eEF1A phosphorylation in the nucleus of insulin-stimulated C2C12 myoblasts: Ser53 is a novel substrate for protein kinase C betaI. (Articolo in rivista)

Type

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

Label

• eEF1A phosphorylation in the nucleus of insulin-stimulated C2C12 myoblasts: Ser53 is a novel substrate for protein kinase C betaI. (Articolo in rivista) (literal)

Anno

• 2010-01-01T00:00:00+01:00 (literal)

Alternative label

• Piazzi M, Bavelloni A, Faenza I, Blalock W, Urbani A, D'Aguanno S, Fiume R, Ramazzotti G, Maraldi NM, Cocco L. (2010)
  eEF1A phosphorylation in the nucleus of insulin-stimulated C2C12 myoblasts: Ser53 is a novel substrate for protein kinase C betaI.
  in Molecular & cellular proteomics
  (literal)

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

• Piazzi M, Bavelloni A, Faenza I, Blalock W, Urbani A, D'Aguanno S, Fiume R, Ramazzotti G, Maraldi NM, Cocco L. (literal)

Pagina inizio

• 2719 (literal)

Pagina fine

• 2728 (literal)

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

• 9 (literal)

Rivista

• Molecular & cellular proteomics (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• Cellular Signaling Laboratory, Department of Human Anatomical Sciences, University of Bologna, via Irnerio 48, 40126 Bologna, Italy, Laboratory of Cell Biology and Electron Microscopy, Istituti Ortopedici Rizzoli (I.O.R.), 40136 Bologna, Italy, stituto di Genetica Molecolare-Consiglio Nazionale delle Ricerche, Sezione di Bologna c/o I.O.R., 40136 Bologna, Italy, Laboratory of Proteomics, Istituto di Ricovero e Cura a Carattere Scientifico-Santa Lucia Foundation, 00100 Roma, Italy, Department of Internal Medicine, University of Rome Tor Vergata, 00133 Roma, Italy. (literal)

Titolo

• eEF1A phosphorylation in the nucleus of insulin-stimulated C2C12 myoblasts: Ser53 is a novel substrate for protein kinase C betaI. (literal)

Abstract

• Recent data indicate that some PKC isoforms are translocated to the nucleus, in response to certain stimuli, where they play an important role in nuclear signaling events. To identify novel interacting proteins of conventional PKC (cPKC) at the nuclear level during myogenesis and to find new PKC isozyme-specific phosphosubstrates, we performed a proteomics analysis of immunoprecipitated nuclear samples from mouse myoblast C2C12 cells following insulin administration. Using a phospho(Ser)-PKC substrate antibody, specific interacting proteins were identified by LC-MS/MS spectrometry. A total of 16 proteins with the exact and complete motif recognized by the phospho-cPKC substrate antibody were identified; among these, particular interest was given to eukaryotic elongation factor 1± (eEF1A). Nuclear eEF1A was focalized in the nucleoli, and its expression was observed to increase following insulin treatment. Of the cPKC isoforms, only PKC²I was demonstrated to be expressed in the nucleus of C2C12 myocytes and to co-immunoprecipitate with eEF1A. In-depth analysis using site-directed mutagenesis revealed that PKC²I could phosphorylate Seru³ of the eEF1A2 isoform and that the association between eEF1A2 and PKC²I was dependent on the phosphorylation status of eEF1A2. (literal)

Prodotto di

• Institute of molecular genetics (IGM) (Istituto)
• Bersagli molecolari per il controllo della progressione tumorale (ME.P03.012.001) (Modulo)

Autore CNR

• NADIR MARIO MARALDI (Unità di personale esterno)

Incoming links:

Prodotto

• Institute of molecular genetics (IGM) (Istituto)
• Bersagli molecolari per il controllo della progressione tumorale (ME.P03.012.001) (Modulo)

Autore CNR di

• NADIR MARIO MARALDI (Unità di personale esterno)

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

• Molecular & cellular proteomics (Rivista)