Cellular protein TTRAP interacts with HIV-1 integrase to facilitate viral integration

Zhang, Jian Qi; Wang, Jing jing; Li, Wen Juan; Huang, Lu; Tian, Ling; Xue, Jing; Chen, Jin Zhong; Jia, William

doi:10.1016/j.bbrc.2009.06.153

Cited by 20 publications

(12 citation statements)

References 19 publications

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“…The mammalian expression vector pcDNA3.1-TTRAP was constructed as described previously (14). The cDNA sequences for the mutants TTARP E152A and TTRAP D262A were generated with PCR using pcDNA3.1-TTRAP as a template and subcloned into the vector pcDNA3.1/myc-His(-) A (Life Technologies, Carlsbad, CA) between the Eco R I and Bam H I sites.…”

Section: Methodsmentioning

confidence: 99%

“…In 2009, TTRAP, also known as tyrosyl DNA phosphodiesterase-2 (TDP2), was shown to be the first 5’- tyrosyl DNA phosphodiesterase necessary for the repair of DNA double-strand breaks (11). Proteins derived from exogenous pathogens, such as Hantaan hantavirus (HTNV) nucleocapsid proteins, ΦC31 and HIV-1 integrases, interact with TTRAP directly (12-14). TTRAP has also been identified as a novel promyelocytic leukemia nuclear body (PML NB) protein involved in the regulation of ribosome biogenesis (15,16).…”

Section: Introductionmentioning

confidence: 99%

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Overexpression of TTRAP inhibits cell growth and induces apoptosis in osteosarcoma cells

Zhou

Shen²,

Xue³

et al. 2013

BMB Reports

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TTRAP is a multi-functional protein that is involved in multiple aspects of cellular functions including cell proliferation, apoptosis and the repair of DNA damage. Here, we demonstrated that the lentivirus-mediated overexpression of TTRAP significantly inhibited cell growth and induced apoptosis in osteosarcoma cells. The ectopic TTRAP suppressed the growth and colony formation capacity of two osteosarcoma cell lines, U2OS and Saos-2. Cell apoptosis was induced in U2OS cells and the cell cycle was arrested at G2/M phase in Saos-2 cells. Exogenous expression of TTRAP in serum-starved U2OS and Saos-2 cells induced an increase in caspase-3/-7 activity and a decrease in cyclin B1 expression. In comparison with wild-type TTRAP, mutations in the 5'-tyrosyl-DNA phosphodiesterase activity of TTRAP, in particular TTRAPE152A, showed decreased inhibitory activity on cell growth. These results may aid in clarifying the physiological functions of TTRAP, especially its roles in the regulation of cell growth and tumorigenesis. [BMB Reports 2013; 46(2): 113-118]

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Overexpression of TTRAP inhibits cell growth and induces apoptosis in osteosarcoma cells

Zhou

Shen²,

Xue³

et al. 2013

BMB Reports

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“…It was named following the prior discovery by Nash and coworkers (14) of TDP1, which repairs Top1 cleavage complexes (Top1cc) by cleaving 3Ј-tyrosyl-DNA bonds (14). TDP2 was initially named TTRAP and EAPII because of its role in NF-B (15) and MAPK-ERK (16) signaling transduction, in transcription regulation (17), in zebrafish development (18), and in HIV-1 integration (19). It also promotes cancer cell proliferation (20) and regulates rRNA biogenesis (21).…”

Section: Tdp2 Is a Multifunctional Enzyme Previously Known For Its Romentioning

confidence: 99%

Biochemical Characterization of Human Tyrosyl-DNA Phosphodiesterase 2 (TDP2/TTRAP)

Gao

Huang

Marchand

et al. 2012

Journal of Biological Chemistry

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Background: TDP2 is the only known tyrosine 5Ј-phosphodiesterase. Results: Recombinant human TDP2 preferentially processes single-stranded DNA ends. Its catalytic site is similar to APE-1 and consists of at least four essential residues Asn-120, Glu-152, Asp-262, and His-351 and two divalent metals. Conclusion: We elucidated the catalytic mechanisms of TDP2 and its substrate preference. Significance: TDP2 is critical for the repair of trapped topoisomerase complexes.

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“…Importin 7 (Imp7) has been proposed to play a role in nuclear import of HIV-1 DNA as well, and knockdown of Imp7 reduced nuclear accumulation of HIV-1 DNA, but had only modest effects on replication [100]. TRAF and TNF receptor-associated protein (TTRAP), a promyelocytic leukemia nuclear body associated protein (PML-NB), was isolated in a yeast two-hybrid screen with HIV-1 integrase as bait and its knockdown was shown to reduce viral integration [101]. A recent yeast two-hybrid screen using acetylated HIV-1 IN as bait identified thirteen cofactors [102].…”

Section: Identifying and Isolating Interacting Factorsmentioning

confidence: 99%

Interactions of Host Proteins with the Murine Leukemia Virus Integrase

Studamire

Goff

2010

Viruses

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Retroviral infections cause a variety of cancers in animals and a number of diverse diseases in humans such as leukemia and acquired immune deficiency syndrome. Productive and efficient proviral integration is critical for retroviral function and is the key step in establishing a stable and productive infection, as well as the mechanism by which host genes are activated in leukemogenesis. Host factors are widely anticipated to be involved in all stages of the retroviral life cycle, and the identification of integrase interacting factors has the potential to increase our understanding of mechanisms by which the incoming virus might appropriate cellular proteins to target and capture host DNA sequences. Identification of MoMLV integrase interacting host factors may be key to designing efficient and benign retroviral-based gene therapy vectors; key to understanding the basic mechanism of integration; and key in designing efficient integrase inhibitors. In this review, we discuss current progress in the field of MoMLV integrase interacting proteins and possible roles for these proteins in integration.

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Cellular protein TTRAP interacts with HIV-1 integrase to facilitate viral integration

Cited by 20 publications

References 19 publications

Overexpression of TTRAP inhibits cell growth and induces apoptosis in osteosarcoma cells

Overexpression of TTRAP inhibits cell growth and induces apoptosis in osteosarcoma cells

Biochemical Characterization of Human Tyrosyl-DNA Phosphodiesterase 2 (TDP2/TTRAP)

Interactions of Host Proteins with the Murine Leukemia Virus Integrase

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