| Autor: |
McMullin EL; Department of Medicine (Gastroenterology) and Cell Biology, Vanderbilt University School of Medicine, Nashville, TN 37232., Haas DW, Abramson RD, Thach RE, Merrick WC, Hagedorn CH |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1988 May 31; Vol. 153 (1), pp. 340-6. |
| DOI: |
10.1016/s0006-291x(88)81228-2 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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