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Inhibition of CTNNB1-dependent transcription phenocopies loss of PSA in NMuMG cells.

By Mohadeseh Mehrabian (455336), Dylan Brethour (672163), Hansen Wang (272657), Zhengrui Xi (735628), Ekaterina Rogaeva (23289) and Gerold Schmitt-Ulms (195668)

Abstract

<p>(a) Comparison of global proteomes of stable PrP kd clones versus wt NMuMG cells and stable versus transient PrP-deficient cell clones. Of the total of 1421 proteins quantified in all global proteome analyses, relative levels of 41 proteins were changed by more than 20% in the direct comparisons. Four and three proteins had prior GO annotations, which identified them as ‘DNA binding’ and/or ‘Transcriptional regulators’. Based on these annotations, only β-catenin emerged as a DNA-binding transcriptional regulator whose levels are also changed during EMT. Note also that the level changes between stable kd cells and wt or transient kd NMuMG cells turned out to be equidirectional for all proteins whose levels changed more than 20%. (b) Transient kd of CTNNB1 or inhibitor-based disruption of protein-protein interactions between CTNNB1 and TCF or CBP reduces polysialylation of NCAM1. (c) Stable PrP ko or kd in NMuMG cells altered nuclear levels of SNAI1 and p133-CREB, developmental transcription factors known to interact with CTNNB1. Lamin A served as a nuclear reporter protein in these experiments, indicating both enrichment levels of nuclear fractions and equal protein loading. (d) Quantitation of nuclear levels of SNAI1 and p133-CREB in stable PrP ko or kd NMuMG clones versus wild-type or transient PrP kd NMuMG cells. The asterisks indicate significant differences in levels of SNAI1 (p = 0.029) and p133-CREB (p = 0.029) in cells that support or are impaired in NCAM1 polysialylation during EMT. (e) Cartoon depicting signaling pathways which may underlie differences in NCAM1 polysialylation in stable PrP-deficient cells.</p

Topics: Biological Sciences, NCAM 1 polysialylation, Neural Cell Adhesion Molecule 1, emt, ZIP metal ion transporters, Cellular Morphogenesis, Prion Protein Controls Polysialylation, PrP transcription, proteomics analysis, cell adhesion molecule 1, polysialyltransferase ST 8SIA gene, Neurodegenerative diseases, transcriptional regulator, cell model, candidate mediator, Proteomics data, prion protein
Year: 2015
DOI identifier: 10.1371/journal.pone.0133741.g006
OAI identifier: oai:figshare.com:article/1514596
Provided by: FigShare
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