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The role of E3 ubiquitin ligase HECTD3 in cancer and beyond

  • Qiuyun Jiang
  • Fubing Li
  • Zhuo Cheng
  • Yanjie Kong
  • Ceshi ChenEmail author
Review
  • 154 Downloads

Abstract

Ubiquitin modification plays significant roles in protein fate determination, signaling transduction, and cellular processes. Over the past 2 decades, the number of studies on ubiquitination has demonstrated explosive growth. E3 ubiquitin ligases are the key enzymes that determine the substrate specificity and are involved in cancer. Several recent studies shed light on the functions and mechanisms of HECTD3 E3 ubiquitin ligase. This review describes the progress in the recent studies of HECTD3 in cancer and other diseases. We propose that HECTD3 is a potential biomarker and a therapeutic target, and discuss the future directions for HECTD3 investigations.

Keywords

Ubiquitination HECTD3 Cancer Inhibitors 

Abbreviations

ACC

Adrenocortical carcinoma

ANGPT1

Angiopoietin 1

BRCA

Breast invasive carcinoma

BRCA1

Breast cancer type 1 susceptibility protein

c-Abl

Abelson murine leukemia viral homolog 1

CHOL

Cholangiocarcinoma

CRAF

RAF proto-oncogene serine/threonine-protein kinase

CRL7

Cullin-RING E3 ubiquitin ligase 7

CUL1

Cullin1

CUL7

Cullin 7

DECL

DNA-encoded compound libraries

DISC

Death-inducing signaling complex

DLBC

Lymphoid neoplasm diffuse large B-cell lymphoma

DUB

Deubiquitinating enzyme

E1

Ubiquitin-activating enzyme

E2

Ubiquitin-conjugating enzyme

E3

Ubiquitin ligase

E6-AP

E6-associated protein

EAE

Experimental autoimmune encephalomyelitis

ECT2

Epithelial cell transforming 2

EGFR

Epidermal growth factor receptor

ER

Endoplasmic reticulum

ERBB4

Erb-b2 receptor tyrosine kinase 4

ERK

Mitogen-activated protein kinase 1

ESCC

Esophageal squamous cell carcinoma

FBDD

Fragment-based drug discovery

FBW7

F-box and WD repeat domain containing 7

FP-HTS

Fluorescence polarization assay for high-throughput screening

HECT

Homologous to E6AP C terminus

HECTD3

Homologous to the E6-associated protein carboxyl terminus domain containing 3

HER2

Erb-b2 receptor tyrosine kinase 2

HIF1α

Hypoxia inducible factor 1 subunit alpha

HSP90

Heat shock protein 90

HTS

High-throughput screening technologies

HUWE1

HECT, UBA, and WWE domain containing E3 ubiquitin protein ligase 1

IFN

Interferon

IRE1α

Inositol requiring enzyme 1 alpha

IRF3

Interferon regulatory factor 3

ITCH

Itchy E3 ubiquitin protein ligase

KLF5

Kruppel like factor 5

LATS1

Large tumor suppressor kinase 1

LIHC

Liver hepatocellular carcinoma

LGG

Brain lower grade glioma

LUAD

Lung adenocarcinoma

MALT1

MALT1 paracaspase

MCL1

Myeloid cell leukemia 1

MDM2

Murine double minute 2

miR-153

MicroRNA-153

NEDD4-1

NEDD4 E3 ubiquitin protein ligase

OV

Ovarian serous cystadenocarcinoma

PMA

Phorbol-12-myristate-13-acetate

PML

Promyelocytic leukemia protein

PTEN

Phosphatase and tensin homolog

RBR

RING-IBR-RINGs

RING

Really interesting new genes

RLD

RCC1 like domain

RNF20

Ring finger protein 20

RORγt

Retineic-acid-receptor-related orphan nuclear receptor γ

SCF

SKP1-CUL1-F-box protein

SKP2

S-phase kinase-associated protein 2

SMAD2

SMAD family member 2

SMURF2

SMAD specific E3 ubiquitin protein ligase 2

Stat3

Signal transducer and activator of transcription 3

Tara

Trio-associated repeat on actin

TBK1

TANK binding kinase 1

TGFβ

Transforming growth factor β

TGFβR1

Transforming growth factor β receptor 1

Th17

T helper 17

THCA

Thyroid carcinoma

THYM

Thymoma

TNBC

Triple negative breast cancer

TRAF3

TNF receptor-associated factor 3

TRAF6

TNF receptor-associated factor 6

TRAIL

TNF-related apoptosis-inducing ligand

Ub

Ubiquitin

UCEC

Uterine Corpus Endometrial Carcinoma

UCS

Uterine Carcinosarcoma

UbV

Ub variant

UCS

Uterine carcinosarcoma

VCB-CR

pVHL-elongin C-elongin B-cullin 2-RBX1

VHL

Von Hippel–Lindau disease tumor suppressor

WWP1

WW domain containing E3 ubiquitin protein ligase 1

WWP2

WW domain containing E3 ubiquitin protein ligase 2

XBP1

X-box binding protein 1

Notes

Acknowledgements

This study was supported in part by grants from the National Key R&D Program of China (2018YFC2000400) and the National Nature Science Foundation of China (81830087, U1602221, and 31771516 to Chen, C and 81773149 to Kong Y) and the Shenzhen Municipal Government of China (KQTD20170810160226082).

Compliance with ethical standards

Conflict of interest

The authors have no conflict of interest.

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Copyright information

© Springer Nature Switzerland AG 2019

Authors and Affiliations

  • Qiuyun Jiang
    • 1
    • 2
  • Fubing Li
    • 3
  • Zhuo Cheng
    • 1
    • 2
  • Yanjie Kong
    • 4
  • Ceshi Chen
    • 1
    • 2
    • 5
    Email author
  1. 1.Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences and Yunnan Province, Kunming Institute of ZoologyChinese Academy of SciencesKunmingChina
  2. 2.Kunming College of Life ScienceUniversity of the Chinese Academy of SciencesKunmingChina
  3. 3.Affiliated Cancer Hospital and Institute of Guangzhou Medical UniversityGuangzhouChina
  4. 4.Institute of Translation Medicine, Shenzhen Second People’s HospitalThe First Affiliated Hospital of Shenzhen UniversityShenzhenChina
  5. 5.KIZ-CUHK Joint Laboratory of Bioresources and Molecular Research in Common Diseases, Kunming Institute of ZoologyChinese Academy of SciencesKunmingChina

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