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• W2034711912 endingPage "83" @default.
• W2034711912 startingPage "77" @default.
• W2034711912 abstract "The family of polo like kinases (Plks) regulate cell cycle progression through key functional roles in mitosis. While the four mammalian family members, Plk1-4, share overlapping functions, each member possesses unique functions that may be dictated in part by their ability to phosphorylate different substrates. Numerous cellular substrates for Plk1, 2, and 3 have been characterized, but the protein targets for Plk4/Sak remain unknown. We have purified the kinase domain of Sak and demonstrated that it has robust kinase activity in vitro. Using in vitro kinase assays on peptide spots arrays, we determined the consensus phosphorylation motif for Sak to be yen-[Ile/Leu/Val]-Ser/Thr-phi-phi-X- yen/Pro (where phi denotes a large hydrophobic residue, yen is a charged residue dependent on the context of the surrounding sequence, and residues in brackets are unfavoured). This consensus phosphorylation motif differs from that of Plk1, and provides a basis for future studies to identify in vivo substrates of Sak." @default.
• W2034711912 created "2016-06-24" @default.
• W2034711912 creator A5038574343 @default.
• W2034711912 creator A5049108001 @default.
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• W2034711912 creator A5064288188 @default.
• W2034711912 creator A5082249464 @default.
• W2034711912 date "2006-12-11" @default.
• W2034711912 modified "2023-09-27" @default.
• W2034711912 title "Determination of the Plk4/Sak consensus phosphorylation motif using peptide spots arrays" @default.
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• W2034711912 doi "https://doi.org/10.1016/j.febslet.2006.11.080" @default.
• W2034711912 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17174311" @default.
• W2034711912 hasPublicationYear "2006" @default.
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