PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of Stathmin1

Oncotarget
Chao LiYongxin Ma

Abstract

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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Citations

Dec 26, 2018·Cancers·Ryte RynkevicieneKestutis Suziedelis
Jan 2, 2019·World Journal of Gastroenterology : WJG·Taíssa AraújoPaulo Assumpção
Feb 23, 2019·Cell Communication and Signaling : CCS·Jaime Santo-DomingoAndreas Wiederkehr
Mar 16, 2021·Frontiers in Cell and Developmental Biology·Peixin DongHidemichi Watari

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Methods Mentioned

BETA
two-hybrid
PCR
co-immuoprecipitation
ubiquitination
transfection
immuoprecipitation
confocal microscopy
coimmunoprecipitation
immunoprecipitation assay
Co-immunoprecipitation

Software Mentioned

SPSS

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