Ubiquitin and ubiquitin-like proteins in cancer pathogenesis

Hoeller, Daniela; Hecker, Christina; Đikić, Ivan

doi:10.1038/nrc1994

Cited by 360 publications

(312 citation statements)

References 133 publications

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“…As the SUMO field has evolved, several diseases, including cancers, have been linked to perturbations in the SUMO system and/or disruption of sumoylation by mutations in substrate proteins (Hoeller et al, 2006). Using hematopoietic transformation assays (Pattabiraman et al, 2009), we examined the transforming abilities of the SUMO interaction mutants.…”

Section: Discussionmentioning

confidence: 99%

A functional SUMO-interacting motif in the transactivation domain of c-Myb regulates its myeloid transforming ability

et al. 2010

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Section: Discussionmentioning

confidence: 99%

A functional SUMO-interacting motif in the transactivation domain of c-Myb regulates its myeloid transforming ability

et al. 2010

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“…Deregulation of ubiquitin and Ubl pathways leads to the development of diseases including cancers [24]. For example, covalent modification of tumor suppressor p53 by ubiquitin, SUMO-1, or NEDD8 regulates its degradation, nuclear export or transcriptional activity [25,24].…”

Section: Discussionmentioning

confidence: 99%

Deficiency of a potential 3p21.3 tumor suppressor gene UBE1L (UBA7) does not accelerate lung cancer development in K-rasLA2 mice

et al. 2009

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SummaryGenetic lesions in chromosomal region 3p21.3 marks one of the earliest events in human lung cancer development. It is hypothesized that one or more tumor suppressor genes reside in this region. Identification and characterization of these genes are important for the understanding of lung cancer initiation. UBE1L (UBA7) is a long-suspected 3p21.3 residing tumor suppressor gene. It encodes the key enzyme that activates ISGylation, a novel, ubiquitination-like, post-translational protein modification system that is inducible by interferon. It has been implicated that ISGylation plays a variety of biological roles ranging from viral defense to tumor surveillance. Here we tested the possible function of ISGylation during lung cancer development by using the Ube1l-deficient mice and the K-ras LA2 lung cancer mice. Protein ISGylation levels were largely unchanged during lung cancer progression. Ube1l deficiency neither altered the lung cancer progression nor affected the overall survival of K-ras LA2 lung cancer mice. Our study suggests that Ube1l is not a tumor suppressor gene in K-ras LA2 lung cancer mouse model. However, as described in the discussion, additional studies with other lung cancer mouse models will be necessary to elucidate the potential tumor suppressor function of UBE1L in K-RAS mutation independent human lung cancers.

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“…Coordinates are from Dueber and colleagues (Dueber et al 2011), PDB: 3T6P, and Mace and colleagues (Mace et al 2008) (Komander and Rape 2012). Whether ubiquitylation targets proteins for degradation or mediates nondegradative signaling depends on protein interactions between the ubiquitylated protein and Ub-binding proteins, which can therefore be considered as Ub "receptors" (Hoeller et al 2006). Ub receptors carry specialized Ub-binding domains (UBDs) that enable them to interact with the specific linkage types and assemble Ub-dependent signaling hubs.…”

Section: Ring Fingermentioning

confidence: 99%