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  • 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 (en)
Title
  • Quantitative Analysis of the Human Spindle Phosphoproteome at Distinct Mitotic Stages
  • Quantitative Analysis of the Human Spindle Phosphoproteome at Distinct Mitotic Stages (en)
skos:prefLabel
  • Quantitative Analysis of the Human Spindle Phosphoproteome at Distinct Mitotic Stages
  • Quantitative Analysis of the Human Spindle Phosphoproteome at Distinct Mitotic Stages (en)
skos:notation
  • RIV/61989592:15310/09:00010597!RIV10-MSM-15310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(MSM6198959216)
http://linked.open...iv/cisloPeriodika
  • 10
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
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http://linked.open...dnocenehoVysledku
  • 337845
http://linked.open...ai/riv/idVysledku
  • RIV/61989592:15310/09:00010597
http://linked.open...riv/jazykVysledku
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  • mitosis; spindle; phosphorylation; kinase consensus; signaling (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [9C618EFB0E19]
http://linked.open...i/riv/nazevZdroje
  • Journal of Proteome Research
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 8
http://linked.open...iv/tvurceVysledku
  • Lenobel, René
  • Malik, Rainer
  • Koerner, Roman
  • Nigg, Erich A.
  • Ries, Albert
  • Santamaria, Anna
http://linked.open...n/vavai/riv/zamer
issn
  • 1535-3893
number of pages
http://localhost/t...ganizacniJednotka
  • 15310
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