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Characterization of DNp73β protein interaction partners

ABSTRACT: The human osteosarcoma cell line SaOs2 was transduced with adenoviral vectors expressing DNp73β. Subsequent Co-IP/MS analysis characterised the p73 isoform-specific interactome. The raw data include identified cofactors and provide a basis for further research into p73-associated complexes.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Elke Hammer

LAB HEAD: Elke Hammer

PROVIDER: PXD058814 | Pride | 2025-08-07

REPOSITORIES: Pride

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			Action	DRS
	181218_HF_UL_BMFZ_IP1_Ctrl_8ul.msf	Msf
	181218_HF_UL_BMFZ_IP2_TAp73_8ul.raw	Raw
	181218_HF_UL_BMFZ_IP3_DNp73_8ul.msf	Msf
	181218_HF_UL_BMFZ_IP3_DNp73_8ul.raw	Raw
	190416_QE1_UL_BMFZ_Ctrl_4ul.msf	Msf

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Publications

TAp73α drives cancer metastasis via PPI-mediated derepression of the neuronal HDAC2/REST-GABBR2 axis.

Murr Nico N Richter Christin C Gupta Shailendra K SK Hammer Elke E Trakooljul Nares N Stoll Anja A Möller Steffen S Neumann Lukas E LE Pützer Brigitte M BM Spitschak Alf A

Cancer letters 20250610

Metastasis is the leading cause of death in patients with malignant melanoma, yet the molecular and transcriptional mechanisms remain elusive. This study reveals a crucial role of the p53 homolog, TAp73α, in promoting melanoma metastasis. Using multi-omics approaches combining transcriptomics, proteomics, cistromics and 3D modeling, we discovered a paradigm-shifting mechanism by which TAp73α binds directly to HDAC2, disassembles the HDAC2/REST repressor complex and aberrantly triggers activation ...[more]

PMID: 40505831

Similar Datasets

Characterization of TAp73α protein interaction partners

Project description:The human osteosarcoma cell line SaOs2 was transduced with adenoviral vectors expressing TAp73α. Subsequent Co-IP/MS analysis characterised the p73 isoform-specific interactome. The raw data include identified cofactors and provide a basis for further research into p73-associated complexes.

2025-08-07 | PXD058816 | Pride

Comparative analysis of ChAdOx1 nCoV-19 and Ad26.COV2.S SARS-CoV-2 vector vaccines

Project description:Vector-based SARS-CoV-2 vaccines such as AstraZeneca's ChAdOx1 nCoV-19 have been associated with vaccine-induced thrombosis (TTS/VITT). We studied ChAdOx1 nCov-19 (AstraZeneca) and Ad26.COV2.S (Johnson & Johnson) and compared the vaccines using proteomics with mass spectrometric measurements. We could demonstrate that ChAdOx1 nCoV-19 contained significant amounts of human proteins in addition to adenoviral proteins. This was not the case for Ad26.COV2.S. Among the detected human proteins, proteasome subunits beta 1/delta and beta 5/MB1 were identified. In summary, both studied SARS-CoV-2 vaccines are markedly different concerning their content of contaminating proteins, which is most likely a determining factor for different frequencies of TTS/VITT after their application.

2023-05-04 | PXD027344 | Pride

Transcription profiling of human H1299 cellls transformed with different p73/p53 constructs shows C-terminal diversity within the p53 family accounts for differences in DNA binding and transcriptional activity

Project description:The p53 family is known as a family of transcription factors with functions in tumor suppression and development. Whereas the central DNA binding domain is highly conserved among the three family members p53, p63 and p73, the C-terminal domains (CTDs) are diverse and subject to alternative splicing and post-translational modification. Here we demonstrate that the CTDs strongly influence DNA binding and transcriptional activity. While p53 and the p73 isoform p73ï§ have basic CTDs and form weak sequence-specific protein-DNA complexes, the major p73 isoforms ï¡, ï¢ and ï¤ have neutral CTDs and bind DNA strongly. A basic CTD has been previously shown to enable sliding along the DNA backbone and to facilitate the search for binding sites in the complex genome. Our experiments, however, reveal that a basic CTD also reduces protein-DNA complex stability, intranuclear mobility, promoter occupancy in vivo, transgene activation and induction of cell cycle arrest or apoptosis. A basic CTD in p53 and p73ï§ therefore provides both positive and negative regulatory functions presumably to enable rapid switching of protein activity in response to stress. In contrast, most p73 isoforms exhibit constitutive DNA binding activity consistent with a predominant role in developmental control. Experiment Overall Design: Infection of H1299 cell with different p73/p53 constructs by adenoviral system

