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Statements

Subject Item
n2:RIV%2F68378050%3A_____%2F14%3A00436610%21RIV15-GA0-68378050
rdf:type
skos:Concept n15:Vysledek
dcterms:description
Polo-like kinase-1 (Plk1) is required for proper cell division. Activation of Plk1 requires phosphorylation on a conserved threonine in the T-loop of the kinase domain (T210). Plk1 is first phosphorylated on T210 in G2 phase by the kinase Aurora-A, in concert with its cofactor Bora. However, Bora was shown to be degraded prior to entry into mitosis, and it is currently unclear how Plk1 activity is sustained in mitosis. Here we show that the Bora-Aurora-A complex remains the major activator of Plk1 in mitosis. We show that a small amount of Aurora-A activity is sufficient to phosphorylate and activate Plk1 in mitosis. In addition, a fraction of Bora is retained in mitosis, which is essential for continued Aurora-A-dependent T210 phosphorylation of Plk1. We find that once Plk1 is activated, minimal amounts of the Bora-Aurora-A complex are sufficient to sustain Plk1 activity. Thus, the activation of Plk1 by Aurora-A may function as a bistable switch; highly sensitive to inhibition of Aurora-A in its initial activation, but refractory to fluctuations in Aurora-A activity once Plk1 is fully activated. This provides a cell with robust Plk1 activity once it has committed to mitosis. Polo-like kinase-1 (Plk1) is required for proper cell division. Activation of Plk1 requires phosphorylation on a conserved threonine in the T-loop of the kinase domain (T210). Plk1 is first phosphorylated on T210 in G2 phase by the kinase Aurora-A, in concert with its cofactor Bora. However, Bora was shown to be degraded prior to entry into mitosis, and it is currently unclear how Plk1 activity is sustained in mitosis. Here we show that the Bora-Aurora-A complex remains the major activator of Plk1 in mitosis. We show that a small amount of Aurora-A activity is sufficient to phosphorylate and activate Plk1 in mitosis. In addition, a fraction of Bora is retained in mitosis, which is essential for continued Aurora-A-dependent T210 phosphorylation of Plk1. We find that once Plk1 is activated, minimal amounts of the Bora-Aurora-A complex are sufficient to sustain Plk1 activity. Thus, the activation of Plk1 by Aurora-A may function as a bistable switch; highly sensitive to inhibition of Aurora-A in its initial activation, but refractory to fluctuations in Aurora-A activity once Plk1 is fully activated. This provides a cell with robust Plk1 activity once it has committed to mitosis.
dcterms:title
Bora and Aurora-A continue to activate Plk1 in mitosis Bora and Aurora-A continue to activate Plk1 in mitosis
skos:prefLabel
Bora and Aurora-A continue to activate Plk1 in mitosis Bora and Aurora-A continue to activate Plk1 in mitosis
skos:notation
RIV/68378050:_____/14:00436610!RIV15-GA0-68378050
n3:aktivita
n12:P
n3:aktivity
P(GA13-18392S)
n3:cisloPeriodika
4
n3:dodaniDat
n18:2015
n3:domaciTvurceVysledku
n4:6785417
n3:druhVysledku
n8:J
n3:duvernostUdaju
n6:S
n3:entitaPredkladatele
n7:predkladatel
n3:idSjednocenehoVysledku
5694
n3:idVysledku
RIV/68378050:_____/14:00436610
n3:jazykVysledku
n17:eng
n3:klicovaSlova
Aurora-A; Bora; Mitosis; Plk1
n3:klicoveSlovo
n11:Aurora-A n11:Plk1 n11:Mitosis n11:Bora
n3:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n3:kontrolniKodProRIV
[626CEFCBD9AD]
n3:nazevZdroje
Journal of Cell Science
n3:obor
n13:EB
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
5
n3:projekt
n14:GA13-18392S
n3:rokUplatneniVysledku
n18:2014
n3:svazekPeriodika
127
n3:tvurceVysledku
Bruinsma, W. Freire, R. Macůrek, Libor Lindqvist, A. Medema, R. H.
n3:wos
000332114800010
s:issn
0021-9533
s:numberOfPages
11
n16:doi
10.1242/jcs.137216