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Identification of novel interaction partners of threonine aspartase1

ABSTRACT: The goal of this project was to identify interaction partners of human Taspase 1 using a combination of affinity enrichment and mass spectrometry.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Farnusch Kaschani

LAB HEAD: Farnusch Kaschani

PROVIDER: PXD035546 | Pride | 2023-03-11

REPOSITORIES: pride

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Dataset's files

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			Action	DRS
	ACE_0496_GFP.fasta	Fasta
	ACE_0496_UP000005640_9606.fasta	Fasta
	ACE_0533_LO01.raw	Raw
	ACE_0533_LO02.raw	Raw
	ACE_0533_LO03.raw	Raw

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1 - 5 of 13

Publications

Taspase1 Facilitates Topoisomerase IIβ-Mediated DNA Double-Strand Breaks Driving Estrogen-Induced Transcription.

Oelschläger Lisa L Stahl Paul P Kaschani Farnusch F Stauber Roland H RH Knauer Shirley K SK Hensel Astrid A

Cells 20230118 3

The human protease Taspase1 plays a pivotal role in developmental processes and cancerous diseases by processing critical regulators, such as the leukemia proto-oncoprotein MLL. Despite almost two decades of intense research, Taspase1's biology is, however, still poorly understood, and so far its cellular function was not assigned to a superordinate biological pathway or a specific signaling cascade. Our data, gained by methods such as co-immunoprecipitation, LC-MS/MS and Topoisomerase II DNA cl ...[more]

PMID: 36766705

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2024-05-21 | PXD040000 | Pride

Effect of Cpd1 on melanoma proteome

Project description:Investigation of the time dependent effect of Cpd1 (small molecule interactor) on the proteome composition of melanoma WM3734 line by label-free quantification using mass spectrometry. The goal was to identify which protein abundances are increased upon treatment with Cpd1. Melanoma cell line WM3734 was treated with Cpd1 and with the control DMSO. Samples were taken at two time points, 24h and 72h.

2022-03-14 | PXD008757 | Pride

Ubiquitin-independent disassembly by a p97 AAA-ATPase complex drives PP1 holoenzyme formation

Project description:Protein phosphatase-1 (PP1) dephosphorylates a broad spectrum of substrates to regulate a myriad of cellular processes. This functional diversity relies on the ordered assembly of alternative PP1 holoenzymes. Here, we show that newly synthesized PP1 is first held in an inactive complex by its partners SDS22 and inhibitor-3 (I3) that needs to be disassembled by the p97 AAA-ATPase to promote exchange to substrate specifiers. Unlike p97-mediated degradative processes that require the Ufd1-Npl4 ubiquitin adapters, p97 is targeted to PP1 by p37 and related adapter proteins. Reconstitution with purified components revealed direct interaction of the p37 SEP domain with I3 without the need of ubiquitination, and ATP-driven pulling of I3 into the central channel of the p97 hexamer, which triggers dissociation of I3 and SDS22. Thus, we establish regulatory ubiquitin-independent protein complex disassembly as part of the functional arsenal of p97 and define an unanticipated essential step in PP1 biogenesis that illustrates the molecular challenges of ordered subunit exchange.

2018-10-23 | PXD010750 | Pride

Effect of fluvastatin-treatment on the proteome and phosphor-proteome in metastatic pancreatic cancer cells

Project description:Fluvastatin has been identified as novel inhibitors of metastasis in pancreatic cancer. In multiple in vivo and in vitro experiments the compounds phenotypic effects was validated. Since under drug treatment the transcriptomic changes in examined cell lines were rather small, we expected the underlying mechanistic effect to be on the level of the proteome and more importantly the phospho-proteome. To evaluate this assumption we performed label-free full proteome and phosphoproteomics experiments on Fluvastatin treated ASPC1 cells.

2021-11-29 | PXD022345 | Pride

Effect of Bion (BTH treatment) in GST activities on 6-week old A.thaliana plants

Project description:The goal of this project was to investigate GSTs labelled by GST-G probe in non-treated Arabidopsis (Water samples: Click control vs GST-G) or GSTs activated upon Bion treatment of Arabidopsis (Water GST-G vs Bion GST-G).

