Identification of the PLK2-Dependent Phosphopeptidome by Quantitative Proteomics (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Identification of the PLK2-Dependent Phosphopeptidome by Quantitative Proteomics (Articolo in rivista) (literal)

Anno

• 2014-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1371/journal.pone.0114202 (literal)

Alternative label

• Franchin, C.; Cesaro, L.; Pinna, L. A.; Arrigoni, G.; Salvi, M. (2014)
  Identification of the PLK2-Dependent Phosphopeptidome by Quantitative Proteomics
  in PloS one
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Franchin, C.; Cesaro, L.; Pinna, L. A.; Arrigoni, G.; Salvi, M. (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 9 (literal)

Rivista

• PloS one (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 1 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 11 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• 1, 4: Department of Biomedical Sciences, University of Padova, Padova, Italy / Proteomics Center of Padova University, Padova, Italy; 2, 5: Department of Biomedical Sciences, University of Padova, Padova, Italy; 3: Department of Biomedical Sciences, University of Padova, Padova, Italy / CNR Institute of Neurosciences, Padova, Italy (literal)

Titolo

• Identification of the PLK2-Dependent Phosphopeptidome by Quantitative Proteomics (literal)

Abstract

• Polo-like kinase 2 (PLK2) has been recently recognized as the major enzyme responsible for phosphorylation of a-synuclein at S129 in vitro and in vivo, suggesting that this kinase may play a key role in the pathogenesis of Parkinson's disease and other synucleinopathies. Moreover PLK2 seems to be implicated in cell division, oncogenesis, and synaptic regulation of the brain. However little is known about the phosphoproteome generated by PLK2 and, consequently the overall impact of PLK2 on cellular signaling. To fill this gap we exploited an approach based on in vitro kinase assay and quantitative phosphoproteomics. A proteome-derived peptide library obtained by digestion of undifferentiated human neuroblastoma cell line was exhaustively dephosphorylated by lambda phosphatase followed by incubation with or without PLK2 recombinant kinase. Stable isotope labeling based quantitative phosphoproteomics was applied to identify the phosphosites generated by PLK2. A total of 98 unique PLK2-dependent phosphosites from 89 proteins were identified by LC-MS/MS. Analysis of the primary structure of the identified phosphosites allowed the detailed definition of the kinase specificity and the compilation of a list of potential PLK2 targets among those retrieved in PhosphositePlus, a curated database of in cell/vivo phosphorylation sites (literal)

Prodotto di

• Institute of neuroscience (IN) (Istituto)
• Neurobiologia e Neuropatologia (ME.P02.005.001) (Modulo)

Autore CNR

• LORENZO PINNA (Persona)

Incoming links:

Prodotto

• Institute of neuroscience (IN) (Istituto)
• Neurobiologia e Neuropatologia (ME.P02.005.001) (Modulo)

Autore CNR di

• LORENZO PINNA (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• PloS one (Rivista)