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MS analsysis of phosphoproteins separated by phos-tag diagonal electrophoresis of Human 26S proteasome

ABSTRACT: Phosphorylation status of human 26S proteasome subunits was analyzed by phos-tag diagonal electrophoresis and GeLC-MS analysis.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Hisashi Hirano

PROVIDER: PXD020705 | JPOST Repository | Tue Aug 03 00:00:00 BST 2021

REPOSITORIES: jPOST

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			Action	DRS
	huaman_10.raw	Raw
	human_1.raw	Raw
	human_11.raw	Raw
	human_12.raw	Raw
	human_13.raw	Raw

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Publications

Phos-tag diagonal electrophoresis precisely detects the mobility change of phosphoproteins in Phos-tag SDS-PAGE.

Okawara Yuki Y Hirano Hisashi H Kimura Ayuko A Sato Natsumi N Hayashi Yuriko Y Osada Makoto M Kawakami Takao T Ootake Norihisa N Kinoshita Eiji E Fujita Kiyotaka K

Journal of proteomics 20201007

Phos-tag diagonal electrophoresis was developed to identify precisely a change in electrophoretic mobility of phosphoproteins in Phos-tag SDS-PAGE. Previously, if a single protein band was detected, it was impossible to determine whether mobility of the protein altered by Mn<sup>2+</sup> Phos-tag in Phos-tag SDS-PAGE gels because SDS-PAGE and Phos-tag SDS-PAGE were performed on different gels. Moreover, when multiple protein bands were detected, it was difficult to determine whether the band wit ...[more]

PMID: 33035715

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MS analsysis of phosphoproteins separated by phos-tag diagonal electrophoresis of yeast 26S proteasome

Project description:Phosphorylation status of yeast 26S proteasome subunits was analyzed by phos-tag diagonal electrophoresis and GeLC-MS analysis.

2021-08-03 | PXD020706 | JPOST Repository

Proteasome Function is Required for Platelet Production

Project description:RNA-seq expression analysis of transcripts encoding proteasome subunits in human CD34+ cord blood cell-derived megakaryocytes and mouse bone marrow-derived megakaryocytes. Analysis of transcript expression in human CD34+ cord blood cell-derived megakaryocytes and mouse bone marrow-derived megakaryocytes.

2015-01-31 | E-GEOD-58202 | biostudies-arrayexpress

Proteasome Function is Required for Platelet Production

Project description:RNA-seq expression analysis of transcripts encoding proteasome subunits in human CD34+ cord blood cell-derived megakaryocytes and mouse bone marrow-derived megakaryocytes.

2015-01-31 | GSE58202 | GEO

Proteasome gene expression is controlled by the coordinated functions of multiple transcription factors

Project description:Proteasome activity is crucial for cellular integrity, but how tissues adjust proteasome content in response to catabolic stimuli is uncertain. Here, we demonstrate that transcriptional coordination by multiple transcription factors is required to increase proteasome content and activate proteolysis in catabolic states. Using denervated mouse muscle as a model system for accelerated proteolysis in vivo, we reveal that a two-phase transcriptional program activates genes encoding proteasome subunits and assembly chaperones to boost an increase in proteasome content. Initially, gene induction is necessary to maintain basal proteasome levels, and in a more delayed phase (7-10 d after denervation) it stimulates proteasome assembly to meet cellular demand for excessive proteolysis. Intriguingly, the transcription factors PAX4 and α-PALNRF-1 control the expression of proteasome among other genes in a combinatorial manner, driving cellular adaptation to muscle denervation. Consequently, PAX4 and α-PALNRF-1 represent new therapeutic targets to inhibit proteolysis in catabolic diseases (e.g. type-2 diabetes, cancer).

2024-05-01 | GSE232348 | GEO

Phos-tag SDS-PAGE followed by LC-MS/MS analysis of in vitro phosphorylated Nab2, Foxk1, and HURP

Project description:Purified GST-fused Nab2, Foxk1, and HURP were incubated with ATP in the presence or absence of His-tagged active ERK in vitro, separated by Phos-tag SDS-PAGE, and visualized by CBB staining. The most shifted regions of protein bands on the Phos-tag-containing gels were excised, digested with trypsin, and analyzed by LC-MS/MS.

