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Staurosporine inhibits phosphorylation of translational regulators linked to mTOR

Staurosporine inhibits phosphorylation of translational regulators linked to mTOR
Staurosporine inhibits phosphorylation of translational regulators linked to mTOR
Treatment of Swiss 3T3 cells with staurosporine resulted in dephosphorylation of two proteins which play key roles in regulating mRNA translation. This occurred before the execution of apoptosis, assessed by caspase-3 activity. These translation regulators are p70 S6 kinase, which phosphorylates ribosomal protein S6, and eukaryotic initiation factor (eIF) 4E binding protein 1 (4E-BP1), which both lie downstream of the mammalian target of rapamycin (mTOR). This resulted in decreased p70 S6 kinase activity, dephosphorylation of ribosomal protein S6, increased binding of 4E-BP1 to eIF4E and a concomitant decrease in eIF4F complexes. Our data show that staurosporine impairs mTOR signalling in vivo but that this not due to direct inhibition of mTOR or to inhibition of protein kinase C. It is becoming clear that agents which cause apoptosis inactivate mTOR signalling as a common early response prior to the execution of apoptosis, i.e., before caspase activation.
1350-9047
841-849
Tee, A.R.
1b63bc1f-d26b-447f-9429-e83d2468e068
Proud, C.G.
c2cc50f9-4565-4d59-9dfc-aa70b9268a6e
Tee, A.R.
1b63bc1f-d26b-447f-9429-e83d2468e068
Proud, C.G.
c2cc50f9-4565-4d59-9dfc-aa70b9268a6e

Tee, A.R. and Proud, C.G. (2001) Staurosporine inhibits phosphorylation of translational regulators linked to mTOR. Cell Death and Differentiation, 8 (8), 841-849.

Record type: Article

Abstract

Treatment of Swiss 3T3 cells with staurosporine resulted in dephosphorylation of two proteins which play key roles in regulating mRNA translation. This occurred before the execution of apoptosis, assessed by caspase-3 activity. These translation regulators are p70 S6 kinase, which phosphorylates ribosomal protein S6, and eukaryotic initiation factor (eIF) 4E binding protein 1 (4E-BP1), which both lie downstream of the mammalian target of rapamycin (mTOR). This resulted in decreased p70 S6 kinase activity, dephosphorylation of ribosomal protein S6, increased binding of 4E-BP1 to eIF4E and a concomitant decrease in eIF4F complexes. Our data show that staurosporine impairs mTOR signalling in vivo but that this not due to direct inhibition of mTOR or to inhibition of protein kinase C. It is becoming clear that agents which cause apoptosis inactivate mTOR signalling as a common early response prior to the execution of apoptosis, i.e., before caspase activation.

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Published date: August 2001

Identifiers

Local EPrints ID: 55954
URI: http://eprints.soton.ac.uk/id/eprint/55954
ISSN: 1350-9047
PURE UUID: 19783e5c-14bd-470c-bf33-aefff8226bd5

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Date deposited: 07 Aug 2008
Last modified: 07 Jan 2022 22:32

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Contributors

Author: A.R. Tee
Author: C.G. Proud

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