2008-10-18 | E-GEOD-8660 | biostudies-arrayexpress

Transcription profiling of human steosarcoma cell line Saos-2 infected separately with p53 and TAp73beta expressing adenovirus to identify targets specifically regulated by TAp73

Project description:The p53 family consists of three members, p53, p73, and p63. These proteins share a high degree of amino-acid sequence similarity and major functional domains. The p53 gene, the first member of the family to be identified, is the most frequent target gene for genetic alterations in human cancers. In contrast, p73 and p63 are mainly involved in normal development and differentiation. These differences among the p53 family are likely to depend on activation or repression of different sets of target genes. In this study, to identify targets specifically regulated by p73, we performed microarray analysis and compared expression patterns in a human steosarcoma cell line Saos-2 infected separately with p53 and TAp73beta expressing adenovirus. Experiment Overall Design: Saos2 osteosarcoma cells were infected with p53, TAp73beta expressing or control adenovirus for 24 h and then harvested.

2008-11-15 | E-GEOD-13504 | biostudies-arrayexpress

The phosphatase PTPRG controls FGFR1 activity and influences sensitivity to FGFR kinase inhibitors

Project description:Recently, FGFR1 has been found to be overexpressed in osteosarcoma and thus represents an important target for precision medicine. However, because targeted cancer therapy based on FGFR inhibitors has so far been less efficient than expected, a detailed understanding of the target is important. We have here applied proximity labelling of FGFR1 in an osteosarcoma cell line to identify determinants of FGFR1 activity. Many known FGFR interactors were identified (e.g. FRS2, PLC, RSK2, SHC4, SRC), but the data also suggested novel determinants. A strong hit in our screen was the tyrosine phosphatase PTPRG. We show that PTPRG and FGFR1 interact and colocalize at the plasma membrane where PTPRG directly dephosphorylates activated FGFR1. We further show that osteosarcoma cell lines depleted for PTPRG display increased FGFR activity and are hypersensitive to stimulation by FGF1. In addition, PTPRG depletion elevated cell growth and negatively affected the efficacy of FGFR kinase inhibitors. Thus, PTPRG may have future clinical relevance by being a predictor of outcome after FGFR inhibitor treatment.

2018-01-29 | PXD006157 | Pride

The E2F4/p130 repressor complex cooperates with oncogenic Np73 to promote cell survival

Project description:Tumor suppressor p53 and its related proteins, p63 and p73, can be synthesized as multiple isoforms lacking part of the N- or C-terminal regions. Specifically, high expression of the Np73 isoform is notoriously associated with poor prognosis in cancer. Here, we have performed proteomics analysis of Np73 using as a cellular model human papillomavirus type 38-transformed keratinocytes (38HK) that express high levels of this isoform. We find that Np73 associates with the E2F4/p130 repressor complex through a direct interaction with E2F4. Remarkably, this interaction is favored by the N-terminal truncation of p73 characteristic of Np73 isoforms and is independent of the C-terminal splicing status. We show that the Np73-E2F4/p130 complex is recruited to the promoters of specific genes, thereby enforcing inhibition of their expression both in 38HK and in cancer-derived cell lines. Consistently, silencing of E2F4 in 38HK and in cancer cells resulted in induction of senescence. In conclusion, we have identified and characterized a novel transcriptional regulatory complex that exerts pro-proliferative functions in transformed cells

2023-02-28 | PXD022947 | Pride

Interplay between c-Jun and TAp73M-NM-1/M-NM-2 contributes to the apoptosis-survival balance

