Role of UEV‐1A, a homologue of the tumor suppressor protein TSG101, in protection from DNA damage

Thomson, Timothy M.; Khalid, Hajji; Lozano, Juan José; Sancho, Elena; Ariño, Joaquı́n

doi:10.1016/s0014-5793(98)00060-x

Cited by 17 publications

(18 citation statements)

References 18 publications

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“…This might be of biological relevance taking into consideration the role of ubiquitination in cell cycle regulation (Hershko, 1997). The phenotype of a de®ciency in TSG101A protein results in mitotic abnormalities, such as aberrant spindles and abnormal distribution of chromosomes, suggesting that this gene de®ciency contributes to genome stability (Xie et al, 1998), consistent with the reported phenotype in yeast, where UEV-1A, a yeast homologue of TSG101 that protects from DNA damage (Thomson et al, 1998).…”

Section: Discussionsupporting

confidence: 62%

“…Therefore it is likely that the alteration of TSG101 proteins can have consequences for the proliferation phenotype (Sancho et al, 1988). Also this N-terminus also has homology to a novel transcription factor, CROC-1/UEV-1, which appears to modulate the human FOS gene (Ponting et al, 1997;Rodofsky and Lin, 1997), and to protect from DNA damage (Thomson et al, 1998). This might be of biological relevance taking into consideration the role of ubiquitination in cell cycle regulation (Hershko, 1997).…”

Section: Discussionmentioning

confidence: 99%

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Expression of a new isoform of the tumor susceptibility TSG101 protein lacking a leucine zipper domain in Burkitt lymphoma cell lines

1999

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The tumor susceptibility gene, TSG101, has been identi®ed as a candidate tumor suppressor gene. We have examined the expression of TSG101 in Burkitt lymphoma cell lines. Several aberrant messages were detected in all cell lines. Aberrant splice donor sites are located within exon 1 at positions 132, 154, 172 and 284. Splice acceptors are located at positions 847 and 1054 within exon 5. The aberrant messages are coexpressed with a normal message and could be the result of additional splicing reactions of the mature message that behaves as an intermediate. The normal message codes for 46 kDa protein (TSG101A). One aberrant message joins in frame nucleotides 283 ± 1055 and codes for a protein isoform of 17 kDa (TSG101B), as demonstrated by in vitro translation assays. The TSG101B isoform lacks the leucine zipper near the C-terminus, a transcriptional repressor domain, and retains most of the N-terminal region which has homology to E2 ubiquitin regulatory enzymes and the CROC-1 transcriptional regulator. The TSG101B isoform was detected in sixteen out of twenty-two (72%) BL cell lines, but not in normal lymphoid populations. The presence of two TSG101 isoforms with di erent dimerization potential opens up a new level of regulation of the TSG101 proteins possibly a ecting cell cycle regulation.

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Section: Discussionsupporting

confidence: 62%

Section: Discussionmentioning

confidence: 99%

Expression of a new isoform of the tumor susceptibility TSG101 protein lacking a leucine zipper domain in Burkitt lymphoma cell lines

1999

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“…1998; Thomson et al 1998). However, COP10 is phylogenetically closer to yeast UBC4/UBC5 and Arabidopsis UBC8/UBC9, than to the TSG101 or MMS2 (UEV1) families of UEVs, suggesting that COP10 defines a new group of UEV proteins.…”

Section: Cop10 Encodes An E2 Variant Protein Conserved In Higher Plantsmentioning

confidence: 99%

Arabidopsis COP10 is a ubiquitin-conjugating enzyme variant that acts together with COP1 and the COP9 signalosome in repressing photomorphogenesis

Suzuki

Yanagawa²,

Kwok³

et al. 2002

Genes Dev.

115

129

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A group of evolutionarily conserved pleiotropic COP/ DET/FUS proteins was initially defined by their ability to repress photomorphogenesis in Arabidopsis. It was proposed that this regulation be mediated by targeting degradation of key cellular regulators that promote photomorphogenesis. Among them, COP1 and the COP9 signalosome have been hypothesized to fulfill the roles as an ubiquitin ligase (E3) and an essential E3 modulator. Here we report that COP10 encodes a protein similar to ubiquitin-conjugating enzyme (E2) variant proteins (UEV). COP10 is part of a nuclear protein complex and capable of directly interacting with both COP1 and the COP9 signalosome. Our data indicates that COP10 defines a possible E2 activity, thus validating the working hypothesis that the pleiotropic COP/DET/FUS group of proteins defined a protein ubiquitination pathway.

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“…These proteins are well conserved in sequence and structure in all eukaryotic organisms, and this results in the sharing of specific functions, such as protection of cells from DNA damaging agents ; Thomson et al 1998) and enhancement of transcription from the c-FOS promoter , by UEV proteins from distant organisms. The biochemical mode of action of UEV proteins in the yeast Saccharomyces cerevisiae has been established by Hoffman and Pickart (1999).…”

mentioning

confidence: 99%

Fusion of the Human Gene for the Polyubiquitination Coeffector UEV1 with Kua, a Newly Identified Gene

Thomson

Lozano²,

Loukili³

et al. 2000

Genome Research

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UEV proteins are enzymatically inactive variants of the E2 ubiquitin-conjugating enzymes that regulate noncanonical elongation of ubiquitin chains. In Saccharomyces cerevisiae, UEV is part of the RAD6-mediated error-free DNA repair pathway. In mammalian cells, UEV proteins can modulate c-FOS transcription and the G2-M transition of the cell cycle. Here we show that the UEV genes from phylogenetically distant organisms present a remarkable conservation in their exon-intron structure. We also show that the human UEV1 gene is fused with the previously unknown gene Kua. In Caenorhabditis elegans and Drosophila melanogaster, Kua and UEV are in separated loci, and are expressed as independent transcripts and proteins. In humans, Kua and UEV1 are adjacent genes, expressed either as separate transcripts encoding independent Kua and UEV1 proteins, or as a hybrid Kua-UEV transcript, encoding a two-domain protein. Kua proteins represent a novel class of conserved proteins with juxtamembrane histidine-rich motifs. Experiments with epitope-tagged proteins show that UEV1A is a nuclear protein, whereas both Kua and Kua-UEV localize to cytoplasmic structures, indicating that the Kua domain determines the cytoplasmic localization of Kua-UEV. Therefore, the addition of a Kua domain to UEV in the fused Kua-UEV protein confers new biological properties to this regulator of variant polyubiquitination.

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Role of UEV‐1A, a homologue of the tumor suppressor protein TSG101, in protection from DNA damage

Cited by 17 publications

References 18 publications

Expression of a new isoform of the tumor susceptibility TSG101 protein lacking a leucine zipper domain in Burkitt lymphoma cell lines

Expression of a new isoform of the tumor susceptibility TSG101 protein lacking a leucine zipper domain in Burkitt lymphoma cell lines

Arabidopsis COP10 is a ubiquitin-conjugating enzyme variant that acts together with COP1 and the COP9 signalosome in repressing photomorphogenesis

Fusion of the Human Gene for the Polyubiquitination Coeffector UEV1 with Kua, a Newly Identified Gene

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