Thyroid Hormone Receptor Interacting Protein 13 (TRIP13) AAA-ATPase Is a Novel Mitotic Checkpoint-silencing Protein

Wang, Kexi; Sturt-Gillespie, Brianne; Hittle, James C.; Macdonald, Dawn; Chan, Gordon K.; Yen, Tim J.; Liu, Song‐Tao

doi:10.1074/jbc.m114.585315

Cited by 135 publications

(155 citation statements)

References 70 publications

Supporting

Mentioning

148

Contrasting

Order By: Relevance

“…These results clearly demonstrate that maintenance of the SAC is critical to prevent cancer formation. TRIP13 has been shown to promote the dissociation of the MCC complex (15)(16)(17), which subsequently inactivates the SAC to prevent the completion of mitosis (18). Thus, overexpression of TRIP13 and silencing of MCC components have similar effects on cells, since both can lead to dysregulation of the SAC.…”

Section: Discussionmentioning

confidence: 99%

“…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). Defects in the SAC pathway induce failure in chromosome separation and result in aneuploidy, which eventually leads to cellular apoptosis or transformation (19).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

TRIP13 is expressed in colorectal cancer and promotes cancer cell invasion

et al. 2016

View full text Add to dashboard Cite

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

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

TRIP13 is expressed in colorectal cancer and promotes cancer cell invasion

et al. 2016

View full text Add to dashboard Cite

show abstract

“…But recent attention has focused on mutual inhibition between the MCC and the APC/C (Reddy et al 2007), which requires a particular APC/C subunit, APC15 (Mansfeld et al 2011;Foster and Morgan 2012;Uzunova et al 2012). In animal cells, a second important player for MCC disassembly is the p31 comet protein (Habu et al 2002;Teichner et al 2011;Westhorpe et al 2011), which has recently been implicated in targeting an AAA ATPase to the MCC to initiate its disassembly (Eytan et al 2014;Wang et al 2014).…”

Section: The Biochemistry Of Mitosismentioning

confidence: 99%

The Biochemistry of Mitosis

Wieser

Pines

2015

Cold Spring Harb Perspect Biol

View full text Add to dashboard Cite

In this article, we will discuss the biochemistry of mitosis in eukaryotic cells. We will focus on conserved principles that, importantly, are adapted to the biology of the organism. It is vital to bear in mind that the structural requirements for division in a rapidly dividing syncytial Drosophila embryo, for example, are markedly different from those in a unicellular yeast cell. Nevertheless, division in both systems is driven by conserved modules of antagonistic protein kinases and phosphatases, underpinned by ubiquitin-mediated proteolysis, which create molecular switches to drive each stage of division forward. These conserved control modules combine with the self-organizing properties of the subcellular architecture to meet the specific needs of the cell. Our discussion will draw on discoveries in several model systems that have been important in the long history of research on mitosis, and we will try to point out those principles that appear to apply to all cells, compared with those in which the biochemistry has been specifically adapted in a particular organism.

show abstract

“…Neither the role of AGS7/Trip13 as a regulator of the thyroid hormone receptor nor G protein signaling functions have been elucidated in the kidney in vivo. Instead, most of the work involving AGS7/Trip13, which is also a homolog to mouse pachytene checkpoint 2 (mPCH2), has focused on its AAAATPase activity with emphasis on the mechanistic control of DNA damage repair (Bolcun-Filas et al, 2014), cell-cycle checkpoint, kinetochore control (Tipton et al, 2012;Wang et al, 2014), and meiotic recombination (Li and Schimenti, 2007;Roig et al, 2010). These initial studies led to recent highimpact findings regarding AGS7/Trip13 in reproductive cell biology (Li and Schimenti, 2007;Roig et al, 2010) and cancer (Banerjee et al, 2014).…”

Section: Group III Ags Proteinsmentioning

confidence: 99%

Activators of G Protein Signaling in the Kidney

Park

2015

J Pharmacol Exp Ther

View full text Add to dashboard Cite

Heterotrimeric G proteins play a crucial role in regulating signal processing to maintain normal cellular homeostasis, and subtle perturbations in its activity can potentially lead to the pathogenesis of renal disorders or diseases. Cell-surface receptors and accessory proteins, which normally modify and organize the coupling of individual G protein subunits, contribute to the regulation of heterotrimeric G protein activity and their convergence and/or divergence of downstream signaling initiated by effector systems. Activators of G protein signaling (AGS) are a family of accessory proteins that intervene at multiple distinct points during the activation-inactivation cycle of G proteins, even in the absence of receptor stimulation. Perturbations in the expression of individual AGS proteins have been reported to modulate signal transduction pathways in a wide array of diseases and disorders within the brain, heart, immune system, and more recently, the kidney. This review will provide an overview of the expression profile, localization, and putative biologic role of the AGS family in the context of normal and diseased states of the kidney.

show abstract

Thyroid Hormone Receptor Interacting Protein 13 (TRIP13) AAA-ATPase Is a Novel Mitotic Checkpoint-silencing Protein

Cited by 135 publications

References 70 publications

TRIP13 is expressed in colorectal cancer and promotes cancer cell invasion

TRIP13 is expressed in colorectal cancer and promotes cancer cell invasion

The Biochemistry of Mitosis

Activators of G Protein Signaling in the Kidney

Contact Info

Product

Resources

About