RGD Reference Report - Role of calmodulin-dependent phosphorylation of elongation factor 2 in the proliferation of rat glial cells. - Rat Genome Database

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Role of calmodulin-dependent phosphorylation of elongation factor 2 in the proliferation of rat glial cells.

Authors: Bagaglio, DM  Hait, WN 
Citation: Bagaglio DM and Hait WN, Cell Growth Differ. 1994 Dec;5(12):1403-8.
RGD ID: 10401648
Pubmed: PMID:7696190   (View Abstract at PubMed)

Calmodulin (CaM) is believed to play an important role in the regulation of cellular proliferation. The mechanism of regulation, although unknown, may involve CaM-binding proteins, particularly CaM-dependent protein kinases. Previously, we have shown that CaM-dependent protein kinase III phosphorylates elongation factor 2 (EF-2) in proliferating, C6 glioma cells but not in normal white matter, a tissue rich in nonproliferating glia. To determine whether CaM-dependent phosphorylation of EF-2 is linked, in general, to cellular division, we studied the phosphorylation of EF-2 in proliferating and growth-arrested C6 cells and in proliferating, primary cultures of normal glia. Phosphorylation of EF-2 was not detectable in C6 cells arrested in their growth by serum deprivation. When serum-deprived cells were stimulated to proliferate by the re-addition of serum, the amount of phosphorylated EF-2 correlated with levels of [3H]thymidine incorporation into DNA. Primary cultures of dividing, normal glia, obtained from neonatal rats, also demonstrated phosphorylation of EF-2. Therefore, the CaM-dependent phosphorylation of EF-2 appears to be associated with cellular proliferation in normal and malignant glia in the rat.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
glial cell proliferation  IEP 10401648 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Eef2  (eukaryotic translation elongation factor 2)


Additional Information