Geometry of membrane fission

Frolov, Vadim A.; Escalada, Artur; Akimov, Sergey A.; Shnyrova, Anna V.

doi:10.1016/j.chemphyslip.2014.07.006

Cited by 42 publications

(56 citation statements)

References 139 publications

(258 reference statements)

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“…Membrane fission is a process that involves a splitting of one membrane-enclosed compartment into two. This process usually evolves through three steps: membrane neck formation, hemifission and formation of two separate membranes [252][253][254][255][256][257][258][259]. During membrane fission, initially saddle-shaped membrane neck forms: both monolayers remain continuous, but aqueous volume consists of two parts connected by a narrow 'capillary'.…”

Section: Box 2 Membrane Rearrangements: Fissionmentioning

confidence: 99%

Phosphatidic acid in membrane rearrangements

et al. 2019

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Phosphatidic acid (PA) is the simplest cellular glycerophospholipid characterized by unique biophysical properties: a small headgroup; negative charge; and a phosphomonoester group. Upon interaction with lysine or arginine, PA charge increases from −1 to −2 and this change stabilizes protein–lipid interactions. The biochemical properties of PA also allow interactions with lipids in several subcellular compartments. Based on this feature, PA is involved in the regulation and amplification of many cellular signalling pathways and functions, as well as in membrane rearrangements. Thereby, PA can influence membrane fusion and fission through four main mechanisms: it is a substrate for enzymes producing lipids (lysophosphatidic acid and diacylglycerol) that are involved in fission or fusion; it contributes to membrane rearrangements by generating negative membrane curvature; it interacts with proteins required for membrane fusion and fission; and it activates enzymes whose products are involved in membrane rearrangements. Here, we discuss the biophysical properties of PA in the context of the above four roles of PA in membrane fusion and fission.

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Section: Box 2 Membrane Rearrangements: Fissionmentioning

confidence: 99%

Phosphatidic acid in membrane rearrangements

et al. 2019

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“…1) (18). This is rather intriguing because the existing model of membrane scission requires lipids to come in close proximity and pass through a hemifission state before scission to avoid any leak during the topological transition (20)(21)(22)(23). How then does a shallow invagination directly transform into a detached vesicle?…”

Section: Bar Proteinsmentioning

confidence: 99%

Endocytic proteins drive vesicle growth via instability in high membrane tension environment

Walani

Torres

Agrawal

2015

Proc. Natl. Acad. Sci. U.S.A.

152

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Clathrin-mediated endocytosis (CME) is a key pathway for transporting cargo into cells via membrane vesicles; it plays an integral role in nutrient import, signal transduction, neurotransmission, and cellular entry of pathogens and drug-carrying nanoparticles. Because CME entails substantial local remodeling of the plasma membrane, the presence of membrane tension offers resistance to bending and hence, vesicle formation. Experiments show that in such high-tension conditions, actin dynamics is required to carry out CME successfully. In this study, we build on these pioneering experimental studies to provide fundamental mechanistic insights into the roles of two key endocytic proteins-namely, actin and BAR proteins-in driving vesicle formation in high membrane tension environment. Our study reveals an actin force-induced "snapthrough instability" that triggers a rapid shape transition from a shallow invagination to a highly invaginated tubular structure. We show that the association of BAR proteins stabilizes vesicles and induces a milder instability. In addition, we present a rather counterintuitive role of BAR depolymerization in regulating the shape evolution of vesicles. We show that the dissociation of BAR proteins, supported by actin-BAR synergy, leads to considerable elongation and squeezing of vesicles. Going beyond the membrane geometry, we put forth a stress-based perspective for the onset of vesicle scission and predict the shapes and composition of detached vesicles. We present the snap-through transition and the high in-plane stress as possible explanations for the intriguing direct transformation of broad and shallow invaginations into detached vesicles in BAR mutant yeast cells.clathrin-mediated endocytosis | membrane tension | instability | actin | BAR proteins

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“…These conditions depend on the microscopic details of the dynamin‐membrane interaction and the nature of dynamin's conformational change. Dynamin binds to the membrane via its pleckstrin homology (PH) domain, which has a small hydrophobic loop that inserts into the membrane, sometimes characterized as a wedge . It is possible (though, perhaps unlikely, given that the loop is only a few amino acids long) that this insertion of the PH domain into the bilayer disrupts the bilayer's integrity, allowing the creation of a kink.…”

Section: Theoretical Modelmentioning

confidence: 99%

Dynamin's helical geometry does not destabilize membranes during fission

McDargh

Deserno

2018

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It is now widely accepted that dynamin-mediated fission is a fundamentally mechanical process: dynamin undergoes a GTP-dependent conformational change, constricting the neck between two compartments, somehow inducing their fission. However, the exact connection between dynamin's conformational change and the scission of the neck is still unclear. In this paper, we re-evaluate the suggestion that a change in the pitch or radius of dynamin's helical geometry drives the lipid bilayer through a mechanical instability, similar to a well-known phenomenon occurring in soap films. We find that, contrary to previous claims, there is no such instability. This lends credence to an alternative model, in which dynamin drives the membrane up an energy barrier, allowing thermal fluctuations to take it into the hemifission state.

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Geometry of membrane fission

Cited by 42 publications

References 139 publications

Phosphatidic acid in membrane rearrangements

Phosphatidic acid in membrane rearrangements

Endocytic proteins drive vesicle growth via instability in high membrane tension environment

Dynamin's helical geometry does not destabilize membranes during fission

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