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Chronoregulation by Asparagine Deamidation

Weintraub, Steven J. and Deverman, Benjamin E. (2007) Chronoregulation by Asparagine Deamidation. Science Signaling, 2007 (409). re7. ISSN 1937-9145. doi:10.1126/stke.4092007re7.

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Every asparagine in every protein undergoes nonenzymatic deamidation to aspartate or isoaspartate at a rate determined by the surrounding protein structure and cellular environment. Under physiologic conditions, the deamidation half-life of individual asparagines in proteins is proposed to range from less than a day to several centuries. More than 200 proteins have been shown to undergo deamidation to a meaningful degree, and modeling predicts that hundreds more undergo deamidation at rates that have the potential to be of biological consequence. Because deamidation converts an asparagine into an aspartate or isoaspartate, it introduces a negative charge into a protein and results in the isomerization of a residue. Therefore, deamidation has the potential to change protein function. Additionally, deamidation is thought to render some proteins more susceptible to degradation. In most instances in which asparagine deamidation has been identified in vivo, it is involved in pathology. Hence, deamidation has been viewed primarily as a form of protein damage. However, the pervasiveness and evolutionary persistence of these unstable asparagines suggest that they may have a beneficial role. Notably, the change of even a single neighboring amino acid can have a marked effect on the rate of deamidation of an asparagine. Therefore, the underlying rate of deamidation of any asparagine is genetically programmable. This characteristic, combined with the wide range of deamidation rates that can be programmed, imparts to asparagines the potential to serve as molecular timers that regulate protein function and stability.

Item Type:Article
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Deverman, Benjamin E.0000-0002-6223-9303
Additional Information:© 2007 American Association for the Advancement of Science. Published 23 October 2007. S.J.W. was supported by grants from the N.I.H. and the Elsa U. Pardee Foundation.
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Elsa U. Pardee FoundationUNSPECIFIED
Issue or Number:409
Record Number:CaltechAUTHORS:20141112-091601606
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Official Citation:S. J. Weintraub, B. E. Deverman, Chronoregulation by asparagine deamidation. Sci. STKE 2007, re7 (2007)
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:51634
Deposited By: Tony Diaz
Deposited On:12 Nov 2014 21:52
Last Modified:10 Nov 2021 19:13

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