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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Public Library of Science (PLoS)
2021-01-01
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Series: | PLoS ONE |
Online Access: | https://doi.org/10.1371/journal.pone.0256282 |
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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 |
collection | DOAJ |
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. |
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institution | Directory Open Access Journal |
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language | English |
last_indexed | 2024-12-21T23:18:38Z |
publishDate | 2021-01-01 |
publisher | Public Library of Science (PLoS) |
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spelling | doaj.art-a400f67bda40476188a07de2769a25752022-12-21T18:46:51ZengPublic Library of Science (PLoS)PLoS ONE1932-62032021-01-01168e025628210.1371/journal.pone.0256282Phosphorylation of PUF-A/PUM3 on Y259 modulates PUF-A stability and cell proliferation.Hung-Wei LinJin-Yu LeeNai-Lin ChouTing-Wei ShihMau-Sun ChangHuman 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.https://doi.org/10.1371/journal.pone.0256282 |
spellingShingle | 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. PLoS ONE |
title | 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_short | 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 |
url | https://doi.org/10.1371/journal.pone.0256282 |
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