2022-03-03 | PXD028837 | JPOST Repository

Tight Junction Protein 1 is a Modulator and Biomarker of Proteasome Inhibitor Sensitivity in Multiple Myeloma

Project description:Proteasome inhibitors are important chemotherapeutics in the treatment of multiple myeloma, but they are currently used empirically as no markers of sensitivity have been validated. We have identified expression of tight junction protein (TJP) 1 as being associated with sensitivity of plasma cells in vitro and in vivo to proteasome inhibitors. TJP1 suppressed expression of genes in the major histocompatibility class II region, including two catalytically active immunoproteasome subunits, thereby decreasing proteasome activity, a critical determinant of proteasome inhibitor sensitivity. This occurred through suppression by TJP1 of signaling through the epidermal growth factor receptor/Janus kinase 1/signal transducer and activator of transcription 3 pathway. In the clinic, high TJP1 expression in myeloma patients was associated with a significantly higher likelihood of responding to bortezomib, and with a longer time-to-progression after treatment. Taken together, these data support the use of TJP1 as a biomarker of sensitivity and resistance to proteasome inhibitors. To further elucidate mechanisms of bortezomib resistance, we developed human-derived multiple myeloma cell lines with a 4-fold or greater resistance to bortezomib. Then total RNA for bortezomib resistant (BR) and wild type (WT) was extracted and used for comparison by gene expression profiling.

2015-12-31 | E-GEOD-52369 | biostudies-arrayexpress

siRNA of human MCF7 cells incubated with proteasome inhibitors bortezomib or Argyrin A or proteasome activity and knocked down for proteosomal subunits

Project description:Reduction in the cellular levels of the cyclin kinase inhibitor p27kip1 are frequently found in many human cancers and correlate directly with patient prognosis. Specifically ubiquitin dependent proteasomal turnover has been shown to cause reduced p27 expression in many human cancers. We recently demonstated that expression of a stabilized version of p27kip1 (p27kip1T187A) in a genetically modified mouse significantly reduced the number of intestinal adenomatous polyps which progressed to invasive carcinomas. Based on this work we set out to identify compounds which lead to a re-expression of p27 in cancer tissues. In this work we identify Argyrin A a compound derived from myxobacterium archangium gephyra as a potent inducer of p27kip1 expression. Argyrin A induces apoptosis in human colon cancer xenografts and tumor vasculature in vivo leading to a profound reduction in tumor size at well tolerated levels. Argyrin A functions are strictly dependent on the expression of p27kip1 as neither tumor cells nor endothelial cells which do not express p27kip1 respond to this compound. Surprisingly the molecular mechanism by which Argyrin A exerts its p27 dependent biological function is through a potent inhibition of the 20S proteasome. Experiment Overall Design: MCF7 cells were incubated with proteasome inhibitors bortezomib or Argyrin A or proteasome activity was reduced by treatment with siRNA against proteasomal subunits and gene expression profiles were determined at different timepoints thereafter.

2008-06-16 | E-GEOD-8565 | biostudies-arrayexpress

Absolute quantification of proteasome subunits

Project description:we prepared synthetic proteins corresponding to 30 of the proteasome subunits by stable isotope labeling and then performed absolute quantification.

2020-11-13 | PXD016260 | JPOST Repository

Tight Junction Protein 1 is a Modulator and Biomarker of Proteasome Inhibitor Sensitivity in Multiple Myeloma

2015-12-31 | GSE52369 | GEO

GLA and profiling of proteasome, Spt23 and Mga2

Project description:The proteasome can regulate transcription through proteolytic processing of transcription factors and via gene locus binding, but few targets of proteasomal regulation have been identified. Using genome-wide location analysis and transcriptional profiling in Saccharomyces cerevisiae, we have established which genes are bound and regulated by the proteasome, and by Spt23 and Mga2, transcription factors activated by the proteasome. We observed proteasome association with gene sets that are highly transcribed, controlled by the mating-type loci, and involved in lipid metabolism. At ribosomal protein genes, proteasome and RNA polymerase II binding was enriched in a proteasome mutant, indicating a role for the proteasome in dissociating elongation complexes. The genomic occupancies of Spt23 and Mga2 overlapped significantly with the genes bound by the proteasome. Finally, the proteasome acts in two distinct ways, one dependent and one independent of Spt23/Mga2 cleavage, providing evidence for cooperative gene regulation by the proteasome and its substrates. Keywords: ChIP-chip; genetic modification transcriptional profiling Six genomic localization analysis (GLA, ChIP2) experiments are represented by 18 samples. Six transcriptional profiling experiments (prof) are also represented. Experiments were generally done in triplicate, with fluors swapped on the third replicate.

2006-02-28 | E-GEOD-4272 | biostudies-arrayexpress

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