Editors' ChoiceCell Biology

Making Modifications

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Science Signaling  21 Sep 2010:
Vol. 3, Issue 140, pp. ec290
DOI: 10.1126/scisignal.3140ec290

Arginylation of β-actin regulates cell motility and the actin cytoskeleton, but how differential arginylation of the two highly similar actin isoforms—β and γ—is achieved in vivo is unclear. Zhang et al. (see the Perspective by Weygand-Durasevic and Ibba) describe a cotranslational mechanism that selectively regulates the arginylation of proteins through degradation and is dependent on the nucleotide coding sequence coupled to the translation speed. The work provides an explanation for the different N-terminal arginylation states of β- and γ-actin in vivo and suggests that translation rate affected by nucleotide coding sequence confers different posttranslational states to proteins and selectively regulates protein degradation.

F. Zhang, S. Saha, S. A. Shabalina, A. Kashina, Differential arginylation of actin isoforms is regulated by coding sequence–dependent degradation. Science 329, 1534–1537 (2010). [Abstract] [Full Text]

I. Weygand-Durasevic, M. Ibba, New roles for codon usage. Science 329, 1473–1474 (2010). [Summary] [Full Text]

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