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Molecular and Cellular Biology, March 2001, p. 2192-2202, Vol. 21, No. 6
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.6.2192-2202.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

ATF4 Degradation Relies on a Phosphorylation-Dependent Interaction with the SCFbeta TrCP Ubiquitin Ligase

Irina Lassot,1 Emmanuel Ségéral,1 Clarisse Berlioz-Torrent,1 Herve Durand,1 Lionel Groussin,2 Tsonwin Hai,3 Richard Benarous,1,* and Florence Margottin-Goguet1

INSERM Unite 529, Interactions Moléculaires Hôte-pathogène1 and CNRS, UPR 1524, Institut Cochin de Génétique Moléculaire,2 75014 Paris, France, and Department of Molecular and Cellular Biochemistry and Neurobiotechnology Center, Ohio State University, Columbus, Ohio3

Received 7 August 2000/Returned for modification 19 September 2000/Accepted 12 December 2000

The ubiquitin-proteasome pathway regulates gene expression through protein degradation. Here we show that the F-box protein beta TrCP, the receptor component of the SCF E3 ubiquitin ligase responsible for Ikappa Balpha and beta -catenin degradation, is colocalized in the nucleus with ATF4, a member of the ATF-CREB bZIP family of transcription factors, and controls its stability. Association between the two proteins depends on ATF4 phosphorylation and on ATF4 serine residue 219 present in the context of DSGXXXS, which is similar but not identical to the motif found in other substrates of beta TrCP. ATF4 ubiquitination in HeLa cells is enhanced in the presence of beta TrCP. The F-box-deleted beta TrCP protein behaves as a negative transdominant mutant that inhibits ATF4 ubiquitination and degradation and, subsequently, enhances its activity in cyclic AMP-mediated transcription. ATF4 represents a novel substrate for the SCFbeta TrCP complex, which is the first mammalian E3 ubiquitin ligase identified so far for the control of the degradation of a bZIP transcription factor.

* Corresponding author. Mailing address: INSERM Unite 529, ICGM, 24 rue de Faubourg Saint Jacques, 75014 Paris, France. Phone: 33 1 44 41 25 65. Fax: 33 1 44 41 23 99. E-mail: benarous{at}cochin.inserm.fr.

Molecular and Cellular Biology, March 2001, p. 2192-2202, Vol. 21, No. 6
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.6.2192-2202.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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