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Actual fusion efficiency in the lipid mixing assay - Comparison between nanodiscs and liposomes

Claire François-Martin
Frédéric Pincet
ResearchOpen Access07 Mar 2017
Scientific Reports

Volume: 7, P: 1-8
Freezing and piercing of in vitro asymmetric plasma membrane by α-synuclein

Heo and Pincet demonstrate the influence of α-synuclein aggregation on in vitro asymmetric membranes using a microfluidic setup. They show that synuclein aggregation on the asymmetric membranes leads to its thinning and formation of pores of discrete sizes and synuclein insertion immobilizes both the leaflets of the asymmetric membrane.

Paul Heo
Frederic Pincet
ResearchOpen Access31 Mar 2020
Communications Biology

Volume: 3, P: 1-8
Two successive oligomeric Munc13 assemblies scaffold vesicle docking and SNARE assembly to support neurotransmitter release

The presynaptic protein Munc13 forms nanoclusters at synaptic release sites, but its internal organization is unclear. Here, the authors show that two distinct ordered Munc13 oligomers couple synaptic vesicle docking and SNARE assembly to regulate neurotransmission

Manindra Bera
Kirill Grushin
Jeremy S. Dittman
ResearchOpen Access05 Aug 2025
Nature Communications

Volume: 16, P: 1-18
Biomimetic membrane in a microfluidic chip for the electrical and optical monitoring of biological reactions

This protocol describes a suspended asymmetric fluid membrane. Two membrane leaflets form from different liposomes and remain accessible through microfluidic channels. Chemical and molecular reactions can be monitored optically and electrically.

Delphine Mion
Louis Bunel
Frédéric Pincet
Protocols03 Jun 2025
Nature Protocols

Volume: 20, P: 3477-3508
Direct determination of oligomeric organization of integral membrane proteins and lipids from intact customizable bilayer

Editor summary: A native-mass-spectrometry-based approach analyzes integral membrane protein–lipid complexes directly from near-physiological membrane conditions, providing information about protein oligomeric states, lipid identities, and membrane properties.

Aniruddha Panda
Fabian Giska
Kallol Gupta
Research27 Apr 2023
Nature Methods

Volume: 20, P: 891-897
Author Correction: Kinetic study of membrane protein interactions: from three to two dimensions

Vladimir Adrien
Myriam Reffay
Wladimir Urbach
Amendments and CorrectionsOpen Access08 Apr 2024
Scientific Reports

Volume: 14, P: 1
Placing and shaping liposomes with reconfigurable DNA nanocages

Controlling liposome shape, arrangement and dynamics is important for biophysical studies and synthetic biology applications. Now, using a family of reconfigurable DNA nanocages as templates, spherical, tubular, toroidal and helical liposomes with predefined geometry have been produced. DNA-guided membrane fusion and bending is also demonstrated.

Zhao Zhang
Yang Yang
Chenxiang Lin
Research23 Jun 2017
Nature Chemistry

Volume: 9, P: 653-659
Complexin cross-links prefusion SNAREs into a zigzag array

Structural studies of complexin bound to a mimetic of a prefusion SNARE complex provide insight into how complexin 'clamps' SNARE complex assembly, thereby inhibiting membrane fusion. While the central helix of complexin is anchored to a SNARE complex, its accessory helix extends away and bridges to a second SNARE complex, generating a zigzag array incompatible with fusion.

Daniel Kümmel
Shyam S Krishnakumar
Karin M Reinisch
Research24 Jul 2011
Nature Structural & Molecular Biology

Volume: 18, P: 927-933
A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion

Comparison of the prefusion and postfusion structures of complexin associated with SNAREs reveals a conformational switch in complexin, which is triggered by the zippering of three key Asp residues in the “switch” region of v-SNAREs into t-SNAREs. This causes complexin to move its accessory helix, thereby releasing the clamped state. This switch is triggered when the calcium sensor synaptotagmin binds calcium ions.

Shyam S Krishnakumar
Daniel T Radoff
James E Rothman
Research24 Jul 2011
Nature Structural & Molecular Biology

Volume: 18, P: 934-940
Energetics and dynamics of SNAREpin folding across lipid bilayers

Feng Li
Frédéric Pincet
David Tareste
Research30 Sept 2007
Nature Structural & Molecular Biology

Volume: 14, P: 890-896
Complexin activates and clamps SNAREpins by a common mechanism involving an intermediate energetic state

The SNARE-binding protein complexin (CPX) can both facilitate and inhibit membrane fusion, which has been puzzling. Using the Surface Forces Apparatus (SFA) system to obtain distance and interaction measurements of SNARE complexes assembling between bilayers demonstrates that CPX stabilizes an intermediate energetic state in which the SNAREpins are half-zippered, explaining activation and inhibition as the dual consequences of this single mechanism of action.

Feng Li
Frédéric Pincet
James E Rothman
Research24 Jul 2011
Nature Structural & Molecular Biology

Volume: 18, P: 941-946
Lithium fine tunes lipid membranes through phospholipid binding

Louis Bunel
Vladimir Adrien
Frédéric Pincet
ResearchOpen Access17 Apr 2025
Scientific Reports

Volume: 15, P: 1-12
Highly stable planar asymmetric suspended membranes for investigating protein dynamics and membrane fusion

Membrane fusion is a complex biological process. In this protocol, asymmetric membranes derived from cultured cells or prepared synthetically, are suspended across micrometer -sized holes on a silicon chip to allow proteins to move freely in the bilayer.

Manindra Bera
Ramalingam Venkat Kalyana Sundaram
Sathish Ramakrishnan
Protocols03 Jun 2025
Nature Protocols

Volume: 20, P: 3582-3606
Control of plasma membrane lipid homeostasis by the extended synaptotagmins

Saheki and colleagues show that extended synaptotagmins (E-Syts), ER proteins that function as tethers to the plasma membrane, can transfer lipids between bilayers in a Ca²⁺- and SMP-domain-dependent manner, thus regulating plasma membrane lipid homeostasis.

Yasunori Saheki
Xin Bian
Pietro De Camilli
Research11 Apr 2016
Nature Cell Biology

Volume: 18, P: 504-515
Quantitative single-molecule analysis of assembly and Ca²⁺-dependent disassembly of synaptotagmin oligomers on lipid bilayers

The kinetics of assembly and Ca²⁺-dependent disassembly of Syt-1 oligomers, determined by quantitative single molecule analysis, meet or exceed the physiologic requirements to function as a clamp.

Feng Li
Jeff Coleman
Frédéric Pincet
ResearchOpen Access03 Dec 2024
Communications Biology

Volume: 7, P: 1-14
Kinetic study of membrane protein interactions: from three to two dimensions

Vladimir Adrien
Myriam Reffay
Wladimir Urbach
ResearchOpen Access09 Jan 2024
Scientific Reports

Volume: 14, P: 1-10
Synaptotagmin-1 membrane binding is driven by the C2B domain and assisted cooperatively by the C2A domain

Clémence Gruget
Oscar Bello
Stephen H. Donaldson Jr
ResearchOpen Access22 Oct 2020
Scientific Reports

Volume: 10, P: 1-10
Preparation and characterization of SNARE-containing nanodiscs and direct study of cargo release through fusion pores

Lei Shi
Kevin Howan
Frédéric Pincet
Protocols18 Apr 2013
Nature Protocols

Volume: 8, P: 935-948
CX3CL1 homo-oligomerization drives cell-to-cell adherence

Mariano A. Ostuni
Patricia Hermand
Philippe Deterre
ResearchOpen Access03 Jun 2020
Scientific Reports

Volume: 10, P: 1-16

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