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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Main Authors: Hung-Wei Lin, Jin-Yu Lee, Nai-Lin Chou, Ting-Wei Shih, Mau-Sun Chang
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2021-01-01
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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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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