What is it about?
The most abundant protein in the human body, actin, is acetylated at the beginning of its sequence (so called N terminus) by the newly identified enzyme NAA80. In cells actin N-terminal acetylation is nearly 100% and when cells are lacking this modification, it leads to alteration of the whole cytoskeleton. This affects actin's ability and speed to polymerize into filaments as well as the regulation of cell motility. In fact, cells are moving faster when NAA80 is not expressed in the cells and actin is missing the N-terminal acetylation. Thus, N-terminal acetylation seems to function as a break for controlled cell motility.
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Why is it important?
Actin controls numerous functions in the cell, such as muscle contraction, cell integrity, cell motility and gene regulation. Thereby, actin itself is regulated by interaction with dozens of actin binding proteins and post-translational modifications such as N-terminal acetylation. The global effects on the cytoskeleton and the cell when NAA80, and thus N-terminal acetylation, is missing, indicates that this is an important regulator to control cell movement and potential other functions.
Perspectives
Identifying this new enzyme targeting such an important protein such as actin, opened dozens of new possibilities for future studies. It was also great pleasure to combine actin biochemistry with cell biology.
Adrian Drazic
Universitetet i Bergen
Read the Original
This page is a summary of: Actin polymerization and cell motility are affected by NAA80-mediated posttranslational N-terminal acetylation of actin, Communicative & Integrative Biology, September 2018, Taylor & Francis,
DOI: 10.1080/19420889.2018.1526572.
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