Publication Date:
2022-05-25
Description:
© The Author(s), 2017. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Molecular Biology of the Cell 28 (2017): 1208-1222, doi:10.1091/mbc.E16-11-0774.
Description:
Changes in protein by posttranslational modifications comprise an important mechanism for the control of many cellular processes. Several flagellar proteins are methylated on arginine residues during flagellar resorption; however, the function is not understood. To learn more about the role of protein methylation during flagellar dynamics, we focused on protein arginine methyltransferases (PRMTs) 1, 3, 5, and 10. These PRMTs localize to the tip of flagella and in a punctate pattern along the length, very similar, but not identical, to that of intraflagellar transport (IFT) components. In addition, we found that PRMT 1 and 3 are also highly enriched at the base of the flagella, and the basal localization of these PRMTs changes during flagellar regeneration and resorption. Proteins with methyl arginine residues are also enriched at the tip and base of flagella, and their localization also changes during flagellar assembly and disassembly. PRMTs are lost from the flagella of fla10-1 cells, which carry a temperature-sensitive mutation in the anterograde motor for IFT. The data define the distribution of specific PRMTs and their target proteins in flagella and demonstrate that PRMTs are cargo for translocation within flagella by the process of IFT.
Description:
This work was supported by National Science Foundation Award MCB 0950402 (R.D.S.), the Ira Allen Eastman (Class of 1829) Professorship at Dartmouth (R.D.S.), which was established in 1910 through a gift to the College by his widow, Jane Eastman, and by a Postdoctoral Fellowship for Research Abroad from the Japan Society for the Promotion of Science (K.M.).
Repository Name:
Woods Hole Open Access Server
Type:
Article
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