4.7 Review

Recent Advances in Genetic Code Expansion Techniques for Protein Phosphorylation Studies

Journal

JOURNAL OF MOLECULAR BIOLOGY
Volume 434, Issue 8, Pages -

Publisher

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2021.167406

Keywords

post-translational phosphorylation; aminoacyl-tRNA synthetase; noncanonical amino acids; kinase; phosphatase

Funding

  1. National Natural Science Foundation of China [21778005, 21922701, 91853111]
  2. Beijing Natural Science Foundation [JQ20034]

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Protein phosphorylation is a crucial posttranslational modification involved in cell signaling. The use of genetic code expansion has advanced the study of protein phosphorylation.
Protein phosphorylation is a reversible, residue-specific posttranslational modification that plays a pivotal role in cell signaling, and the phosphorylation state of proteins is tightly regulated by kinases and phosphatases. Malfunction of this regulation is often associated with human diseases, and therefore elucidation of the function and regulation of this posttranslational modification is important. Genetic code expansion, which allows for site-specific introduction of noncanonical amino acids directly into target pro-teins in response to a non-sense codon is a powerful method for preparing homogeneously phosphorylated proteins both in Escherichia coli and mammalian cells and therefore is useful for studying protein phosphorylation. Herein, we summarize recent developments in the application of genetic code expansion for protein phosphorylation studies. (C) 2021 Elsevier Ltd. All rights reserved.

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