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J. Biol. Chem., Vol. 265, Issue 27, 16556-16563, 09, 1990
WS Lai, DJ Stumpo and PJ Blackshear
By differential hybridization screening of a cDNA library derived from
insulin-stimulated cells, we selected a clone which hybridized to an mRNA
species that rapidly accumulated in response to insulin. The insert from
this clone encoded a putative polypeptide of Mr 33,600, pI 11.2; because
the protein was enriched in proline residues (14.4 mol %) and contained
three Pro-Pro-Pro-Pro repeats, we have tentatively labeled it
tris-tetraprolin (TTP). The function of this protein is not known, but it
contains two regions very rich in proline (30-40 mol %); similar
proline-rich regions have been shown to be involved in transcriptional
activation by other proteins. The mRNA (2.0 kilobases) encoding the TTP
protein was essentially undetectable in serum-deprived HIR 3.5 cells, but
accumulated dramatically within 10 min of stimulation by insulin. This
effect appeared to be due to insulin acting through the intrinsic
protein-tyrosine kinase activity of its own receptor. Insulin induction of
TTP mRNA accumulation was prevented by actinomycin D and superinduced by
cycloheximide. Accumulation of TTP mRNA was also stimulated by a variety of
growth factors and active phorbol esters; however, the insulin effect was
virtually normal in cells depleted of protein kinase C. A single TTP gene
appeared to be present in the mouse genome. This gene joins the group of
genes whose members are rapidly transcribed in response to insulin and
other mitogens.
Rapid insulin-stimulated accumulation of an mRNA encoding a proline- rich protein
Howard Hughes Medical Institute Laboratories, Durham, North Carolina 27710.
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