2024-01-26 | PXD045884 | Pride

Proteomic differences in the synovial fluid of patients undergoing septic or aseptic revision arthroplasty

Project description:In 21 patients undergoing revision arthroplasty due to septic or aseptic implant loosening, synovial fluid was collected intraoperatively after opening the joint capsule. In a proteomic MS approach, we wanted now to investigate these synovial fluids for novel proteogenic markers of periprosthetic infections.

2024-05-21 | PXD047507 | Pride

Cathepsin L Regulates Metabolic Networks Controlling Rapid Cell Growth and Proliferation

Project description:Rapidly proliferating cells reshape their metabolism to satisfy their ever-lasting need for building blocks. This phenomenon is exemplified in certain malignant conditions but also occurs during embryonic development, when cells rely heavily on glycolytic metabolism to exploit their metabolic intermediates for biosynthetic routes. How cells regulate this metabolic makeover is currently unknown. Here we report that loss of cathepsin L (CtsL) is associated with fast proliferation rate and enhanced glycolytic metabolism that depend on lactate dehydrogenase A (LDHA) activity. Furthermore, we show that CtsL inhibition led to increased LDHA expression, suggesting of a causal relationship between LDHA expression and function. In conclusion, we propose that CtsL regulate this metabolic circuit to keep cell division under check.

2019-05-06 | PXD011588 | Pride

Activity profiling of αlpha-glycosidases in plants

Project description:With nearly 140 α-glycosidases in 14 different families, plants are well equipped with enzymes that can break the α-glucosidic bonds in a large diversity of molecules. Here, we introduce activity profiling of α-glycosidases in plants using α-configured cyclophellitol aziridine probes carrying various fluorophores or biotin. In Arabidopsis, these probes label members of the GH31 family of Glycosyl Hydrolases, including ER-resident α-glucosidase-II RSW3/PSL5 and Golgi-resident α-mannosidase-II HGL1, which both trim N-glycans on glycoproteins. We also detect the active state of extracellular α-glycosidases such as α-xylosidase XYL1, which acts on xyloglucan in the cell wall to promote cell expansion, and α-glucosidase AGLU1, which acts in starch hydrolysis and can suppress fungal invasion. α-glycosidase labelling causes specific signals at 100-130 kDa that are pH-dependent and can be supressed by α-glycosidase inhibitors miglitol and acarbose. The α-glycosidase probes display similar miglitol-sensitive signals in leaf extracts of in a broad range of plant species. To show its use on a non-model plant, we applied glycosidase activity profiling on Crocus sativa, a cash crop for the production of saffron spice. Using a combination of biotinylated glycosidase probes, we identified and quantified 70 active glycosidases in stigma stages 1 and 4 of saffron (Crocus sativa L.), ten of which are differentially active. We also uncover massive changes in hydrolase activities in corms upon infection with Fusarium oxysporum using multiplex fluorescent labelling in combination with probes for serine hydrolases and cysteine proteases. These experiments demonstrate the ease by which active α-glycosidases and other hydrolases can be displayed in non-model plants.

2018-05-17 | PXD009014 | Pride

Proteogenomics uncovers critical elements of host response in bovine soft palate epithelial cells following in vitro infection with foot-and-mouth disease virus (FMDV)

Project description:The pathogen and host factors that contribute to the establishment of foot-and-mouth disease virus (FMDV) persistence are currently not understood. Using primary bovine soft palate multilayers in combination with RNA sequencing, we analyzed the transcriptional responses during acute and persistent FMDV infection.

2019-01-18 | E-MTAB-7605 | biostudies-arrayexpress

Large-scale activity profiling of the apoplast upon bacterial infection

Project description:Pathogens suppress hydrolases in the plant apoplast to cause disease. Despite the importance of these enzyme-inhibitor interaction to plant diseases, to date only a handful examples have been described. Unravelling new plant targets and their inhibitory mechanisms will identify novel components of the plant immune system and point to molecular coevolution operating in the apoplast. Here, we simultaneously monitor the changes in activity of over 170 extracellular enzymes during bacterial infection.

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