SPOP promotes ubiquitination and degradation of LATS1 to enhance kidney cancer progression.


Journal

EBioMedicine
ISSN: 2352-3964
Titre abrégé: EBioMedicine
Pays: Netherlands
ID NLM: 101647039

Informations de publication

Date de publication:
Jun 2020
Historique:
received: 14 12 2019
revised: 26 04 2020
accepted: 27 04 2020
pubmed: 28 5 2020
medline: 13 4 2021
entrez: 28 5 2020
Statut: ppublish

Résumé

Emerging evidence has demonstrated that SPOP functions as an oncoprotein in kidney cancer to promote tumorigenesis by ubiquitination-mediated degradation of multiple regulators of cellular proliferation and apoptosis. However, the detailed molecular mechanism underlying the oncogenic role of SPOP in kidney tumorigenesis remains elusive. Multiple approaches such as Co-IP, Transfection, RT-PCR, Western blotting, and animal studies were utilized to explore the role of SPOP in kidney cancer. Here we identified LATS1, a critical component of the Hippo tumour suppressor pathway, as a novel ubiquitin substrate of SPOP. We found that LATS1 interacted with Cullin3, and depletion of Cullin 3 upregulated the abundance of LATS1 largely via prolonging LATS1 protein half-life. Mechanistically, SPOP specifically interacted with LATS1, and promoted the poly-ubiquitination and subsequent degradation of LATS1 in a degron-dependent manner. As such, over-expression of SPOP promoted cell proliferation partly through regulating cell cycle distribution in kidney cancer cells. Furthermore, SPOP also promoted kidney cancer cell invasion via degrading LATS1. Our study provides evidence for a novel mechanism of SPOP in kidney cancer progression in part through promoting degradation of the LATS1 tumour suppressor.

Sections du résumé

BACKGROUND BACKGROUND
Emerging evidence has demonstrated that SPOP functions as an oncoprotein in kidney cancer to promote tumorigenesis by ubiquitination-mediated degradation of multiple regulators of cellular proliferation and apoptosis. However, the detailed molecular mechanism underlying the oncogenic role of SPOP in kidney tumorigenesis remains elusive.
METHODS METHODS
Multiple approaches such as Co-IP, Transfection, RT-PCR, Western blotting, and animal studies were utilized to explore the role of SPOP in kidney cancer.
FINDINGS RESULTS
Here we identified LATS1, a critical component of the Hippo tumour suppressor pathway, as a novel ubiquitin substrate of SPOP. We found that LATS1 interacted with Cullin3, and depletion of Cullin 3 upregulated the abundance of LATS1 largely via prolonging LATS1 protein half-life. Mechanistically, SPOP specifically interacted with LATS1, and promoted the poly-ubiquitination and subsequent degradation of LATS1 in a degron-dependent manner. As such, over-expression of SPOP promoted cell proliferation partly through regulating cell cycle distribution in kidney cancer cells. Furthermore, SPOP also promoted kidney cancer cell invasion via degrading LATS1.
INTERPRETATION CONCLUSIONS
Our study provides evidence for a novel mechanism of SPOP in kidney cancer progression in part through promoting degradation of the LATS1 tumour suppressor.

Identifiants

pubmed: 32460168
pii: S2352-3964(20)30170-5
doi: 10.1016/j.ebiom.2020.102795
pmc: PMC7248661
pii:
doi:

Substances chimiques

CUL3 protein, human 0
Cullin Proteins 0
Nuclear Proteins 0
Repressor Proteins 0
SPOP protein, human 0
LATS1 protein, human EC 2.7.1.-
Protein Serine-Threonine Kinases EC 2.7.11.1

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

102795

Commentaires et corrections

Type : CommentIn

Informations de copyright

Copyright © 2020 The Author(s). Published by Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no conflict of interest.

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Auteurs

Lixia Wang (L)

Department of Obstetrics and Gynecology, The Second Affiliated Hospital of Wenzhou Medical University, Wenzhou, Zhejiang 325027, China; Department of Urology, The Second Affiliated Hospital of Soochow University, Suzhou, Jiangsu 215006, China.

Min Lin (M)

Department of Obstetrics and Gynecology, The Second Affiliated Hospital of Wenzhou Medical University, Wenzhou, Zhejiang 325027, China.

Man Chu (M)

Department of Obstetrics and Gynecology, The Second Affiliated Hospital of Wenzhou Medical University, Wenzhou, Zhejiang 325027, China.

Yi Liu (Y)

Department of Obstetrics and Gynecology, The Second Affiliated Hospital of Wenzhou Medical University, Wenzhou, Zhejiang 325027, China.

Jia Ma (J)

Department of Biochemistry and Molecular Biology, and Research Center of Clinical Laboratory Science, School of Laboratory Medicine, Bengbu Medical College, Anhui 233030, China. Electronic address: majiamj10@126.com.

Youhua He (Y)

Department of Urology, The Second Affiliated Hospital of Wenzhou Medical University, Wenzhou, Zhejiang 325027, China. Electronic address: feymnwk@126.com.

Zhi-Wei Wang (ZW)

Department of Obstetrics and Gynecology, The Second Affiliated Hospital of Wenzhou Medical University, Wenzhou, Zhejiang 325027, China. Electronic address: zwang6@bidmc.harvard.edu.

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Classifications MeSH