TRAF-interacting protein (TRIP) is a RING-dependent ubiquitin ligase

Besse, Arnaud; Campos, Alejandro D.; Webster, William K.; Darnay, Bryant G.

doi:10.1016/j.bbrc.2007.05.149

Cited by 33 publications

(57 citation statements)

References 16 publications

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“…TRA IP localizes to genotoxic stress sites via a PCNA-binding PIP box TRA IP is an active E3 ubiquitin ligase by virtue of an N-terminal RING domain (Besse et al, 2007) and also contains coiledcoil motifs in its middle portion (Fig. 2 A).…”

Section: Tra Ip Associates With Active and Stalled Replication Forksmentioning

confidence: 99%

TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress

Hoffmann¹,

Smedegaard²,

Nakamura³

et al. 2016

J Exp Med

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Section: Tra Ip Associates With Active and Stalled Replication Forksmentioning

confidence: 99%

TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress

Hoffmann¹,

Smedegaard²,

Nakamura³

et al. 2016

J Exp Med

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“…The putative mammalian homolog of NOPO was named 'TRAF-interacting protein' (TRIP) based on its ability to bind tumor necrosis factor (TNF) receptor-associated factors (TRAFs) (Lee et al, 1997). Mammalian TRIP was recently demonstrated to have RINGdependent E3 ubiquitin ligase activity in an auto-ubiquitination assay (Besse et al, 2007). Drosophila NOPO and human TRIP are 20% identical and 34% similar overall, with 47% identity and 65% similarity in their RING domains.…”

Section: Z1447mentioning

confidence: 99%

no polesencodes a predicted E3 ubiquitin ligase required for early embryonic development ofDrosophila

et al. 2009

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In a screen for cell-cycle regulators, we identified a Drosophilamaternal effect-lethal mutant that we named `no poles'(nopo). Embryos from nopo females undergo mitotic arrest with barrel-shaped, acentrosomal spindles during the rapid S-M cycles of syncytial embryogenesis. We identified CG5140, which encodes a candidate RING domain-containing E3 ubiquitin ligase, as the nopogene. A conserved residue in the RING domain is altered in our EMS-mutagenized allele of nopo, suggesting that E3 ligase activity is crucial for NOPO function. We show that mutation of a DNA checkpoint kinase, CHK2,suppresses the spindle and developmental defects of nopo-derived embryos, revealing that activation of a DNA checkpoint operational in early embryos contributes significantly to the nopo phenotype. CHK2-mediated mitotic arrest has been previously shown to occur in response to mitotic entry with DNA damage or incompletely replicated DNA. Syncytial embryos lacking NOPO exhibit a shorter interphase during cycle 11, suggesting that they may enter mitosis prior to the completion of DNA replication. We show that Bendless (BEN), an E2 ubiquitin-conjugating enzyme, interacts with NOPO in a yeast two-hybrid assay; furthermore, ben-derived embryos arrest with a nopo-like phenotype during syncytial divisions. These data support our model that an E2-E3 ubiquitination complex consisting of BEN-UEV1A (E2 heterodimer) and NOPO (E3 ligase) is required for the preservation of genomic integrity during early embryogenesis.

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“…The TNF-receptorassociated factor (TRAF)-interacting protein (TRAIP, also known as TRIP or RNF206) is a RING-type E3 ubiquitin ligase (Besse et al, 2007), but hitherto no in vivo substrate has been identified. Ectopically expressed TRAIP interacts with TRAF proteins and represses NF-kB signaling (Besse et al, 2007;Lee et al, 1997), although this might not be physiologically relevant (Chapard et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

The TRAF-interacting protein (TRAIP) is a regulator of the spindle assembly checkpoint

Chapard¹,

Meraldi²,

Gleich³

et al. 2014

Journal of Cell Science

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Accurate chromosome segregation during mitosis is temporally and spatially coordinated by fidelity-monitoring checkpoint systems. Deficiencies in these checkpoint systems can lead to chromosome segregation errors and aneuploidy, and promote tumorigenesis. Here, we report that the TRAF-interacting protein (TRAIP), a ubiquitously expressed nucleolar E3 ubiquitin ligase important for cellular proliferation, is localized close to mitotic chromosomes. Its knockdown in HeLa cells by RNA interference (RNAi) decreased the time of early mitosis progression from nuclear envelope breakdown (NEB) to anaphase onset and increased the percentages of chromosome alignment defects in metaphase and lagging chromosomes in anaphase compared with those of control cells. The decrease in progression time was corrected by the expression of wild-type but not a ubiquitin-ligase-deficient form of TRAIP. TRAIP-depleted cells bypassed taxol-induced mitotic arrest and displayed significantly reduced kinetochore levels of MAD2 (also known as MAD2L1) but not of other spindle checkpoint proteins in the presence of nocodazole. These results imply that TRAIP regulates the spindle assembly checkpoint, MAD2 abundance at kinetochores and the accurate cellular distribution of chromosomes. The TRAIP ubiquitin ligase activity is functionally required for the spindle assembly checkpoint control.

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TRAF-interacting protein (TRIP) is a RING-dependent ubiquitin ligase

Cited by 33 publications

References 16 publications

TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress

TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress

no polesencodes a predicted E3 ubiquitin ligase required for early embryonic development ofDrosophila

The TRAF-interacting protein (TRAIP) is a regulator of the spindle assembly checkpoint

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