Pch2 is a hexameric ring ATPase that remodels the chromosome axis protein Hop1

Chen, Cheng; Jomaa, Ahmad; Ortega, Joaquı́n; Alani, Eric

doi:10.1073/pnas.1310755111

Cited by 87 publications

(116 citation statements)

References 69 publications

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“…This finding supports the idea that when these proteins are aberrantly expressed in cells that lack the proteins necessary to subsequently remove them (e.g., Chen et al 2014;Lambing et al 2015), they may make chromosomes "sticky," driving aberrant interactions and missegregation. Recently, we found that a unique allele of ASY1, the A. thaliana homolog of HORMAD1/ HORMAD2 and Hop1 (Armstrong et al 2002), underwent a dramatic selective sweep following WGD in A. arenosa (Hollister et al 2012;Yant et al 2013).…”

Section: Dmc1supporting

confidence: 79%

Genome management and mismanagement—cell-level opportunities and challenges of whole-genome duplication

Yant

Bomblies

2015

Genes Dev.

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Whole-genome duplication (WGD) doubles the DNA content in the nucleus and leads to polyploidy. In whole-organism polyploids, WGD has been implicated in adaptability and the evolution of increased genome complexity, but polyploidy can also arise in somatic cells of otherwise diploid plants and animals, where it plays important roles in development and likely environmental responses. As with whole organisms, WGD can also promote adaptability and diversity in proliferating cell lineages, although whether WGD is beneficial is clearly context-dependent. WGD is also sometimes associated with aging and disease and may be a facilitator of dangerous genetic and karyotypic diversity in tumorigenesis. Scaling changes can affect cell physiology, but problems associated with WGD in large part seem to arise from problems with chromosome segregation in polyploid cells. Here we discuss both the adaptive potential and problems associated with WGD, focusing primarily on cellular effects. We see value in recognizing polyploidy as a key player in generating diversity in development and cell lineage evolution, with intriguing parallels across kingdoms.

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Section: Dmc1supporting

confidence: 79%

Genome management and mismanagement—cell-level opportunities and challenges of whole-genome duplication

Yant

Bomblies

2015

Genes Dev.

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“…In some instances, an AAA-ATPase can bind to different adaptor proteins, thus changing its substrate specificities and cellular functions (19). In the case of the TRIP13 AAA-ATPase and of its homologs, a role in meiotic recombination has been reported in mice, yeast, worms, and plants (25)(26)(27)(28). This function has been explained by their action to dislocate certain proteins from Recombinant Cdc20-Mad2 complex was expressed and purified as described in Materials and Methods and was added to the assay at 2 nM.…”

Section: Discussionmentioning

confidence: 99%

“…2A. chromatin (26)(27)(28). A different function of TRIP13 has been suggested by a proteomic data mining study that identified it as a kinetochore protein that interacts with p31 comet (16).…”

Section: Discussionmentioning

confidence: 99%

Disassembly of mitotic checkpoint complexes by the joint action of the AAA-ATPase TRIP13 and p31 ^comet

Eytan

Wang

Miniowitz-Shemtov

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

114

131

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Significance The mitotic checkpoint system has an important role to ensure accurate segregation of chromosomes in mitosis. This system regulates the activity of the ubiquitin ligase Anaphase-Promoting Complex/Cyclosome (APC/C) by the formation of a negatively acting Mitotic Checkpoint Complex (MCC). When the checkpoint is satisfied, MCC is disassembled, but the mechanisms of MCC disassembly are not well understood. We show here that the ATP-hydrolyzing enzyme Thyroid Receptor Interacting Protein 13 (TRIP13), along with the MCC-targeting protein p31 comet , promote the disassembly of the mitotic checkpoint complexes and the inactivation of the mitotic checkpoint. The results reveal an important molecular mechanism in the regulation of APC/C by the mitotic checkpoint.

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“…Mutations in the Walker A motif are known to disrupt ATP binding, whereas Walker B motif mutations disrupt ATP hydrolysis (2). Both were shown to be essential for the function of TRIP13 in yeast (13). The present study generated TRIP13 mutants that have mutations either in the Walker A or Walker B motifs, or in both motifs, including TRIP13-GK/AA, which has glycine 184 and lysine 185 in the Walker A motif substituted with alanine; and TRIP13-DE/NQ, which has aspartic acid 252 and glutamic acid 253 in the Walker B motif substituted with asparagine and glutamine, respectively; and TRIP13-GK/AA-DE/NQ, which has both mutations.…”

