Membrane-mediated interaction between strongly anisotropic protein scaffolds.
Specialized proteins serve as scaffolds sculpting strongly curved membranes of intracellular organelles. Effective membrane shaping requires segregation of these proteins into domains and is, therefore, critically dependent on the protein-protein interaction. Interactions mediated by membrane elasti...
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Public Library of Science (PLoS)
2015-02-01
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| Series: | PLoS Computational Biology |
| Online Access: | https://journals.plos.org/ploscompbiol/article/file?id=10.1371/journal.pcbi.1004054&type=printable |
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| author | Yonatan Schweitzer Michael M Kozlov |
| author_facet | Yonatan Schweitzer Michael M Kozlov |
| author_sort | Yonatan Schweitzer |
| collection | DOAJ |
| description | Specialized proteins serve as scaffolds sculpting strongly curved membranes of intracellular organelles. Effective membrane shaping requires segregation of these proteins into domains and is, therefore, critically dependent on the protein-protein interaction. Interactions mediated by membrane elastic deformations have been extensively analyzed within approximations of large inter-protein distances, small extents of the protein-mediated membrane bending and small deviations of the protein shapes from isotropic spherical segments. At the same time, important classes of the realistic membrane-shaping proteins have strongly elongated shapes with large and highly anisotropic curvature. Here we investigated, computationally, the membrane mediated interaction between proteins or protein oligomers representing membrane scaffolds with strongly anisotropic curvature, and addressed, quantitatively, a specific case of the scaffold geometrical parameters characterizing BAR domains, which are crucial for membrane shaping in endocytosis. In addition to the previously analyzed contributions to the interaction, we considered a repulsive force stemming from the entropy of the scaffold orientation. We computed this interaction to be of the same order of magnitude as the well-known attractive force related to the entropy of membrane undulations. We demonstrated the scaffold shape anisotropy to cause a mutual aligning of the scaffolds and to generate a strong attractive interaction bringing the scaffolds close to each other to equilibrium distances much smaller than the scaffold size. We computed the energy of interaction between scaffolds of a realistic geometry to constitute tens of kBT, which guarantees a robust segregation of the scaffolds into domains. |
| format | Article |
| id | doaj-art-0e40df4e310c4e4ca2fb4fca59388218 |
| institution | OA Journals |
| issn | 1553-734X 1553-7358 |
| language | English |
| publishDate | 2015-02-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Computational Biology |
| spelling | doaj-art-0e40df4e310c4e4ca2fb4fca593882182025-08-20T02:15:15ZengPublic Library of Science (PLoS)PLoS Computational Biology1553-734X1553-73582015-02-01112e100405410.1371/journal.pcbi.1004054Membrane-mediated interaction between strongly anisotropic protein scaffolds.Yonatan SchweitzerMichael M KozlovSpecialized proteins serve as scaffolds sculpting strongly curved membranes of intracellular organelles. Effective membrane shaping requires segregation of these proteins into domains and is, therefore, critically dependent on the protein-protein interaction. Interactions mediated by membrane elastic deformations have been extensively analyzed within approximations of large inter-protein distances, small extents of the protein-mediated membrane bending and small deviations of the protein shapes from isotropic spherical segments. At the same time, important classes of the realistic membrane-shaping proteins have strongly elongated shapes with large and highly anisotropic curvature. Here we investigated, computationally, the membrane mediated interaction between proteins or protein oligomers representing membrane scaffolds with strongly anisotropic curvature, and addressed, quantitatively, a specific case of the scaffold geometrical parameters characterizing BAR domains, which are crucial for membrane shaping in endocytosis. In addition to the previously analyzed contributions to the interaction, we considered a repulsive force stemming from the entropy of the scaffold orientation. We computed this interaction to be of the same order of magnitude as the well-known attractive force related to the entropy of membrane undulations. We demonstrated the scaffold shape anisotropy to cause a mutual aligning of the scaffolds and to generate a strong attractive interaction bringing the scaffolds close to each other to equilibrium distances much smaller than the scaffold size. We computed the energy of interaction between scaffolds of a realistic geometry to constitute tens of kBT, which guarantees a robust segregation of the scaffolds into domains.https://journals.plos.org/ploscompbiol/article/file?id=10.1371/journal.pcbi.1004054&type=printable |
| spellingShingle | Yonatan Schweitzer Michael M Kozlov Membrane-mediated interaction between strongly anisotropic protein scaffolds. PLoS Computational Biology |
| title | Membrane-mediated interaction between strongly anisotropic protein scaffolds. |
| title_full | Membrane-mediated interaction between strongly anisotropic protein scaffolds. |
| title_fullStr | Membrane-mediated interaction between strongly anisotropic protein scaffolds. |
| title_full_unstemmed | Membrane-mediated interaction between strongly anisotropic protein scaffolds. |
| title_short | Membrane-mediated interaction between strongly anisotropic protein scaffolds. |
| title_sort | membrane mediated interaction between strongly anisotropic protein scaffolds |
| url | https://journals.plos.org/ploscompbiol/article/file?id=10.1371/journal.pcbi.1004054&type=printable |
| work_keys_str_mv | AT yonatanschweitzer membranemediatedinteractionbetweenstronglyanisotropicproteinscaffolds AT michaelmkozlov membranemediatedinteractionbetweenstronglyanisotropicproteinscaffolds |