title: Multiple phosphorylation sites and quaternary organization of guanine-nucleotide exchange complex of elongation factor-1 (EF-1betagammadelta/ValRS) control the various functions of EF-1alpha.
abstract: The eukaryotic guanine-nucleotide exchange factor commonly called elongation factor-1 betagammadelta (EF-1betagammadelta), comprises four different subunits including valyl-tRNA synthetase (EF-1betagammadelta/ValRS). The factor is multiply-phosphorylated by three different protein kinases, protein kinase C, casein kinase II and cyclin dependent kinase 1 (CDKI). EF-1betagammadelta/ValRS is organized as a macromolecular complex for which we propose a new structural model. Evidence that EF-1betagammadelta/ValRS is a sophisticated supramolecular complex containing many phosphorylation sites, makes it a potential regulator of any of the functions of its partner EF-1alpha, not only involved in protein synthesis elongation, but also in many other cellular functions.
authors.affiliation: Biologie Cellulaire de l'Ovocyte. Station Biologique de Roscoff, Centre National de la Recherche Scientifique (CNRS UPR 9042), Université Pierre et Marie Curie, Roscoff, France.
authors.forename: O
authors.initials: O
authors.lastname: Minella
authors.forename: O
authors.initials: O
authors.lastname: Mulner-Lorillon
authors.forename: G
authors.initials: G
authors.lastname: Bec
authors.forename: P
authors.initials: P
authors.lastname: Cormier
authors.forename: R
authors.initials: R
authors.lastname: Bellé
mesh_terms: D001665:Binding Sites; D020662:Guanine Nucleotide Exchange Factors; D008958:Models, Molecular; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D010766:Phosphorylation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*
chemical_list: D020662:Guanine Nucleotide Exchange Factors; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D011506:Proteins