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.
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.
Minella
O
O
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.
Mulner-Lorillon
O
O
Bec
G
G
Cormier
P
P
Bellé
R
R
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*
D020662:Guanine Nucleotide Exchange Factors; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D011506:Proteins