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PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of stathmin1

Human PIWIL1, alias HIWI, is a member of Piwi protein family and expressed in various tumors. However, the underlying mechanism of PIWIL1 in tumorigenesis remains largely unknown. Stathmin1 is a cytosolic phosphoprotein which has a critical role in regulating microtubule dynamics and is overexpresse...

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Autores principales: Li, Chao, Zhou, Xiaoyan, Chen, Jianhui, Lu, Yilu, Sun, Qianqian, Tao, Dachang, Hu, Wei, Zheng, Xulei, Bian, Shasha, Liu, Yunqiang, Ma, Yongxin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals LLC 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4695026/
https://www.ncbi.nlm.nih.gov/pubmed/26317901
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author Li, Chao
Zhou, Xiaoyan
Chen, Jianhui
Lu, Yilu
Sun, Qianqian
Tao, Dachang
Hu, Wei
Zheng, Xulei
Bian, Shasha
Liu, Yunqiang
Ma, Yongxin
author_facet Li, Chao
Zhou, Xiaoyan
Chen, Jianhui
Lu, Yilu
Sun, Qianqian
Tao, Dachang
Hu, Wei
Zheng, Xulei
Bian, Shasha
Liu, Yunqiang
Ma, Yongxin
author_sort Li, Chao
collection PubMed
description Human PIWIL1, alias HIWI, is a member of Piwi protein family and expressed in various tumors. However, the underlying mechanism of PIWIL1 in tumorigenesis remains largely unknown. Stathmin1 is a cytosolic phosphoprotein which has a critical role in regulating microtubule dynamics and is overexpressed in many cancers. Here we report that PIWIL1 can directly bind to Stathmin1. Meanwhile, PIWIL1 can up-regulate the expression of Stathmin1 through inhibiting ubiquitin-mediated degradation induced by an E3 ubiquitin ligase RLIM. Furthermore, PIWIL1 can also reduce phosphorylation level of Stathmin1 at Ser-16 through inhibiting the interaction between CaMKII and Stathmin1. Our results showed that PIWIL1 suppresses microtubule polymerization, and promotes cell proliferation and migration via Stathmin1 for the first time. Our study reveals a novel mechanism for PIWIL1 in tumorigenesis.
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spelling pubmed-46950262016-01-20 PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of stathmin1 Li, Chao Zhou, Xiaoyan Chen, Jianhui Lu, Yilu Sun, Qianqian Tao, Dachang Hu, Wei Zheng, Xulei Bian, Shasha Liu, Yunqiang Ma, Yongxin Oncotarget Research Paper Human PIWIL1, alias HIWI, is a member of Piwi protein family and expressed in various tumors. However, the underlying mechanism of PIWIL1 in tumorigenesis remains largely unknown. Stathmin1 is a cytosolic phosphoprotein which has a critical role in regulating microtubule dynamics and is overexpressed in many cancers. Here we report that PIWIL1 can directly bind to Stathmin1. Meanwhile, PIWIL1 can up-regulate the expression of Stathmin1 through inhibiting ubiquitin-mediated degradation induced by an E3 ubiquitin ligase RLIM. Furthermore, PIWIL1 can also reduce phosphorylation level of Stathmin1 at Ser-16 through inhibiting the interaction between CaMKII and Stathmin1. Our results showed that PIWIL1 suppresses microtubule polymerization, and promotes cell proliferation and migration via Stathmin1 for the first time. Our study reveals a novel mechanism for PIWIL1 in tumorigenesis. Impact Journals LLC 2015-07-15 /pmc/articles/PMC4695026/ /pubmed/26317901 Text en Copyright: © 2015 Li et al. http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Paper
Li, Chao
Zhou, Xiaoyan
Chen, Jianhui
Lu, Yilu
Sun, Qianqian
Tao, Dachang
Hu, Wei
Zheng, Xulei
Bian, Shasha
Liu, Yunqiang
Ma, Yongxin
PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of stathmin1
title PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of stathmin1
title_full PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of stathmin1
title_fullStr PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of stathmin1
title_full_unstemmed PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of stathmin1
title_short PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of stathmin1
title_sort piwil1 destabilizes microtubule by suppressing phosphorylation at ser16 and rlim-mediated degradation of stathmin1
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4695026/
https://www.ncbi.nlm.nih.gov/pubmed/26317901
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