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

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

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Hisashi Hirano

PROVIDER: PXD020706 | JPOST Repository | Tue Aug 03 00:00:00 BST 2021

REPOSITORIES: jPOST

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			Action	DRS
	yeast_1.raw	Raw
	yeast_10.raw	Raw
	yeast_11.raw	Raw
	yeast_12.raw	Raw
	yeast_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 Human 26S proteasome

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

2021-08-03 | PXD020705 | JPOST Repository

Activity guided profiling of yeast proteasome - protein extraction test

Project description:This experiment compared the impact of protein extraction conditions on the identification and quantification of proteasome subunits in WT yeast. It involved comparing proteins extracted from identical WT yeast samples under two different conditions: native and denaturing (in the presence of SDS and TCA).

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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.

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Synergistic effects of TOR and proteasome pathways on the yeast transcriptome and cell growth

Project description:The experiments were designed to interrogate the genetic interaction relationship between the TOR signalling pathway and the UPS-proteasome pathway in gene expression and cell growth. Yeast cells (BY4742pdr5delta) were treated with the drug vehicle, MG132 (50uM), rapamycin (200ng/ml) or both drugs. Samples in triplicates were taken at 0, 1, 2 and 3hours after treatment. Transcriptome were assayed using Affimetrixs genechips (Yeast 2).

2013-05-24 | E-MTAB-1550 | 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.

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Structural Analysis of the 20S Proteasome using Native Mass Spectrometry and Ultraviolet Photodissociation

Project description:The yeast 20S proteasome was analyzed using native mass spectrometry combined with UVPD, HCD, and vT-ESI. Nano-LC-MS-EThcD was used to characterize the primary sequence features of the 20S subunits.

2024-11-01 | PXD056549 | JPOST Repository

Tagging the proteasome active site ?5 causes tag specific phenotypes in yeast.

Project description:The efficient and timely degradation of proteins is crucial for many cellular processes and to maintain general proteostasis. The proteasome, a complex multisubunit protease, plays a critical role in protein degradation. Therefore, it is important to understand the assembly, regulation, and localization of proteasome complexes in the cell under different conditions. Fluorescent tags are often utilized to study proteasomes. A GFP-tag on the ?5 subunit, one of the core particle (CP) subunits with catalytic activity, has been shown to be incorporated into proteasomes and commonly used by the field. We report here that a tag on this subunit results in aberrant phenotypes that are not observed when several other CP subunits are tagged. These phenotypes appear in combination with other proteasome mutations and include poor growth, and, more significantly, altered 26S proteasome localization. In strains defective for autophagy, ?5-GFP tagged proteasomes, unlike other CP tags, localize to granules upon nitrogen starvation. These granules are reflective of previously described proteasome storage granules but display unique properties. This suggests proteasomes with a ?5-GFP tag are specifically recognized and sequestered depending on physiological conditions. In all, our data indicate the intricacy of tagging proteasomes, and possibly, large complexes in general.

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

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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.

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