Membrane to cytosol redistribution of αII-spectrin drives extracellular vesicle biogenesis in malignant breast cells.
- Publisher:
- Wiley
- Publication Type:
- Journal Article
- Citation:
- Proteomics, 2021, 21, (13-14), pp. 1-13
- Issue Date:
- 2021-07
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Proteomics - 2021 - Taylor - Membrane to cytosol redistribution of II%u2010spectrin drives extracellular vesicle biogenesis in.pdf | 10.49 MB | Adobe PDF |
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Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Taylor, J | |
dc.contributor.author | Patio, K | |
dc.contributor.author |
De Rubis, G https://orcid.org/0000-0001-7088-396X |
|
dc.contributor.author | Morris, MB | |
dc.contributor.author |
Evenhuis, C https://orcid.org/0000-0001-9903-7716 |
|
dc.contributor.author | Johnson, M | |
dc.contributor.author |
Bebawy, M https://orcid.org/0000-0003-2606-921X |
|
dc.date.accessioned | 2022-01-05T03:41:35Z | |
dc.date.available | 2021-03-22 | |
dc.date.available | 2022-01-05T03:41:35Z | |
dc.date.issued | 2021-07 | |
dc.identifier.citation | Proteomics, 2021, 21, (13-14), pp. 1-13 | |
dc.identifier.issn | 1615-9853 | |
dc.identifier.issn | 1615-9861 | |
dc.identifier.uri | http://hdl.handle.net/10453/152689 | |
dc.description.abstract | Spectrin is a ubiquitous cytoskeletal protein that provides structural stability and supports membrane integrity. In erythrocytes, spectrin proteolysis leads to the biogenesis of plasma membrane extracellular vesicles (EVs). However, its role in non-erythroid or cancer-derived plasma membrane EVs biogenesis is unknown. This study aims to examine the role of αII-spectrin in malignant and non-malignant plasma membrane vesiculation. We developed a custom, automated cell segmentation plugin for the image processor, Fiji, that provides an unbiased assessment of high resolution confocal microscopy images of the subcellular distribution of αII-spectrin. We show that, in low vesiculating non-malignant MBE-F breast cells, prominent cortical spectrin localises to the cell periphery at rest. In comparison, cortical spectrin is diminished in high vesiculating malignant MCF-7 breast cells at rest. A cortical distribution of spectrin correlates with increased biomechanical stiffness as measured by Atomic Force Microscopy. Furthermore, cortical spectrin can be induced in malignant MCF-7 cells by treatment with known vesiculation modulators including the calcium chelator, BAPTA-AM or the calpain inhibitor II (ALLM). These results demonstrate that the subcellular localisation of spectrin is distinctly different in malignant and non-malignant cells at rest and shows that the redistribution of cortical αII-spectrin to the cytoplasm supports plasma membrane-derived EV biogenesis in malignant cells. | |
dc.format | Print-Electronic | |
dc.language | eng | |
dc.publisher | Wiley | |
dc.relation.ispartof | Proteomics | |
dc.relation.isbasedon | 10.1002/pmic.202000091 | |
dc.rights | info:eu-repo/semantics/closedAccess | |
dc.subject | 06 Biological Sciences, 08 Information and Computing Sciences, 11 Medical and Health Sciences | |
dc.subject.classification | Biochemistry & Molecular Biology | |
dc.subject.mesh | Actin Cytoskeleton | |
dc.subject.mesh | Calpain | |
dc.subject.mesh | Cytosol | |
dc.subject.mesh | Extracellular Vesicles | |
dc.subject.mesh | Spectrin | |
dc.subject.mesh | Cytosol | |
dc.subject.mesh | Calpain | |
dc.subject.mesh | Spectrin | |
dc.subject.mesh | Actin Cytoskeleton | |
dc.subject.mesh | Extracellular Vesicles | |
dc.subject.mesh | Actin Cytoskeleton | |
dc.subject.mesh | Calpain | |
dc.subject.mesh | Cytosol | |
dc.subject.mesh | Extracellular Vesicles | |
dc.subject.mesh | Spectrin | |
dc.title | Membrane to cytosol redistribution of αII-spectrin drives extracellular vesicle biogenesis in malignant breast cells. | |
dc.type | Journal Article | |
utslib.citation.volume | 21 | |
utslib.location.activity | Germany | |
utslib.for | 06 Biological Sciences | |
utslib.for | 08 Information and Computing Sciences | |
utslib.for | 11 Medical and Health Sciences | |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Health | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Strength - CHT - Health Technologies | |
pubs.organisational-group | /University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science/School of Life Sciences | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Health/Graduate School of Health | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Health/Graduate School of Health/GSH.Pharmacy | |
pubs.organisational-group | /University of Technology Sydney/Centre for Health Technologies (CHT) | |
utslib.copyright.status | closed_access | * |
pubs.consider-herdc | false | |
dc.date.updated | 2022-01-05T03:41:30Z | |
pubs.issue | 13-14 | |
pubs.publication-status | Published | |
pubs.volume | 21 | |
utslib.citation.issue | 13-14 |
Abstract:
Spectrin is a ubiquitous cytoskeletal protein that provides structural stability and supports membrane integrity. In erythrocytes, spectrin proteolysis leads to the biogenesis of plasma membrane extracellular vesicles (EVs). However, its role in non-erythroid or cancer-derived plasma membrane EVs biogenesis is unknown. This study aims to examine the role of αII-spectrin in malignant and non-malignant plasma membrane vesiculation. We developed a custom, automated cell segmentation plugin for the image processor, Fiji, that provides an unbiased assessment of high resolution confocal microscopy images of the subcellular distribution of αII-spectrin. We show that, in low vesiculating non-malignant MBE-F breast cells, prominent cortical spectrin localises to the cell periphery at rest. In comparison, cortical spectrin is diminished in high vesiculating malignant MCF-7 breast cells at rest. A cortical distribution of spectrin correlates with increased biomechanical stiffness as measured by Atomic Force Microscopy. Furthermore, cortical spectrin can be induced in malignant MCF-7 cells by treatment with known vesiculation modulators including the calcium chelator, BAPTA-AM or the calpain inhibitor II (ALLM). These results demonstrate that the subcellular localisation of spectrin is distinctly different in malignant and non-malignant cells at rest and shows that the redistribution of cortical αII-spectrin to the cytoplasm supports plasma membrane-derived EV biogenesis in malignant cells.
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