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Formation of Toxic Oligomeric Assemblies of RNA-binding Protein: Musashi in Alzheimer’s disease

Sengupta, Urmi, Montalbano, Mauro, McAllen, Salome, Minuesa, Gerard, Kharas, Michael, Kayed, Rakez·2018·Acta Neuropathologica Communications
DOI 10.1186/s40478-018-0615-0PMC PMC6203984
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Fig. 1 Domain structures of Musashi proteins, alongside TDP-43, FUS and TIA-1, three extensively studied RBPs forming inclusions in neurodegenerative diseases. Tau domain structure is also represented. NLS Nuclear Localization Signal
Fig. 1 Domain structures of Musashi proteins, alongside TDP-43, FUS and TIA-1, three extensively studied RBPs forming inclusions in neurodegenerative diseases. Tau domain structure is also represented. NLS Nuclear Localization SignalCC BY · PubMed Central
Fig. 2 Biochemical and biophysical characterization of recombinant MSI1 and MSI2 protein aggregates (a) Western blot images showing in vitro aggregation of recombinant MSI1 and MSI2 aggregates as revealed by immunoblotting with α-Oligomer antibody, F11G3. Generic α-MSI1 antibody detected recombinant MSI1 aggregates, as well as Aβ aggregates. Whereas, α-MSI2 antibody detected only recombinant MSI2 aggregates. (b) AFM images of MSI1 and MSI2 protein aggregates showed different morphologies. MSI1 aggregates appeared as pear-shaped oligomers, while MSI2 had mostly spheroid oligomers. Proto-fibrils formation was observed in both MSI1 and MSI2 oligomers (black arrows, black scale bar: 100 nm). (c) GST pull down assay of MSI and tau demonstrates their physical interaction. Western blot analysis of immunoprecipitated GST-MSI1 and GST-MSI2 (Lane 2: IP’d GST-MSI1-Tau; Lane 4: IP’d GST-MSI2-tau) with Tau 13 (Pan-tau antibody) revealed the presence of tau proteins in the immunoprecipitated material as well. The inputs from the two reaction mixtures are also shown here (Lane 1: Tau + MSI1 input; Lane 3: Tau + MSI2 input). (d) Representative Western blot images of brain homogenates from AD (N = 4) and age-matched control cases (N = 4) demonstrating a significant increase in the levels of both MSI1 and MSI2 proteins ((p = 0.035, *; p = 0.005, **). (e) Representative images of both soluble and insoluble fractions of AD (N = 3) and age-matched control (N = 3) brain tissues obtained from filter trap assay. Soluble fractions from all the cases studied demonstrate increased levels of tau protein upon probing with Tau 13 antibody when compared to their insoluble fractions. Similarly, both MSI1 and MSI2 protein levels are increased in the soluble fractions compared to the insoluble fractions (p = 0.0279, *; p = 0.0045, **)
Fig. 2 Biochemical and biophysical characterization of recombinant MSI1 and MSI2 protein aggregates (a) Western blot images showing in vitro aggregation of recombinant MSI1 and MSI2 aggregates as revealed by immunoblotting with α-Oligomer antibody, F11G3. Generic α-MSI1 antibody detected recombinant MSI1 aggregates, as well as Aβ aggregates. Whereas, α-MSI2 antibody detected only recombinant MSI2 aggregates. (b) AFM images of MSI1 and MSI2 protein aggregates showed different morphologies. MSI1 aggregates appeared as pear-shaped oligomers, while MSI2 had mostly spheroid oligomers. Proto-fibrils formation was observed in both MSI1 and MSI2 oligomers (black arrows, black scale bar: 100 nm). (c) GST pull down assay of MSI and tau demonstrates their physical interaction. Western blot analysis of immunoprecipitated GST-MSI1 and GST-MSI2 (Lane 2: IP’d GST-MSI1-Tau; Lane 4: IP’d GST-MSI2-tau) with Tau 13 (Pan-tau antibody) revealed the presence of tau proteins in the immunoprecipitated material as well. The inputs from the two reaction mixtures are also shown here (Lane 1: Tau + MSI1 input; Lane 3: Tau + MSI2 input). (d) Representative Western blot images of brain homogenates from AD (N = 4) and age-matched control cases (N = 4) demonstrating a significant increase in the levels of both MSI1 and MSI2 proteins ((p = 0.035, *; p = 0.005, **). (e) Representative images of both soluble and insoluble fractions of AD (N = 3) and age-matched control (N = 3) brain tissues obtained from filter trap assay. Soluble fractions from all the cases studied demonstrate increased levels of tau protein upon probing with Tau 13 antibody when compared to their insoluble fractions. Similarly, both MSI1 and MSI2 protein levels are increased in the soluble fractions compared to the insoluble fractions (p = 0.0279, *; p = 0.0045, **)CC BY · PubMed Central
