Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Originally published in Science Express on 18 August 2005
Science 26 August 2005:
Vol. 309. no. 5739, pp. 1390 - 1394
DOI: 10.1126/science.1110689
Prev | Table of Contents | Next

Reports

Circadian Clock Control by SUMOylation of BMAL1

Luca Cardone,1 Jun Hirayama,1 Francesca Giordano,1 Teruya Tamaru,2 Jorma J. Palvimo,3* Paolo Sassone-Corsi1{dagger}

The molecular machinery that governs circadian rhythmicity is based on clock proteins organized in regulatory feedback loops. Although posttranslational modification of clock proteins is likely to finely control their circadian functions, only limited information is available to date. Here, we show that BMAL1, an essential transcription factor component of the clock mechanism, is SUMOylated on a highly conserved lysine residue (Lys259) in vivo. BMAL1 shows a circadian pattern of SUMOylation that parallels its activation in the mouse liver. SUMOylation of BMAL1 requires and is induced by CLOCK, the heterodimerization partner of BMAL1. Ectopic expression of a SUMO-deficient BMAL1 demonstrates that SUMOylation plays an important role in BMAL1 circadian expression and clock rhythmicity. This reveals an additional level of regulation within the core mechanism of the circadian clock.

1 Institut de Génétique et de Biologie Moléculaire et Cellulaire, 1 rue Laurent Fries, 67404 Illkirch, Strasbourg, France.
2 Department of Physiology, Toho University School of Medicine, 5-21-16 Ohmori-nishi Ohta-ku, Tokyo 143-8540, Japan.
3 Biomedicum Helsinki, Institute of Biomedicine, Post Office Box 63, University of Helsinki, 00014 Helsinki, Finland.

* Present address: Department of Medical Biochemistry, University of Kuopio, 70211 Kuopio, Finland.

{dagger} To whom correspondence should be addressed. E-mail: paolosc{at}igbmc.u-strasbg.fr

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Circadian Organization oftau Mutant Hamsters: Aftereffects and Splitting.
E. L. Bittman, M. K. Costello, and J. McKinley Brewer (2007)
J Biol Rhythms 22, 425-431
   Abstract »    PDF »
The After-Hours Mutant Reveals a Role for Fbxl3 in Determining Mammalian Circadian Period.
S. I. H. Godinho, E. S. Maywood, L. Shaw, V. Tucci, A. R. Barnard, L. Busino, M. Pagano, R. Kendall, M. M. Quwailid, M. R. Romero, et al. (2007)
Science 316, 897-900
   Abstract »    Full Text »    PDF »
Molecular components of the mammalian circadian clock.
C. H. Ko and J. S. Takahashi (2006)
Hum. Mol. Genet. 15, R271-R277
   Abstract »    Full Text »    PDF »
BMAL1 Shuttling Controls Transactivation and Degradation of the CLOCK/BMAL1 Heterodimer..
I. Kwon, J. Lee, S. H. Chang, N. C. Jung, B. J. Lee, G. H. Son, K. Kim, and K. H. Lee (2006)
Mol. Cell. Biol. 26, 7318-7330
   Abstract »    Full Text »    PDF »
The BMAL1 C terminus regulates the circadian transcription feedback loop.
Y. B. Kiyohara, S. Tagao, F. Tamanini, A. Morita, Y. Sugisawa, M. Yasuda, I. Yamanaka, H. R. Ueda, G. T. J. van der Horst, T. Kondo, et al. (2006)
PNAS 103, 10074-10079
   Abstract »    Full Text »    PDF »
MafG Sumoylation Is Required for Active Transcriptional Repression.
H. Motohashi, F. Katsuoka, C. Miyoshi, Y. Uchimura, H. Saitoh, C. Francastel, J. D. Engel, and M. Yamamoto (2006)
Mol. Cell. Biol. 26, 4652-4663
   Abstract »    Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)