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The ESCRT-III isofo...
The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization
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- Alqabandi, Maryam (författare)
- Laboratoire Physico Chimie Curie, Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Paris, France
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- de Franceschi, Nicola (författare)
- Laboratoire Physico Chimie Curie, Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Paris, France
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- Maity, Sourav (författare)
- Moleculaire Biofysica, Zernike Instituut, Rijksuniversiteit Groningen, Nijenborgh 4, Groningen, Netherlands
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- Miguet, Nolwenn (författare)
- Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), Grenoble, France
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- Bally, Marta (författare)
- Umeå universitet,Institutionen för klinisk mikrobiologi,Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM)
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- Roos, Wouter H. (författare)
- Moleculaire Biofysica, Zernike Instituut, Rijksuniversiteit Groningen, Nijenborgh 4, Groningen, Netherlands
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- Weissenhorn, Winfried (författare)
- Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), Grenoble, France
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- Bassereau, Patricia (författare)
- Laboratoire Physico Chimie Curie, Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Paris, France
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- Mangenot, Stéphanie (författare)
- Laboratoire Physico Chimie Curie, Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Paris, France
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(creator_code:org_t)
- 2021-04-08
- 2021
- Engelska.
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Ingår i: BMC Biology. - : BioMed Central. - 1741-7007. ; 19:1
- Relaterad länk:
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https://doi.org/10.1...
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https://umu.diva-por... (primary) (Raw object)
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https://bmcbiol.biom...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Background: ESCRT-III proteins are involved in many membrane remodeling processes including multivesicular body biogenesis as first discovered in yeast. In humans, ESCRT-III CHMP2 exists as two isoforms, CHMP2A and CHMP2B, but their physical characteristics have not been compared yet.Results: Here, we use a combination of techniques on biomimetic systems and purified proteins to study their affinity and effects on membranes. We establish that CHMP2B binding is enhanced in the presence of PI(4,5)P2 lipids. In contrast, CHMP2A does not display lipid specificity and requires CHMP3 for binding significantly to membranes. On the micrometer scale and at moderate bulk concentrations, CHMP2B forms a reticular structure on membranes whereas CHMP2A (+CHMP3) binds homogeneously. Thus, CHMP2A and CHMP2B unexpectedly induce different mechanical effects to membranes: CHMP2B strongly rigidifies them while CHMP2A (+CHMP3) has no significant effect.Conclusions: We therefore conclude that CHMP2B and CHMP2A exhibit different mechanical properties and might thus contribute differently to the diverse ESCRT-III-catalyzed membrane remodeling processes.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Neurologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Neurology (hsv//eng)
Nyckelord
- Atomic force microscopy (AFM)
- Bottom up approach
- Endosomal sorting complexes Required for Transport (ESCRT)
- Giant unilamellar vesicles (GUV)
- Lipid-protein interactions
- Mechanical properties
- Membrane
- Micropipette
- Reconstituted system
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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