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.


Sci. STKE, 23 October 2007
Vol. 2007, Issue 409, p. re7
[DOI: 10.1126/stke.4092007re7]


Chronoregulation by Asparagine Deamidation

Steven J. Weintraub1* and Benjamin E. Deverman2

1Division of Urology, Department of Cell Biology and Physiology, The Siteman Cancer Center, Washington University School of Medicine, 660 South Euclid Avenue, Campus Box 8242, St. Louis, MO 63110, USA.
2Division of Biology, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.

Gloss: The deamidation of an asparagine is a common posttranslational modification. When an asparagine in a protein undergoes deamidation, its amide side chain is nonenzymatically hydrolyzed, which results in the replacement of the asparagine residue with either an aspartate or an isoaspartate. By introducing a negative charge and isomerization into a protein in this manner, the deamidation of an asparagine has the potential to alter protein function. Asparagine deamidation is widely thought to be an unregulated process that is nothing more than a form of protein damage. However, it has been demonstrated that the inherent deamidation rate of an asparagine is actually tightly regulated by its surrounding sequence and that a wide range of deamidation rates can be genetically programmed into a protein simply by altering the amino acids in the sequence surrounding an asparagine. Because of this property, it was proposed 40 years ago that asparagine deamidation could serve as molecular timer that is genetically programmed to time biological processes. This STKE review, with 4 figures and 49 references, discusses the evidence in support of the molecular timer hypothesis.

*Corresponding author. E-mail: weintraub{at}

Citation: S. J. Weintraub, B. E. Deverman, Chronoregulation by Asparagine Deamidation. Sci. STKE 2007, re7 (2007).

Oxidation-induced Structural Changes of Ceruloplasmin Foster NGR Motif Deamidation That Promotes Integrin Binding and Signaling.
M. Barbariga, F. Curnis, A. Spitaleri, A. Andolfo, C. Zucchelli, M. Lazzaro, G. Magnani, G. Musco, A. Corti, and M. Alessio (2014)
J. Biol. Chem. 289, 3736-3748
   Abstract »    Full Text »    PDF »
Isoaspartate-dependent molecular switches for integrin-ligand recognition.
A. Corti and F. Curnis (2011)
J. Cell Sci. 124, 515-522
   Abstract »    Full Text »    PDF »
Repair of Isoaspartate Formation Modulates the Interaction of Deamidated 4E-BP2 with mTORC1 in Brain.
M. Bidinosti, Y. Martineau, F. Frank, and N. Sonenberg (2010)
J. Biol. Chem. 285, 19402-19408
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882