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TitleStructural insights into the cooperative remodeling of membranes by amphiphysin/BIN1.
Journal, issue, pagesSci Rep, Vol. 5, Page 15452, Year 2015
Publish dateOct 21, 2015
AuthorsJulia Adam / Nirakar Basnet / Naoko Mizuno /
PubMed AbstractAmphiphysin2/BIN1 is a crescent-shaped N-BAR protein playing a key role in forming deeply invaginated tubes in muscle T-tubules. Amphiphysin2/BIN1 structurally stabilizes tubular formations in ...Amphiphysin2/BIN1 is a crescent-shaped N-BAR protein playing a key role in forming deeply invaginated tubes in muscle T-tubules. Amphiphysin2/BIN1 structurally stabilizes tubular formations in contrast to other N-BAR proteins involved in dynamic membrane scission processes; however, the molecular mechanism of the stabilizing effect is poorly understood. Using cryo-EM, we investigated the assembly of the amphiphysin/BIN1 on a membrane tube. We found that the N-BAR domains self-assemble on the membrane surface in a highly cooperative manner. Our biochemical assays and 3D reconstructions indicate that the N-terminal amphipathic helix H0 plays an important role in the initiation of the tube assembly and further in organizing BAR-mediated polymerization by locking adjacent N-BAR domains. Mutants that lack H0 or the tip portion, which is also involved in interactions of the neighboring BAR unit, lead to a disruption of the polymer organization, even though tubulation can still be observed. The regulatory region of amphiphysin/BIN1 including an SH3 domain does not have any apparent involvement in the polymer lattice. Our study indicates that the H0 helix and the BAR tip are necessary for efficient and organized self-assembly of amphiphysin/N-BAR.
External linksSci Rep / PubMed:26487375 / PubMed Central
MethodsEM (helical sym.)
Resolution10.3 - 12.1 Å
Structure data

EMDB-3192:
Helical reconstruction of amphiphysin N-BAR with a membrane tube radius of 140 Angstrom by cryo-electron microscopy
Method: EM (helical sym.) / Resolution: 10.3 Å

EMDB-3193:
Helical reconstruction of amphiphysin N-BAR with a membrane tube radius of 156 Angstrom by cryo-electron microscopy
Method: EM (helical sym.) / Resolution: 11.2 Å

EMDB-3194:
Helical reconstruction of amphiphysin N-BAR with a membrane tube radius of 131 Angstrom by cryo-electron microscopy
Method: EM (helical sym.) / Resolution: 10.9 Å

EMDB-3195:
Helical reconstruction of amphiphysin N-BAR with a membrane tube radius of 125 Angstrom by cryo-electron microscopy
Method: EM (helical sym.) / Resolution: 10.9 Å

EMDB-3196:
Helical reconstruction of amphiphysin N-BAR with a membrane tube radius of 121 Angstrom by cryo-electron microscopy
Method: EM (helical sym.) / Resolution: 12.1 Å

Source
  • Drosophila melanogaster (fruit fly)

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