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Cited by 430

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

Mechanisms of Membrane Curvature Sensing

Antonny, Bruno·2011·Annual Review of Biochemistry

Abstract

Bacteria and eukaryotic cells contain geometry-sensing tools in their cytosol: protein motifs or domains that recognize the curvature, concave or convex, deep or shallow, of lipid membranes. These sensors contrast with classical lipid-binding domains by their extended structure and, sometimes, counterintuitive chemistry. Among the sensors are long amphipathic helices, such as the ALPS motif and the N-terminal region of α-synuclein, whose apparent “design defects” translate into a remarkable ability to specifically adsorb to the surface of small vesicles. Fundamental differences in the lipid composition of membranes of the early and late secretory pathways probably explain why some sensors use mostly electrostatics whereas others take advantage of the hydrophobic effect. Membrane curvature sensors help to organize very diverse reactions, such as lipid transfer between membranes, the tethering of vesicles at the Golgi apparatus, and the assembly-disassembly cycle of protein coats.

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Metadata

Authors
Antonny, B.
Venue
Annual Review of Biochemistry
Published
2011-07-07
Volume
80
Issue
1
Pages
101-123
ISSN
  • 0066-4154 (ISSN-L)
  • 1545-4509
OpenAlex
W2127234404
Cited by
430
References
7
FWCI
2.16
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Mechanisms of Membrane Curvature Sensing. https://app.cochat.ai/papers/10.1146/annurev-biochem-052809-155121
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Antonny, B. (2011). Mechanisms of Membrane Curvature Sensing. Annual Review of Biochemistry. https://doi.org/10.1146/annurev-biochem-052809-155121

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