Identification of the PLK2-dependent phosphopeptidome by quantitative proteomics [corrected].

Polo-like kinase 2 (PLK2) has been recently recognized as the major enzyme responsible for phosphorylation of α-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...

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Autores principales:	Cinzia Franchin, Luca Cesaro, Lorenzo A Pinna, Giorgio Arrigoni, Mauro Salvi
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ea46d60780044c449416f199c31e334a
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spelling	oai:doaj.org-article:ea46d60780044c449416f199c31e334a2021-11-25T05:55:31ZIdentification of the PLK2-dependent phosphopeptidome by quantitative proteomics [corrected].1932-620310.1371/journal.pone.0111018https://doaj.org/article/ea46d60780044c449416f199c31e334a2014-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0111018https://doaj.org/toc/1932-6203Polo-like kinase 2 (PLK2) has been recently recognized as the major enzyme responsible for phosphorylation of α-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.Cinzia FranchinLuca CesaroLorenzo A PinnaGiorgio ArrigoniMauro SalviPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 10, p e111018 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Cinzia Franchin Luca Cesaro Lorenzo A Pinna Giorgio Arrigoni Mauro Salvi Identification of the PLK2-dependent phosphopeptidome by quantitative proteomics [corrected].
description	Polo-like kinase 2 (PLK2) has been recently recognized as the major enzyme responsible for phosphorylation of α-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.
format	article
author	Cinzia Franchin Luca Cesaro Lorenzo A Pinna Giorgio Arrigoni Mauro Salvi
author_facet	Cinzia Franchin Luca Cesaro Lorenzo A Pinna Giorgio Arrigoni Mauro Salvi
author_sort	Cinzia Franchin
title	Identification of the PLK2-dependent phosphopeptidome by quantitative proteomics [corrected].
title_short	Identification of the PLK2-dependent phosphopeptidome by quantitative proteomics [corrected].
title_full	Identification of the PLK2-dependent phosphopeptidome by quantitative proteomics [corrected].
title_fullStr	Identification of the PLK2-dependent phosphopeptidome by quantitative proteomics [corrected].
title_full_unstemmed	Identification of the PLK2-dependent phosphopeptidome by quantitative proteomics [corrected].
title_sort	identification of the plk2-dependent phosphopeptidome by quantitative proteomics [corrected].
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/ea46d60780044c449416f199c31e334a
work_keys_str_mv	AT cinziafranchin identificationoftheplk2dependentphosphopeptidomebyquantitativeproteomicscorrected AT lucacesaro identificationoftheplk2dependentphosphopeptidomebyquantitativeproteomicscorrected AT lorenzoapinna identificationoftheplk2dependentphosphopeptidomebyquantitativeproteomicscorrected AT giorgioarrigoni identificationoftheplk2dependentphosphopeptidomebyquantitativeproteomicscorrected AT maurosalvi identificationoftheplk2dependentphosphopeptidomebyquantitativeproteomicscorrected
_version_	1718414434203860992

Identification of the PLK2-dependent phosphopeptidome by quantitative proteomics [corrected].

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