Project description:The p53-family member p73 functions in various cellular signaling pathways and can have tumor suppressor properties. Several isoforms of p73 exist that differ considerably in their function. Whereas the functions of the N-terminal isoforms (TA and M-NM-^TNp73) and their opposing pro- and anti-apoptotic roles became evident, the functional differences of the distinct C-terminal spliceforms of TAp73 have remained unclear. Here, we characterized the genomic binding sites for TAp73M-NM-1 and TAp73M-NM-2 and identified a specific p73 consensus binding-motif. Furthermore, an AP1 motif is strongly enriched close to binding sites for TAp73M-NM-1. These AP1 motif-containing target genes are selectively upregulated by TAp73M-NM-1, while their mRNA expression is repressed upon TAp73M-NM-2 induction. Recruitment of c-Jun to the respective AP1 sites was impaired upon TAp73M-NM-2 expression in part due to downregulation of c-Jun. We show that several of these AP1-site containing TAp73M-NM-1-induced genes reduce on apoptosis-induction suggesting an underlying molecular mechanism for the observed functional differences between TAp73M-NM-1 and TAp73M-NM-2. ChIP-seq and RNA-seq profiles of TAp73alpha, TAp73beta and p53 stably transfected in human osteosarcoma Saos cells

2011-03-01 | E-GEOD-15780 | biostudies-arrayexpress

Transcription profiling of mouseB-cell lymphomas with defined genetic alterations in p53 or p73

Project description:Induction of apoptosis by the tumor suppressor p53 is known to protect from Myc-driven lymphomagenesis. The p53 family member p73 is also a pro-apoptotic protein, which is activated in response to oncogenes like Myc. We therefore investigated whether p73 provides a similar protection from Myc-driven lymphomas as p53. To generate B-cell lymphomas with defined genetic alterations in p53 or p73, we crossed the Eµ-Myc transgenic to mice heterozygous for germ-line deletions in p53 (p53+/) or p73 (p73+/-). Lymphomas which have spontaneously developed in Eµ-Myc transgenic animals with the genotypes p53+/+, p53+/-, p73+/+, p73+/- or p73-/- were isolated when the animals were moribund and further processed for gene expression profiling with 22.5K cDNA microarrays.

2008-12-05 | E-MEXP-1620 | biostudies-arrayexpress

Gene expression signatures in HuH7 cells transfected with super hybrid p53 version 2.

Project description:The p53 tumor suppressor belongs to a gene family that includes two other structurally and functionally related members: p63 and p73. However, the regulation of p53 activity differs significantly from that of p73 and p63. To enhance the tumor suppressive activity of p53, we created a p63/p53 hybrid molecule, named p63-53O, which comprises the transcriptional activation and DNA-binding domains of TAp63? and the oligomerization domain of p53. In this study, we generated a series of p63-53O derivatives and developed an advanced hybrid molecule named “Super Hybrid p53 (SHp53).” SHp53 efficiently transactivated several proapoptotic genes, including CASP10, KCNK3, and PYCARD, compared with p53. Moreover, the silencing of these proapoptotic genes partially abolished the apoptotic response to SHp53 in human cancer cells. The potency of SHp53 for suppressing tumorigenesis was also evaluated using in vivo models. Thus, our results identify a better p63/p53 hybrid molecule for the development of anti-cancer therapies. HuH-7 human hepatocellular carcinoma cells were either transduced with adenoviral vectors expressing p53, TAp63gamma, p53-p63 hybrid (super hybrid p53 version 2, p63-53O-FL), or lacZ. After 24 hours, total RNA was isolated and analyzed by hybridization to Agilent-028004 SurePrint G3 Human GE 8x60K Microarray.

2013-05-23 | E-GEOD-42493 | biostudies-arrayexpress

Proteome data of a BP1092 mutant of Bordetella pertussis

Project description:Proteome data of a BP1092 mutant of Bordetella pertussis under virulence modulating and non-modulating conditions

2024-05-24 | PXD041940 | Pride