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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F09%3A00010597%21RIV10-MSM-15310___
rdf:type
n7:Vysledek skos:Concept
dcterms:description
During mitosis, phosphorylation of spindle associated proteins is a key regulatory mechanism for spindle formation, mitotic progression, and cytokinesis. In the recent past, mass spectrometry has been applied successfully to identify spindle proteomes and phosphoproteomes, but did not address their dynamics. Here, we present a quantitative comparison of spindle phosphoproteomes prepared from different mitotic stages. In total, we report the identification and SILAC based relative quantitation of 1940 unique phosphorylation sites and find that late mitosis (anaphase, telophase) is correlated with a drastic alteration in protein phosphorylation. Further statistical cluster analyses demonstrate a strong dependency of phosphorylation dynamics on kinase consensus patterns, thus, linking subgroups of identified phosphorylation sites to known key mitotic kinases. Surprisingly, we observed that during late mitosis strong dephosphorylation occurred on a significantly larger fraction of phospho-threonine than p During mitosis, phosphorylation of spindle associated proteins is a key regulatory mechanism for spindle formation, mitotic progression, and cytokinesis. In the recent past, mass spectrometry has been applied successfully to identify spindle proteomes and phosphoproteomes, but did not address their dynamics. Here, we present a quantitative comparison of spindle phosphoproteomes prepared from different mitotic stages. In total, we report the identification and SILAC based relative quantitation of 1940 unique phosphorylation sites and find that late mitosis (anaphase, telophase) is correlated with a drastic alteration in protein phosphorylation. Further statistical cluster analyses demonstrate a strong dependency of phosphorylation dynamics on kinase consensus patterns, thus, linking subgroups of identified phosphorylation sites to known key mitotic kinases. Surprisingly, we observed that during late mitosis strong dephosphorylation occurred on a significantly larger fraction of phospho-threonine than p
dcterms:title
Quantitative Analysis of the Human Spindle Phosphoproteome at Distinct Mitotic Stages Quantitative Analysis of the Human Spindle Phosphoproteome at Distinct Mitotic Stages
skos:prefLabel
Quantitative Analysis of the Human Spindle Phosphoproteome at Distinct Mitotic Stages Quantitative Analysis of the Human Spindle Phosphoproteome at Distinct Mitotic Stages
skos:notation
RIV/61989592:15310/09:00010597!RIV10-MSM-15310___
n3:aktivita
n9:Z
n3:aktivity
Z(MSM6198959216)
n3:cisloPeriodika
10
n3:dodaniDat
n6:2010
n3:domaciTvurceVysledku
n13:9896821
n3:druhVysledku
n18:J
n3:duvernostUdaju
n11:S
n3:entitaPredkladatele
n4:predkladatel
n3:idSjednocenehoVysledku
337845
n3:idVysledku
RIV/61989592:15310/09:00010597
n3:jazykVysledku
n17:eng
n3:klicovaSlova
mitosis; spindle; phosphorylation; kinase consensus; signaling
n3:klicoveSlovo
n10:signaling n10:spindle n10:kinase%20consensus n10:phosphorylation n10:mitosis
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[9C618EFB0E19]
n3:nazevZdroje
Journal of Proteome Research
n3:obor
n14:ED
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
6
n3:rokUplatneniVysledku
n6:2009
n3:svazekPeriodika
8
n3:tvurceVysledku
Lenobel, René Santamaria, Anna Nigg, Erich A. Malik, Rainer Ries, Albert Koerner, Roman
n3:zamer
n15:MSM6198959216
s:issn
1535-3893
s:numberOfPages
11
n12:organizacniJednotka
15310