Phosphorylation of PUF-A/PUM3 on Y259 modulates PUF-A stability and cell proliferation.
Human PUF-A/PUM3 is a RNA and DNA binding protein participating in the nucleolar processing of 7S to 5.8S rRNA. The nucleolar localization of PUF-A redistributes to the nucleoplasm upon the exposure to genotoxic agents in cells. However, little is known regarding the roles of PUF-A in tumor progress...
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oai:doaj.org-article:a400f67bda40476188a07de2769a25752021-12-02T20:17:49ZPhosphorylation of PUF-A/PUM3 on Y259 modulates PUF-A stability and cell proliferation.1932-620310.1371/journal.pone.0256282https://doaj.org/article/a400f67bda40476188a07de2769a25752021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0256282https://doaj.org/toc/1932-6203Human PUF-A/PUM3 is a RNA and DNA binding protein participating in the nucleolar processing of 7S to 5.8S rRNA. The nucleolar localization of PUF-A redistributes to the nucleoplasm upon the exposure to genotoxic agents in cells. However, little is known regarding the roles of PUF-A in tumor progression. Phosphoprotein database analysis revealed that Y259 phosphorylation of PUF-A is the most prevalent residue modified. Here, we reported the importance of PUF-A's phosphorylation on Y259 in tumorigenesis. PUF-A gene was knocked out by the Crispr/Cas9 method in human cervix epithelial HeLa cells. Loss of PUF-A in HeLa cells resulted in reduced clonogenic and lower transwell invasion capacity. Introduction of PUF-AY259F to PUF-A deficient HeLa cells was unable to restore colony formation. In addition, the unphosphorylated mutant of PUF-A, PUF-AY259F, attenuated PUF-A protein stability. Our results suggest the important role of Y259 phosphorylation of PUF-A in cell proliferation.Hung-Wei LinJin-Yu LeeNai-Lin ChouTing-Wei ShihMau-Sun ChangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 8, p e0256282 (2021) |
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Medicine R Science Q Hung-Wei Lin Jin-Yu Lee Nai-Lin Chou Ting-Wei Shih Mau-Sun Chang Phosphorylation of PUF-A/PUM3 on Y259 modulates PUF-A stability and cell proliferation. |
description |
Human PUF-A/PUM3 is a RNA and DNA binding protein participating in the nucleolar processing of 7S to 5.8S rRNA. The nucleolar localization of PUF-A redistributes to the nucleoplasm upon the exposure to genotoxic agents in cells. However, little is known regarding the roles of PUF-A in tumor progression. Phosphoprotein database analysis revealed that Y259 phosphorylation of PUF-A is the most prevalent residue modified. Here, we reported the importance of PUF-A's phosphorylation on Y259 in tumorigenesis. PUF-A gene was knocked out by the Crispr/Cas9 method in human cervix epithelial HeLa cells. Loss of PUF-A in HeLa cells resulted in reduced clonogenic and lower transwell invasion capacity. Introduction of PUF-AY259F to PUF-A deficient HeLa cells was unable to restore colony formation. In addition, the unphosphorylated mutant of PUF-A, PUF-AY259F, attenuated PUF-A protein stability. Our results suggest the important role of Y259 phosphorylation of PUF-A in cell proliferation. |
format |
article |
author |
Hung-Wei Lin Jin-Yu Lee Nai-Lin Chou Ting-Wei Shih Mau-Sun Chang |
author_facet |
Hung-Wei Lin Jin-Yu Lee Nai-Lin Chou Ting-Wei Shih Mau-Sun Chang |
author_sort |
Hung-Wei Lin |
title |
Phosphorylation of PUF-A/PUM3 on Y259 modulates PUF-A stability and cell proliferation. |
title_short |
Phosphorylation of PUF-A/PUM3 on Y259 modulates PUF-A stability and cell proliferation. |
title_full |
Phosphorylation of PUF-A/PUM3 on Y259 modulates PUF-A stability and cell proliferation. |
title_fullStr |
Phosphorylation of PUF-A/PUM3 on Y259 modulates PUF-A stability and cell proliferation. |
title_full_unstemmed |
Phosphorylation of PUF-A/PUM3 on Y259 modulates PUF-A stability and cell proliferation. |
title_sort |
phosphorylation of puf-a/pum3 on y259 modulates puf-a stability and cell proliferation. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2021 |
url |
https://doaj.org/article/a400f67bda40476188a07de2769a2575 |
work_keys_str_mv |
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