Journal article

Determination of the Plk4/Sak consensus phosphorylation motif using peptide spots arrays

Genie C Leung, Cynthia SW Ho, Ivan M Blasutig, James M Murphy, Frank Sicheri

FEBS LETTERS | ELSEVIER SCIENCE BV | Published : 2007

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- y..

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University of Melbourne Researchers