Identification of a protein kinase activity in rabbit reticulocytes that phosphorylates the mRNA cap binding protein.

Abstract	The 25 kDa mRNA cap binding protein can be purified in a partially phosphorylated state and the extent of its phosphorylation appears to be regulated during heat shock and mitosis in mammalian cells. We demonstrated that a nonabundant serine protein kinase activity exists in rabbit reticulocytes that phosphorylates the 25 kDa cap binding protein in both the free (eIF-4E) and complexed (eIF-4F) state. This kinase was not inhibited by the cAMP-dependent protein kinase inhibitory peptide IAAGRTGRRNAIHDILVAA, did not phosphorylate S6 ribosomal protein, did not phosphorylate p220 of eIF-4F as protein kinase C does and no other substrates for this kinase were apparent in reticulocyte ribosomal salt wash. The molecular identity of this kinase, the specific site(s) of eIF-4E that it phosphorylates and its in vivo regulatory role remain to be studied.
Authors	E L McMullin, D W Haas, R D Abramson, R E Thach, W C Merrick, C H Hagedorn
Journal	Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 153 Issue 1 Pg. 340-6 (May 31 1988) ISSN: 0006-291X [Print] United States
PMID	2967701 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S., Research Support, U.S. Gov't, P.H.S.)
Chemical References	Carrier Proteins Eukaryotic Initiation Factor-4E Eukaryotic Initiation Factor-4F Intracellular Signaling Peptides and Proteins Peptide Initiation Factors RNA Cap-Binding Proteins RNA Caps protein kinase modulator Protein Kinases Protein Serine-Threonine Kinases
Topics	Animals Carrier Proteins (metabolism, pharmacology) Eukaryotic Initiation Factor-4E Eukaryotic Initiation Factor-4F Intracellular Signaling Peptides and Proteins Peptide Initiation Factors (metabolism) Phosphorylation Protein Kinases (metabolism) Protein Serine-Threonine Kinases RNA Cap-Binding Proteins RNA Caps (metabolism) Rabbits Reticulocytes (enzymology)

Join CureHunter, for free Research Interface BASIC access!

Take advantage of free CureHunter research engine access to explore the best drug and treatment options for any disease. Find out why thousands of doctors, pharma researchers and patient activists around the world use CureHunter every day.

Realize the full power of the drug-disease research graph!