Proteomic Screen Finds pSer/pThr-Binding Domain Localizing Plk1 to Mitotic Substrates

By A. Elia, Lewis C. Cantley, Michael B. Yaffe. Science, 2003

731 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/a8aa9d511dd2b19cefa903a2ab23b8ed0b59a7b7

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. K. Strebhardt
2. J. Pines
3. O. Gavet
4. J. Ferrell
5. Matthias Mann
6. Jesper V. Olsen
7. Lewis C. Cantley
8. A. Ullrich

In Molecular Biology

1. Matthias Mann
2. Jesper V. Olsen
3. Florian Gnad
4. K. Strebhardt
5. J. Pines
6. O. Gavet
7. J. Ferrell
8. Michael B. Yaffe

Citations in the corpus

• Targeting polo-like kinase 1 for cancer therapy (2006, background): “Two remarkable studies using oriented peptide libraries have shown that the PBD contains a phosphopeptide-binding moti”
• The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain. (2003, background): “Site-directed mutagenesis based on pThr-1 position with Val, the amino acid showing the the structural identification of critical phosphothreonine lowest selection in this position, was sufficient to elimibinding residues shows that phosphodependent sub- nate peptide binding (Elia et al., 2003).”
• Mechanisms of specificity in protein phosphorylation (2007, background): “For example, the polo-like kinase PLK1 contains a polo-box domain (PBD”
• Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. (2008, background): “The carboxyterminal polo box domain of PLK1, which targets this kinase to its primed mitotic substrates (Elia et al., 2003; Strebhardt and Ullrich, 2006), was found to harbor four additional phosphorylation sites that showed strong induction in mitosis, suggesting a role in the regulation of PLK1 su”
• The Polo kinase Plk4 functions in centriole duplication (2005, neutral): “Taken together, the above results demonstrate that cells depleted of Plk4 undergo a step-wise (4;2;1) loss of centrioles with continued passage through the cell cycle, indicating that Plk4 is indispensible for centriole duplication.”
• Progressive activation of CyclinB1-Cdk1 coordinates entry to mitosis. (2010, methodology): “, 2004) and YPet (Nguyen and Daugherty, 2005) fluorescent proteins, and as the phosphobinding domain we used the polo box domain (PBD) of Plk1 that binds to CDK phosphorylation sites in vivo (Elia et al., 2003).”