Fig. 3 Musashi aggregates in AD (a) Representative Epifluorescence images of AD and control cortices immunolabeled with α-MSI1, DAPI (blue, for nuclei) (top) and α-Msi1 (green) and α-Oligomer antibody (F11G3, red) (bottom). An increased MSI1 oligomeric signal was noticed in the cytoplasm of AD brains cortices (white arrows) (b) The quantified fluorescence intensity, represented as bar graph demonstrates significantly elevated level of MSI1 signal in AD cortices compared to the controls (N = 3 sections per condition, p = 0.007, **). (c) α-Oligomer antibody (F11G3, red), α-MSI2 antibody (green) and DAPI (nuclei, blue) immunostaining revealed MSI2 oligomers, mostly in the cytoplasm of AD brains cortices (white arrows) (N = 3 sections per condition and magnification: 40X, scale bar: 10 μm). (d) The fluorescence intensity of MSI2, represented as bar graph reveal significantly elevated levels of MSI2 signal in AD cortex compared to the control (N = 3 sections per condition, p = 0.0001, ****)
Fig. 3 Musashi aggregates in AD (a) Representative Epifluorescence images of AD and control cortices immunolabeled with α-MSI1, DAPI (blue, for nuclei) (top) and α-Msi1 (green) and α-Oligomer antibody (F11G3, red) (bottom). An increased MSI1 oligomeric signal was noticed in the cytoplasm of AD brains cortices (white arrows) (b) The quantified fluorescence intensity, represented as bar graph demonstrates significantly elevated level of MSI1 signal in AD cortices compared to the controls (N = 3 sections per condition, p = 0.007, **). (c) α-Oligomer antibody (F11G3, red), α-MSI2 antibody (green) and DAPI (nuclei, blue) immunostaining revealed MSI2 oligomers, mostly in the cytoplasm of AD brains cortices (white arrows) (N = 3 sections per condition and magnification: 40X, scale bar: 10 μm). (d) The fluorescence intensity of MSI2, represented as bar graph reveal significantly elevated levels of MSI2 signal in AD cortex compared to the control (N = 3 sections per condition, p = 0.0001, ****)CC BY · PubMed Central
Fig. 4 Distinct patterns of MSI2 oligomers in AD brain (a) Representative confocal images of AD cortex stained with α-Oligomer antibody (F11G3, red), α-MSI2 antibody (green) and DAPI (blue) for nuclei (white scale bar: 5 μm, magnification: 63X). (b) Confocal orthogonal view of image (showed in A) showing the presence of MSI2 oligomers in the perinuclear area. (c) Co-localization pixel map between MSI2 (green) and oligomer (red) signals confirmed the overlapping of the two signals (grey area delimitated by green dashed line, white scale bar: 5 μm). (d) Confocal (Z-stacks) image demonstrated punctate MSI2 (inset 1) and more diffused distribution of its oligomers (inset 2) in two different cells (white scale bar: 5 μm). (e-1) Twice zoomed (inset 1) image showing a proximal localization of punctate MSI2 protein to the nucleus. (e-2) Twice zoomed (inset 2) image showing distant localization of MSI2 oligomers from the nucleus (the gap between nucleus and MSI2 oligomers is delimitated by green dashed line)
Fig. 4 Distinct patterns of MSI2 oligomers in AD brain (a) Representative confocal images of AD cortex stained with α-Oligomer antibody (F11G3, red), α-MSI2 antibody (green) and DAPI (blue) for nuclei (white scale bar: 5 μm, magnification: 63X). (b) Confocal orthogonal view of image (showed in A) showing the presence of MSI2 oligomers in the perinuclear area. (c) Co-localization pixel map between MSI2 (green) and oligomer (red) signals confirmed the overlapping of the two signals (grey area delimitated by green dashed line, white scale bar: 5 μm). (d) Confocal (Z-stacks) image demonstrated punctate MSI2 (inset 1) and more diffused distribution of its oligomers (inset 2) in two different cells (white scale bar: 5 μm). (e-1) Twice zoomed (inset 1) image showing a proximal localization of punctate MSI2 protein to the nucleus. (e-2) Twice zoomed (inset 2) image showing distant localization of MSI2 oligomers from the nucleus (the gap between nucleus and MSI2 oligomers is delimitated by green dashed line)CC BY · PubMed Central
