Emerging roles of the HECT-type E3 ubiquitin ligases in hematological malignancies

被引：0
作者：
Vincenza Simona Delvecchio
Claudia Fierro
Sara Giovannini
Gerry Melino
Francesca Bernassola
机构：
[1] TOR,Department of Experimental Medicine
[2] University of Rome “Tor Vergata”,undefined
来源：
Discover Oncology | / 12卷
关键词：
Leukemia; Ubiquitin; Ubiquitination; HECT-type E3 ubiquitin protein ligases; Proteasomal degradation;
D O I：
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摘要：
Ubiquitination-mediated proteolysis or regulation of proteins, ultimately executed by E3 ubiquitin ligases, control a wide array of cellular processes, including transcription, cell cycle, autophagy and apoptotic cell death. HECT-type E3 ubiquitin ligases can be distinguished from other subfamilies of E3 ubiquitin ligases because they have a C-terminal HECT domain that directly catalyzes the covalent attachment of ubiquitin to their substrate proteins. Deregulation of HECT-type E3-mediated ubiquitination plays a prominent role in cancer development and chemoresistance. Several members of this subfamily are indeed frequently deregulated in human cancers as a result of genetic mutations and altered expression or activity. HECT-type E3s contribute to tumorigenesis by regulating the ubiquitination rate of substrates that function as either tumour suppressors or oncogenes. While the pathological roles of the HECT family members in solid tumors are quite well established, their contribution to the pathogenesis of hematological malignancies has only recently emerged. This review aims to provide a comprehensive overview of the involvement of the HECT-type E3s in leukemogenesis.
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  • [21] Youle RJ(2020)Excess of the NF-κB p50 subunit generated by the ubiquitin ligase KPC1 suppresses tumors via PD-L1-and chemokines-mediated mechanisms Proc Natl Acad Sci U S A 117 29823-29831
  • [22] Weinelt N(2020)Site-specific ubiquitination of pathogenic huntingtin attenuates its deleterious effects Proc Natl Acad Sci U S A 117 18661-18669
  • [23] van Wijk SJL(2020)Autophagy in cancer: moving from understanding mechanism to improving therapy responses in patients Cell Death Differ 27 843-857
  • [24] Damgaard RB(2020)ER-phagy and human diseases Cell Death Differ 27 833-842
  • [25] Jolin HE(2020)Competitive ubiquitination activates the tumor suppressor p53 Cell Death Differ 27 1807-1818
  • [26] Allison MED(2019)A DHX9-lncRNA-MDM2 interaction regulates cell invasion and angiogenesis of cervical cancer Cell Death Differ 26 1750-1765
  • [27] Davies SE(2020)Autophagy and disease: unanswered questions Cell Death Differ 27 858-871
  • [28] Titheradge HL(2020)Autophagy and microbial pathogenesis Cell Death Differ 27 872-886
  • [29] McKenzie ANJ(2020)Autophagy in animal development Cell Death Differ 27 903-918
  • [30] Komander D(2021)Functions of outer mitochondrial membrane proteins: mediating the crosstalk between mitochondrial dynamics and mitophagy Cell Death Differ 28 827-842
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