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Mol Cell Biol, April 1998, p. 2038-2044, Vol. 18, No. 4
Friedrich Miescher-Institute, CH-4002 Basel,
Switzerland,1 and
Plant Biology
Institute, Biological Research Center, H-6701 Szeged,
Hungary2
Received 13 October 1997/Returned for modification 10 December
1997/Accepted 7 January 1998
In mammalian cells, mitogen-induced phosphorylation of ribosomal
protein S6 by p70s6k has been implicated in the selective
translational upregulation of 5'TOP mRNAs. We demonstrate here that the
homologous Arabidopsis thaliana protein, AtS6k2,
ectopically expressed in human 293 cells or isolated from plant cells,
phosphorylates specifically mammalian and plant S6 at 25°C but not at
37°C. When Arabidopsis suspension culture cells are
shifted from 25 to 37°C, the kinase becomes rapidly inactivated,
consistent with the observation that heat shock abrogates S6
phosphorylation in plants. Treatment with potato acid phosphatase
reduced the specific activity of immunoprecipitated AtS6k2 threefold,
an effect which was blocked in the presence of 4-nitrophenyl phosphate.
In quiescent mammalian cells, AtS6k2 is activated by serum stimulation,
a response which is abolished by the fungal metabolite wortmannin but
is resistant to rapamycin. Treatment of mammalian cells with rapamycin
abolishes in vivo S6 phosphorylation by p70s6k; however,
ectopic expression of AtS6k2 rescues the rapamycin block. Collectively,
the data demonstrate that AtS6k2 is the functional plant homolog of
mammalian p70s6k and identify a new signalling pathway in
plants.
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
A Heat-Sensitive Arabidopsis thaliana
Kinase Substitutes for Human p70s6k Function In
Vivo
*
Corresponding author. Mailing address for George
Thomas: Friedrich Miescher-Institute, P.O. Box 2543, CH-4002 Basel,
Switzerland. Phone: 41-61-6973012. Fax: 41-61-6976681. E-mail:
gthomas{at}fmi.ch. Mailing address for Ferenc Nagy: Plant Biology
Institute, Biological Research Center, P.O. Box 521, H-6701 Szeged,
Hungary. Phone: 36-62-432 232. Fax: 36-62-433 434. E-mail:
nagyf{at}everx.szbk.u-szeged.hu.
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