase ◽  
Chromosome Condensation ◽  
Aurora B ◽  
Aurora A ◽  
Specific Point ◽  
Aurora Kinases ◽  
Central Spindle ◽  
Spindle Poles ◽  
Chromosome Congression

Aurora kinases create phosphorylation gradients within the spindle during prometaphase and anaphase, thereby locally regulating factors that promote spindle organization, chromosome condensation and movement, and cytokinesis. We show that one such factor is the kinesin KIF4A, which is present along the chromosome axes throughout mitosis and the central spindle in anaphase. These two pools of KIF4A depend on condensin I and PRC1, respectively. Previous work has shown KIF4A is activated by Aurora B at the anaphase central spindle. However, whether or not chromosome-associated KIF4A bound to condensin I is regulated by Aurora kinases remain unclear. To determine the roles of the two different pools of KIF4A, we generated specific point mutants that are unable to interact with either condensin I or PRC1 or are deficient for Aurora kinase regulation. By analyzing these mutants, we show that Aurora A phosphorylates the condensin I–dependent pool of KIF4A and thus actively promotes chromosome congression from the spindle poles to the metaphase plate.

scholarly journals Aurora A promotes chromosome congression by activating the condensin-dependent pool of KIF4A

2019 ◽  
Author(s):  
Elena Poser ◽  
Renaud Caous ◽  
Ulrike Gruneberg ◽  
Francis A. Barr
Keyword(s):  
Metaphase Plate ◽  
Aurora Kinase ◽  
Chromosome Condensation ◽  
Aurora B ◽  
Aurora A ◽  
Specific Point ◽  
Aurora Kinases ◽  
Central Spindle ◽  
Spindle Poles ◽  
Chromosome Congression

AbstractAurora kinases create phosphorylation gradients within the spindle during prometaphase and anaphase. These locally regulate factors that promote spindle organisation, chromosome condensation and movement, and cytokinesis. We show that one such factor is the kinesin KIF4A, which is present along the chromosome axes throughout mitosis and the central spindle in anaphase. These two pools of KIF4A depend on condensin I and PRC1, respectively. Previous work has shown KIF4A is activated by Aurora B at the anaphase central spindle. However, whether or not chromosome-associated KIF4A bound to condensin I is regulated by Aurora kinases remain unclear. To determine the roles of the two different pools of KIF4A, we generated specific point mutants that are unable to interact with either condensin I or PRC1, or are deficient for Aurora kinase regulation. By analysing these mutants, we show that Aurora kinases phosphorylate the condensin I dependent pool of KIF4A and thus actively promote chromosome congression from the spindle poles to the metaphase plate.

scholarly journals A single starfish Aurora kinase performs the combined functions of Aurora-A and Aurora-B in human cells

Development ◽  
2010 ◽  
Vol 137 (23) ◽  
pp. e2308-e2308
Author(s):  
Y. Abe ◽  
Y. Abe ◽  
E. Okumura ◽  
T. Hosoya ◽  
T. Hirota ◽  
...  
Keyword(s):  
Aurora Kinase ◽  
Human Cells ◽  
Aurora B ◽  
Aurora A

scholarly journals A single starfish Aurora kinase performs the combined functions of Aurora-A and Aurora-B in human cells

2010 ◽  
Vol 123 (22) ◽  
pp. 3978-3988 ◽  
Author(s):  
Y. Abe ◽  
E. Okumura ◽  
T. Hosoya ◽  
T. Hirota ◽  
T. Kishimoto
Keyword(s):  
Aurora Kinase ◽  
Human Cells ◽  
Aurora B ◽  
Aurora A

Role of myosin II tail sequences in its function and localization at the cleavage furrow in Dictyostelium

1999 ◽  
Vol 112 (13) ◽  
pp. 2195-2201 ◽  
Author(s):  
S. Shu ◽  
R.J. Lee ◽  
J.M. LeBlanc-Straceski ◽  
T.Q. Uyeda
Keyword(s):  
Myosin Head ◽  
Myosin Ii ◽  
Equatorial Region ◽  
Chain Gene ◽  
Cleavage Furrow ◽  
Tail Domain ◽  
Specific Domain ◽  
Dictyostelium Myosin ◽  
Skeletal Myosin

Cytoplasmic myosin II accumulates in the cleavage furrow and provides the force for cytokinesis in animal and amoeboid cells. One model proposes that a specific domain in the myosin II tail is responsible for its localization, possibly by interacting with a factor concentrated in the equatorial region. To test this possibility, we have expressed myosins carrying mutations in the tail domain in a strain of Dictyostelium cells from which the endogenous myosin heavy chain gene has been deleted. The mutations used in this study include four internal tail deletions: Mydelta824-941, Mydelta943-1464, Mydelta943-1194 and Mydelta1156-1464. Contrary to the prediction of the hypothesis, immunofluorescence staining demonstrated that all mutant myosins were able to move toward the furrow region. Chimeric myosins, which consisted of a Dictyostelium myosin head and chicken skeletal myosin tail, also efficiently localized to the cleavage furrow. All these deletion and chimeric mutant myosins, except for Mydelta943-1464, the largest deletion mutant, were able to support cytokinesis in suspension. Our data suggest that there is no single specific domain in the tail of Dictyostelium myosin II that is required for its functioning at and localization to the cleavage furrow.

scholarly journals A single amino acid change converts Aurora-A into Aurora-B-like kinase in terms of partner specificity and cellular function

