Posttranslational Modifications of Smurfs: Emerging Regulation in Cancer

Smad ubiquitination regulatory factors (Smurfs) belong to the Nedd4 subfamily of HECT-type E3 ubiquitin ligases. Under normal situations, Smurfs are exactly managed by upstream regulators, and thereby strictly control tumor biological processes, including cell growth, differentiation, apoptosis, pol...

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Main Authors: Longtao Yang, Wenwen Zhou, Hui Lin
Format: Article
Language:English
Published: Frontiers Media S.A. 2021-02-01
Series:Frontiers in Oncology
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fonc.2020.610663/full
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spelling doaj-20a585cbd3b444049bd477d3d6958e5f2021-02-25T16:06:21ZengFrontiers Media S.A.Frontiers in Oncology2234-943X2021-02-011010.3389/fonc.2020.610663610663Posttranslational Modifications of Smurfs: Emerging Regulation in CancerLongtao Yang0Wenwen Zhou1Hui Lin2Second Clinical Medical School, Nanchang University, Nanchang, ChinaSecond Clinical Medical School, Nanchang University, Nanchang, ChinaDepartment of Pathophysiology, School of Basic Medical Sciences, Nanchang University, Nanchang, ChinaSmad ubiquitination regulatory factors (Smurfs) belong to the Nedd4 subfamily of HECT-type E3 ubiquitin ligases. Under normal situations, Smurfs are exactly managed by upstream regulators, and thereby strictly control tumor biological processes, including cell growth, differentiation, apoptosis, polarization, epithelial mesenchymal transition (EMT), and invasion. Disruption of Smurf activity has been implicated in cancer progression, and Smurf activity is controlled by a series of posttranslational modifications (PTMs), including phosphorylation, ubiquitination, neddylation, sumoylation, and methylation. The effect and function of Smurfs depend on PTMs and regulate biological processes. Specifically, these modifications regulate the functional expression of Smurfs by affecting protein degradation and protein interactions. In this review, we summarize the complexity and diversity of Smurf PTMs from biochemical and biological perspectives and highlight the understanding of their roles in cancer.https://www.frontiersin.org/articles/10.3389/fonc.2020.610663/fullSmurfsposttranslational modification (PTM)cancerphosphorylationubiquitination
collection DOAJ
language English
format Article
sources DOAJ
author Longtao Yang
Wenwen Zhou
Hui Lin
spellingShingle Longtao Yang
Wenwen Zhou
Hui Lin
Posttranslational Modifications of Smurfs: Emerging Regulation in Cancer
Frontiers in Oncology
Smurfs
posttranslational modification (PTM)
cancer
phosphorylation
ubiquitination
author_facet Longtao Yang
Wenwen Zhou
Hui Lin
author_sort Longtao Yang
title Posttranslational Modifications of Smurfs: Emerging Regulation in Cancer
title_short Posttranslational Modifications of Smurfs: Emerging Regulation in Cancer
title_full Posttranslational Modifications of Smurfs: Emerging Regulation in Cancer
title_fullStr Posttranslational Modifications of Smurfs: Emerging Regulation in Cancer
title_full_unstemmed Posttranslational Modifications of Smurfs: Emerging Regulation in Cancer
title_sort posttranslational modifications of smurfs: emerging regulation in cancer
publisher Frontiers Media S.A.
series Frontiers in Oncology
issn 2234-943X
publishDate 2021-02-01
description Smad ubiquitination regulatory factors (Smurfs) belong to the Nedd4 subfamily of HECT-type E3 ubiquitin ligases. Under normal situations, Smurfs are exactly managed by upstream regulators, and thereby strictly control tumor biological processes, including cell growth, differentiation, apoptosis, polarization, epithelial mesenchymal transition (EMT), and invasion. Disruption of Smurf activity has been implicated in cancer progression, and Smurf activity is controlled by a series of posttranslational modifications (PTMs), including phosphorylation, ubiquitination, neddylation, sumoylation, and methylation. The effect and function of Smurfs depend on PTMs and regulate biological processes. Specifically, these modifications regulate the functional expression of Smurfs by affecting protein degradation and protein interactions. In this review, we summarize the complexity and diversity of Smurf PTMs from biochemical and biological perspectives and highlight the understanding of their roles in cancer.
topic Smurfs
posttranslational modification (PTM)
cancer
phosphorylation
ubiquitination
url https://www.frontiersin.org/articles/10.3389/fonc.2020.610663/full
work_keys_str_mv AT longtaoyang posttranslationalmodificationsofsmurfsemergingregulationincancer
AT wenwenzhou posttranslationalmodificationsofsmurfsemergingregulationincancer
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