Section: Hct116 Cells That Constitutively Expressed Either Flag Ormentioning

confidence: 99%

“…Accumulating studies have demonstrated that TRIP13 plays pivotal roles in meiotic recombination and DNA repair in plants, yeast, worms and mice (8)(9)(10)(11)(12). TRIP13 forms a stable hexameric ring, and ATP binding, as well as ATP hydrolysis, are critical for the function of the protein (13). Previous studies have revealed that TRIP13 is a novel component of the spindle assembly checkpoint (SAC) pathway (14)(15)(16)(17), which is crucial for the accurate distribution of duplicated chromosomes (18).…”

Section: Introductionmentioning

confidence: 99%

TRIP13 is expressed in colorectal cancer and promotes cancer cell invasion

et al. 2016

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Abstract. Thyroid hormone receptor interactor 13 (TRIP13) is a member of the ATPases associated with various cellular activities family of proteins and is highly conserved in a wide range of species. Recent studies have demonstrated that TRIP13 is critical for the inactivation of the spindle assembly checkpoint and is associated with the progression of certain cancers. In the present study, the role of TRIP13 in colorectal cancer (CRC) was examined. Reverse transcription-quantitative polymerase chain reaction analysis revealed that TRIP13 messenger RNA was highly expressed in multiple CRC tissues. The depletion of TRIP13 in CRC cells suppressed cell proliferation, migration and invasion. To determine whether the catalytic activity of TRIP13 was critical for cancer progression, an inactive mutant of TRIP13 was expressed in CRC cells. The invasion of cancer cells that expressed the mutant TRIP13 was significantly reduced compared with that of the wild type TRIP13-expressing cancer cells. These results indicate that TRIP13 could be a potential target for CRC treatment. IntroductionThe ATPases associated with various cellular activities (AAA+) family of proteins comprises a functionally different group of enzymes that are involved in an array of cellular processes, including protein degradation, protein-complex disassembly and DNA replication (1). The AAA+ proteins are present in all kingdoms, and are characterized by the presence of conserved AAA+ domains that contain Walker A and Walker B motifs, followed by a conserved region called second region of homology (2). The majority of AAA+ proteins form hexamers to exert their biological functions. The chemical energy generated by adenosine triphosphate (ATP) hydrolysis by this family of proteins induces conformational changes in the substrate proteins to modulate their functions (3,4).A previous study reported that certain AAA+ enzymes are associated with tumor progression (5). For example, reptin [also known as RuvB-like (RUVBL) 2] and pontin (RUVBL1) have been demonstrated to be overexpressed in several tumors (5). These proteins interact with c-Myc or β-catenin, thus modulating their transcriptional activities to promote tumor progression (6). AAA+ proteins hydrolyze ATP, and thus, chemical inhibitors that disrupt the activities of cancer-associated AAA+ proteins may represent promising anti-cancer drugs.Thyroid hormone receptor interactor 13 (TRIP13, also known as 16E1BP and pachytene checkpoint 2) is a member of the AAA+ family proteins and is conserved in a wide range of species (7). It was first identified as a protein that interacts with human papilloma virus E1 proteins by a yeast two-hybrid analysis, but the physiological function of the interaction remains unknown (7). Accumulating studies have demonstrated that TRIP13 plays pivotal roles in meiotic recombination and DNA repair in plants, yeast, worms and mice (8-12). TRIP13 forms a stable hexameric ring, and ATP binding, as well as ATP hydrolysis, are critical for the function of the protein (13). Previous...

show abstract

Pch2 is a hexameric ring ATPase that remodels the chromosome axis protein Hop1

Cited by 87 publications

References 69 publications

Genome management and mismanagement—cell-level opportunities and challenges of whole-genome duplication

Genome management and mismanagement—cell-level opportunities and challenges of whole-genome duplication

Disassembly of mitotic checkpoint complexes by the joint action of the AAA-ATPase TRIP13 and p31 ^comet

TRIP13 is expressed in colorectal cancer and promotes cancer cell invasion

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Pch2 is a hexameric ring ATPase that remodels the chromosome axis protein Hop1

Cited by 87 publications

References 69 publications

Genome management and mismanagement—cell-level opportunities and challenges of whole-genome duplication

Genome management and mismanagement—cell-level opportunities and challenges of whole-genome duplication

Disassembly of mitotic checkpoint complexes by the joint action of the AAA-ATPase TRIP13 and p31 comet

TRIP13 is expressed in colorectal cancer and promotes cancer cell invasion

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Product

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Disassembly of mitotic checkpoint complexes by the joint action of the AAA-ATPase TRIP13 and p31 ^comet