2009 ◽  
Vol 106 (17) ◽  
pp. 6939-6944 ◽  
Author(s):  
Jingyan Fu ◽  
Minglei Bian ◽  
Junjun Liu ◽  
Qing Jiang ◽  
Chuanmao Zhang
Keyword(s):  
Amino Acid ◽  
Aurora Kinase ◽  
Single Amino Acid ◽  
Aurora B ◽  
Aurora A ◽  
Single Amino Acid Residue ◽  
Single Amino Acid Change ◽  
Equivalent Residue ◽  
And Function

Aurora kinase-A and -B are key regulators of the cell cycle and tumorigenesis. It has remained a mystery why these 2 Aurora kinases, although highly similar in protein sequence and structure, are distinct in subcellular localization and function. Here, we report the striking finding that a single amino acid residue is responsible for these differences. We replaced the Gly-198 of Aurora-A with the equivalent residue Asn-142 of Aurora-B and found that in HeLa cells, Aurora-AG198N was recruited to the inner centromere in metaphase and the midzone in anaphase, reminiscent of the Aurora-B localization. Moreover, Aurora-AG198N compensated for the loss of Aurora-B in chromosome misalignment and cell premature exit from mitosis. Furthermore, Aurora-AG198N formed a complex with the Aurora-B partners, INCENP and Survivin, and its localization depended on this interaction. Aurora-AG198N phosphorylated the Aurora-B substrates INCENP and Survivin in vitro. Therefore, we propose that the presence of Gly or Asn at a single site assigns Aurora-A and -B to their respective partners and thus to their distinctive subcellular localizations and functions.

scholarly journals Cytokinesis in vertebrate cells initiates by contraction of an equatorial actomyosin network composed of randomly oriented filaments

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Felix Spira ◽  
Sara Cuylen-Haering ◽  
Shalin Mehta ◽  
Matthias Samwer ◽  
Anne Reversat ◽  
...  
Keyword(s):  
Myosin Ii ◽  
Local Network ◽  
Polarization Microscopy ◽  
Cleavage Furrow ◽  
Mechanical Forces ◽  
Biological Processes ◽  
Actin Network ◽  
Animal Cells ◽  
Mechanical Tension ◽  
Cortical Tension

The actomyosin ring generates force to ingress the cytokinetic cleavage furrow in animal cells, yet its filament organization and the mechanism of contractility is not well understood. We quantified actin filament order in human cells using fluorescence polarization microscopy and found that cleavage furrow ingression initiates by contraction of an equatorial actin network with randomly oriented filaments. The network subsequently gradually reoriented actin filaments along the cell equator. This strictly depended on myosin II activity, suggesting local network reorganization by mechanical forces. Cortical laser microsurgery revealed that during cytokinesis progression, mechanical tension increased substantially along the direction of the cell equator, while the network contracted laterally along the pole-to-pole axis without a detectable increase in tension. Our data suggest that an asymmetric increase in cortical tension promotes filament reorientation along the cytokinetic cleavage furrow, which might have implications for diverse other biological processes involving actomyosin rings.

scholarly journals Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules

2002 ◽  
Vol 156 (3) ◽  
pp. 437-451 ◽  
Author(s):  
Régis Giet ◽  
Doris McLean ◽  
Simon Descamps ◽  
Michael J. Lee ◽  
Jordan W. Raff ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Aurora Kinase ◽  
The Other ◽  
S2 Cells ◽  
Aurora A Kinase ◽  
Aurora A ◽  
Spindle Poles

Disruption of the function of the A-type Aurora kinase of Drosophila by mutation or RNAi leads to a reduction in the length of astral microtubules in syncytial embryos, larval neuroblasts, and cultured S2 cells. In neuroblasts, it can also lead to loss of an organized centrosome and its associated aster from one of the spindle poles, whereas the centrosome at the other pole has multiple centrioles. When centrosomes are present at the poles of aurA mutants or aurA RNAi spindles, they retain many antigens but are missing the Drosophila counterpart of mammalian transforming acidic coiled coil (TACC) proteins, D-TACC. We show that a subpopulation of the total Aurora A is present in a complex with D-TACC, which is a substrate for the kinase. We propose that one of the functions of Aurora A kinase is to direct centrosomal organization such that D-TACC complexed to the MSPS/XMAP215 microtubule-associated protein may be recruited, and thus modulate the behavior of astral microtubules.

scholarly journals Cell polarization during monopolar cytokinesis

2008 ◽  
Vol 181 (2) ◽  
pp. 195-202 ◽  
Author(s):  
Chi-Kuo Hu ◽  
Margaret Coughlin ◽  
Christine M. Field ◽  
Timothy J. Mitchison
Keyword(s):  
Symmetry Breaking ◽  
Kinase Activity ◽  
Equatorial Region ◽  
Cell Polarization ◽  
Feedback Loops ◽  
Cell Cortex ◽  
Aurora B ◽  
Regional Specialization ◽  
Spindle Poles ◽  
Actin Cables

During cytokinesis, a specialized set of proteins is recruited to the equatorial region between spindle poles by microtubules and actin filaments, enabling furrow assembly and ingression before cell division. We investigate the mechanisms underlying regional specialization of the cytoskeleton in HeLa cells undergoing drug-synchronized monopolar cytokinesis. After forced mitotic exit, the cytoskeleton of monopolar mitotic cells is initially radially symmetric but undergoes a symmetry-breaking reaction that simultaneously polarizes microtubules and the cell cortex, with a concentration of cortical furrow markers into a cap at one side of the cell. Polarization requires microtubules, F-actin, RhoA, Myosin II activity, and Aurora B kinase activity. Aurora B localizes to actin cables in a gap between the monopolar midzone and the furrow-like cortex, suggesting a communication between them. We propose that feedback loops between cortical furrow components and microtubules promote symmetry breaking during monopolar cytokinesis and regional specialization of the cytoskeleton during normal bipolar cytokinesis.

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