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Cullin Family Proteins and Tumorigenesis: Genetic Association and Molecular Mechanisms
Cullin family proteins function as scaffolds to form numerous E3 ubiquitin ligases with RING proteins, adaptor proteins and substrate recognition receptors. These E3 ligases further recognize numerous substrates to participate in a variety of cellular processes, such as DNA damage and repair, cell d...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Ivyspring International Publisher
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4317758/ https://www.ncbi.nlm.nih.gov/pubmed/25663940 http://dx.doi.org/10.7150/jca.11076 |
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author | Chen, Zhi Sui, Jie Zhang, Fan Zhang, Caiguo |
author_facet | Chen, Zhi Sui, Jie Zhang, Fan Zhang, Caiguo |
author_sort | Chen, Zhi |
collection | PubMed |
description | Cullin family proteins function as scaffolds to form numerous E3 ubiquitin ligases with RING proteins, adaptor proteins and substrate recognition receptors. These E3 ligases further recognize numerous substrates to participate in a variety of cellular processes, such as DNA damage and repair, cell death and cell cycle progression. Clinically, cullin-associated E3 ligases have been identified to involve numerous human diseases, especially with regard to multiple cancer types. Over the past few years, our understanding of cullin proteins and their functions in genome stability and tumorigenesis has expanded enormously. Herein, this review briefly provides current perspectives on cullin protein functions, and mainly summarizes and discusses molecular mechanisms of cullin proteins in tumorigenesis. |
format | Online Article Text |
id | pubmed-4317758 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Ivyspring International Publisher |
record_format | MEDLINE/PubMed |
spelling | pubmed-43177582015-02-06 Cullin Family Proteins and Tumorigenesis: Genetic Association and Molecular Mechanisms Chen, Zhi Sui, Jie Zhang, Fan Zhang, Caiguo J Cancer Review Cullin family proteins function as scaffolds to form numerous E3 ubiquitin ligases with RING proteins, adaptor proteins and substrate recognition receptors. These E3 ligases further recognize numerous substrates to participate in a variety of cellular processes, such as DNA damage and repair, cell death and cell cycle progression. Clinically, cullin-associated E3 ligases have been identified to involve numerous human diseases, especially with regard to multiple cancer types. Over the past few years, our understanding of cullin proteins and their functions in genome stability and tumorigenesis has expanded enormously. Herein, this review briefly provides current perspectives on cullin protein functions, and mainly summarizes and discusses molecular mechanisms of cullin proteins in tumorigenesis. Ivyspring International Publisher 2015-01-16 /pmc/articles/PMC4317758/ /pubmed/25663940 http://dx.doi.org/10.7150/jca.11076 Text en © 2015 Ivyspring International Publisher. Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited. See http://ivyspring.com/terms for terms and conditions. |
spellingShingle | Review Chen, Zhi Sui, Jie Zhang, Fan Zhang, Caiguo Cullin Family Proteins and Tumorigenesis: Genetic Association and Molecular Mechanisms |
title | Cullin Family Proteins and Tumorigenesis: Genetic Association and Molecular Mechanisms |
title_full | Cullin Family Proteins and Tumorigenesis: Genetic Association and Molecular Mechanisms |
title_fullStr | Cullin Family Proteins and Tumorigenesis: Genetic Association and Molecular Mechanisms |
title_full_unstemmed | Cullin Family Proteins and Tumorigenesis: Genetic Association and Molecular Mechanisms |
title_short | Cullin Family Proteins and Tumorigenesis: Genetic Association and Molecular Mechanisms |
title_sort | cullin family proteins and tumorigenesis: genetic association and molecular mechanisms |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4317758/ https://www.ncbi.nlm.nih.gov/pubmed/25663940 http://dx.doi.org/10.7150/jca.11076 |
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