Fig. 5 Neuronal MSI2 oligomers in AD Brain (a) Representative epifluorescence images of AD cortical section showing co-localization between α-MSI2 (red), NeuN (green) and α-Oligomer antibody (F11G3, blue) (white scale bar: 10 μm, magnification: 40X). (b) Twice zoomed image of ROI (green dashed line) highlighting localization of MSI2 oligomers in neurons (white scale bar: 5 μm, magnification 40X). (c) PCC of 5 ROIs in AD cortex section represented in bar graphs showing the levels of co-localization between MSI2 and F11G3 (PCC: 0.9768 ± 0.01763), MSI2 and NeuN (PCC: 0.7581 ± 0.1237) and F11G3 and NeuN (PCC: 0.8004 ± 0.1149) signals. (d) LUT Fire image of selected ROI between MSI2 and α-Oligomer antibody (F11G3) confirming the presence of MSI2 oligomers in neurons with heterogeneous distribution in the cytoplasm (color scale bar represents pixel intensity)
Fig. 5 Neuronal MSI2 oligomers in AD Brain (a) Representative epifluorescence images of AD cortical section showing co-localization between α-MSI2 (red), NeuN (green) and α-Oligomer antibody (F11G3, blue) (white scale bar: 10 μm, magnification: 40X). (b) Twice zoomed image of ROI (green dashed line) highlighting localization of MSI2 oligomers in neurons (white scale bar: 5 μm, magnification 40X). (c) PCC of 5 ROIs in AD cortex section represented in bar graphs showing the levels of co-localization between MSI2 and F11G3 (PCC: 0.9768 ± 0.01763), MSI2 and NeuN (PCC: 0.7581 ± 0.1237) and F11G3 and NeuN (PCC: 0.8004 ± 0.1149) signals. (d) LUT Fire image of selected ROI between MSI2 and α-Oligomer antibody (F11G3) confirming the presence of MSI2 oligomers in neurons with heterogeneous distribution in the cytoplasm (color scale bar represents pixel intensity)CC BY · PubMed Central
Fig. 6 Co-localization of MSI1 and MSI2 with tau in AD Brains (a) Representative epifluorescence image of AD cortex section stained with α-MSI1 and Pan-tau (Tau5) antibodies (white scale bar: 50 μm, magnification: 10X). (b) Representative epifluorescence image of AD cortex section stained with α-MSI2 and Pan-tau (Tau5) antibodies (white scale bar: 50 μm, magnification: 10X). (c) Inset 1: ten times zoomed image (green square in a) showed diffuse cytoplasmic co-localization of MSI1 and tau (white scale bar: 5 μm). Inset 2: ten times zoomed image (green square in c) showed cytoplasmic co-localization of MSI2 and tau (white scale bar: 5 μm). (d) PCC Graph represent colocalization coefficient between MSI1/Tau (PCC: 0.84 ± 0.07) and MSI2/Tau (PCC: 0.80 ± 0.06) in positive cells to both proteins showing high association in AD brain
Fig. 6 Co-localization of MSI1 and MSI2 with tau in AD Brains (a) Representative epifluorescence image of AD cortex section stained with α-MSI1 and Pan-tau (Tau5) antibodies (white scale bar: 50 μm, magnification: 10X). (b) Representative epifluorescence image of AD cortex section stained with α-MSI2 and Pan-tau (Tau5) antibodies (white scale bar: 50 μm, magnification: 10X). (c) Inset 1: ten times zoomed image (green square in a) showed diffuse cytoplasmic co-localization of MSI1 and tau (white scale bar: 5 μm). Inset 2: ten times zoomed image (green square in c) showed cytoplasmic co-localization of MSI2 and tau (white scale bar: 5 μm). (d) PCC Graph represent colocalization coefficient between MSI1/Tau (PCC: 0.84 ± 0.07) and MSI2/Tau (PCC: 0.80 ± 0.06) in positive cells to both proteins showing high association in AD brainCC BY · PubMed Central
Fig. 7 Co-localization of MSI1 and MSI2 with tau oligomers in AD Brain (a) Epifluorescence images of AD cortex section stained with α-MSI2 (red) and α-tau oligomeric antibody, T22 (green), DAPI (Nuclei, blue). Co-localization was observed in large portion of the tissue. Different distribution pattern was observed. Area positive to MSI1 spot distribution and negative signal of T22 (top graph) and strong co-localization was observed in same cells between MSI1 and T22 in the cytoplasm (bottom graph). The fluorescence intensity was measured and represented as intensity plot profile (DAPI, blue; MSI2, red and TauO, green). These signals have been observed in different sections of cortices (white scale bar: 10 μm magnification, 20X zoomed twice). (b) Epifluorescence images of AD cortex section stained with α-MSI2 (red) and α-tau oligomeric antibody, T22 (green). Different Co-localization grades were evaluated in 3 different ROIs (green squares) (white scale bar: 50 μm, magnification: 40X). Image 1 (MSI2+/TauO-), Image 2 (MSI2+/TauO+) and Image 3 (MSI2+/TauO+) showed different distribution patterns of MSI2 and tau oligomers (white scale bar: 20 μm, magnification: 40X). One ROI from each image (1–3) was selected and the fluorescence intensity was measured which is represented as intensity plot profile (DAPI, blue; MSI2, red and TauO, green)
