Single-molecule turnover dynamics of actin and membrane coat proteins in clathrin-mediated endocytosis

Lacy, Michael M.; Baddeley, David; Berro, Julien

doi:10.1101/617746

Cited by 5 publications

(4 citation statements)

References 68 publications

(118 reference statements)

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“…The residence times of peripheral proteins vary depending on their function, and for example the residence time of a bacterial phospholipase C on small unilamellar vesicles was estimated to 379 ± 49 ms, in agreement with earlier estimations for a highly related PLC [13] or for human phospholipase Cγ2 [14]. The turnover rates for membrane-associated proteins in clathrin-mediated endocytosis have been estimated to a few seconds [15]. Accordingly, PMPs bind membrane through different mechanisms.…”

Section: Introductionsupporting

confidence: 85%

Membrane models for molecular simulations of peripheral membrane proteins

Moqadam

Tubiana

Moutoussamy

et al. 2021

Advances in Physics: X

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Peripheral membrane proteins (PMPs) bind temporarily to the surface of biological membranes. They also exist in a soluble form and their tertiary structure is often known. Yet, their membrane-bound form and their interfacial-binding site with membrane lipids remain difficult to observe directly. Their binding and unbinding mechanism, the conformational changes of the PMPs and their influence on the membrane structure are notoriously challenging to study experimentally. Molecular dynamics simulations are particularly useful to fill some knowledge-gaps and provide hypothesis that can be experimentally challenged to further our understanding of PMP-membrane recognition. Because of the timescales of PMP-membrane binding events and the computational costs associated with molecular dynamics simulations, membrane models at different levels of resolution are used and often combined in multiscale simulation strategies. We here review membrane models belonging to three classes: atomistic, coarse-grained and implicit. Differences between models are rooted in the underlying theories and the reference data they are parameterized against. The choice of membrane model should therefore not only be guided by its computational efficiency. The range of applications of each model is discussed and illustrated using examples from the literature.

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Section: Introductionsupporting

confidence: 85%

Membrane models for molecular simulations of peripheral membrane proteins

Moqadam

Tubiana

Moutoussamy

et al. 2021

Advances in Physics: X

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“…The mechanism of severing and annealing modeled in this work could represent a general feature of actin dendritic networks, including yeast cells where short actin speckle lifetimes have been observed in actin patches of fission yeast (Lacy et al, 2019). It might provide an energetically efficient mechanism for network remodeling matching different mechanical requirements: close to the leading edge, short branched networks would provide rigidity to compressive stresses (resulting from actin polymerization against the membrane) while longer filaments at the back might be better suited for extensional stresses through myosin motors.…”

Section: Discussionmentioning

confidence: 99%

A mechanism with severing near barbed ends and annealing explains structure and dynamics of dendritic actin networks

Holz

Usukura

et al. 2021

Preprint

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Single molecule imaging has shown that part of actin disassembles within a few seconds after incorporation into the dendritic filament network in lamellipodia, suggestive of frequent destabilization near barbed ends. To investigate the mechanisms behind network remodeling, we created a stochastic model with polymerization, depolymerization, branching, capping, uncapping, severing, oligomer diffusion, annealing, and debranching. We find that filament severing, enhanced near barbed ends, can explain the single molecule actin lifetime distribution, if oligomer fragments reanneal to free ends with rate constants comparable to in vitro measurements. The same mechanism leads to actin networks consistent with measured filament, end, and branch concentrations. These networks undergo structural remodeling, leading to longer filaments away from the leading edge, at the +/- 35$^o$ orientation pattern. Imaging of actin speckle lifetimes at sub-second resolution verifies frequent disassembly of newly-assembled actin. We thus propose a unified mechanism that fits a diverse set of basic lamellipodia phenomenology.

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“…Initiation of a clathrin complex requires the accumulation of phosphatidylinositol‑4,5–bisphosphate (PIP2) and adapter proteins such as AP-2 at the pinching site [31] , [32] . After the coat is assembled, the actin filament network polymerizes at the endocytosis site to form an actin module [33] .…”

Section: Endocytosis Mechanisms For Nanomaterialsmentioning

confidence: 99%