Fig. 7 Co-localization of MSI1 and MSI2 with tau oligomers in AD Brain (a) Epifluorescence images of AD cortex section stained with α-MSI2 (red) and α-tau oligomeric antibody, T22 (green), DAPI (Nuclei, blue). Co-localization was observed in large portion of the tissue. Different distribution pattern was observed. Area positive to MSI1 spot distribution and negative signal of T22 (top graph) and strong co-localization was observed in same cells between MSI1 and T22 in the cytoplasm (bottom graph). The fluorescence intensity was measured and represented as intensity plot profile (DAPI, blue; MSI2, red and TauO, green). These signals have been observed in different sections of cortices (white scale bar: 10 μm magnification, 20X zoomed twice). (b) Epifluorescence images of AD cortex section stained with α-MSI2 (red) and α-tau oligomeric antibody, T22 (green). Different Co-localization grades were evaluated in 3 different ROIs (green squares) (white scale bar: 50 μm, magnification: 40X). Image 1 (MSI2+/TauO-), Image 2 (MSI2+/TauO+) and Image 3 (MSI2+/TauO+) showed different distribution patterns of MSI2 and tau oligomers (white scale bar: 20 μm, magnification: 40X). One ROI from each image (1–3) was selected and the fluorescence intensity was measured which is represented as intensity plot profile (DAPI, blue; MSI2, red and TauO, green)CC BY · PubMed Central
Fig. 8 Hypothetical model of Musashi protein aggregation and its interaction with tau oligomers in AD pathology. The dotted area (left) depicts nuclear-cytoplasmic shuttling of Musashi proteins and their localization in RNA granules based on the published literatures. Additionally, tau protein has also been reported to be involved in RNA granule trafficking. The area under solid line (right) depicts the observations made in this study. Musashi proteins co-localized with tau protein, as well as its oligomeric forms in the cytoplasm. In diseased state, these two proteins might be present in the stress granules. Moreover, mislocalization of tau protein in the nucleus and its subsequent interaction with Musashi proteins may lead to impaired functioning of Musashi proteins, thus resulting in its aggregation
Fig. 8 Hypothetical model of Musashi protein aggregation and its interaction with tau oligomers in AD pathology. The dotted area (left) depicts nuclear-cytoplasmic shuttling of Musashi proteins and their localization in RNA granules based on the published literatures. Additionally, tau protein has also been reported to be involved in RNA granule trafficking. The area under solid line (right) depicts the observations made in this study. Musashi proteins co-localized with tau protein, as well as its oligomeric forms in the cytoplasm. In diseased state, these two proteins might be present in the stress granules. Moreover, mislocalization of tau protein in the nucleus and its subsequent interaction with Musashi proteins may lead to impaired functioning of Musashi proteins, thus resulting in its aggregationCC BY · PubMed Central
Fig. 9 Analyses of Musashi proteins by PLAAC software to identify prion-like region. a MSI1 protein does not show the presence of prion-like domain analyzed by this algorithm, whereas (b) MSI2 protein reveals the occurrence of such domain, as indicated by the red line and residues in red
Fig. 9 Analyses of Musashi proteins by PLAAC software to identify prion-like region. a MSI1 protein does not show the presence of prion-like domain analyzed by this algorithm, whereas (b) MSI2 protein reveals the occurrence of such domain, as indicated by the red line and residues in redCC BY · PubMed Central

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Cited by

See all 44

Metadata

Authors
Sengupta, U., Montalbano, M., McAllen, S., Minuesa, G., Kharas, M., & Kayed, R.
Venue
Acta Neuropathologica Communications
Publisher
Springer Science and Business Media LLC
Published
2018-10-26
Volume
6
Issue
1
ISSN
2051-5960
DOI
10.1186/s40478-018-0615-0
PMC
PMC6203984
Cited by
44
References
4
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (tdm)
Funders
Foundation for the National Institutes of Health (AG054025, NS094557, AG055771)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.