VASP localization to lipid bilayers induces polymerization driven actin bundle formation

Nast-Kolb, Timon; Bleicher, Philip; Payr, Marco; Bausch, Andreas R.

doi:10.1091/mbc.e21-11-0577

Cited by 6 publications

(7 citation statements)

References 67 publications

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“…A consequence of this is the depletion of EDP from the LPD-VASP condensate, initiating the rapid polymerization of actin around the bud. We suspect that VASP’s enhanced polymerization efficacy when clustered 12,81 could also play a supportive role in the formation of actin rings at the base of the bud. The topological transition of the condensate from spherical to torus topology is indicated by the single arrow (T2) in Fig 8.…”

Section: Discussionmentioning

confidence: 99%

“…A consequence of this is the depletion of EDP from the LPD-VASP condensate, initiating the rapid polymerization of actin around the bud. We suspect that VASP's enhanced polymerization efficacy when clustered 12,81 could also play a supportive role in the formation of actin rings at the base of the bud. The topological transition of the condensate from spherical to torus topology is indicated by the single arrow (T2) in Fig 8 . Interestingly, the size of the endocytic carriers formed in FEME (~ 1 µm) 3 and the condensate/actin torus formed in our experiments (~ 4-5 µm, Fig 3A and 3D) are within an order of magnitude of each other.…”

Section: Discussionmentioning

confidence: 99%

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VASP phase separation with priming proteins of fast endophilin mediated endocytosis modulates actin polymerization

Narayan,

James,

Cope

et al. 2024

Preprint

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Actin polymerization is essential in several clathrin-independent endocytic pathways including fast endophilin mediated endocytosis (FEME), however the actin machinery involved in FEME has been elusive. Here, we show that the actin polymerase VASP, colocalizes and interacts directly with the FEME priming complex. We identify endophilin (EDP) as a VASP binding partner and establish novel non-canonical interactions between EDP and the EVH1 and EVH2 domains of VASP. The major FEME regulators EDP and lamellipodin (LPD) interact multivalently with VASP undergoing liquid-liquid phase separation both in solution and on lipid membranes. We show that priming complex mimicking condensates localise actin polymerization, with LPD-VASP promoting and EDP antagonising actin assembly, suggesting a novel role for EDP during the priming step of FEME. Finally, we show that LPD and EDP recruits and clusters VASP on lipid membranes mimicking the plasma membrane's inner leaflet to locally assemble actin filaments. Our work supports a model where actin polymerization in FEME is spatiotemporally initiated by the depletion of EDP, mediated by receptor activation.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

VASP phase separation with priming proteins of fast endophilin mediated endocytosis modulates actin polymerization

Narayan,

James,

Cope

et al. 2024

Preprint

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Section: Assembly and Disassembly Of Actin Bundlesmentioning

confidence: 99%

“…Bundling proteins also facilitate bundles elongation by “collaborating” with actin filaments elongating proteins (Ena/VASP and formins) [ 215 , 301 , 302 ]. The “alliance” between Ena/VASP and formins with fascin appears crucial for uniform elongation of all filaments in actin bundles in filopodia [ 215 , 301 , 302 ]. Some formins (that exist as dimers [ 303 ]) and Ena/VASP proteins (that exist as tetramers [ 302 ]) contribute to bundles formation as they have multiple actin-binding sites, a property common in all actin-bundling proteins.…”

Section: Assembly and Disassembly Of Actin Bundlesmentioning

confidence: 99%

“…The “alliance” between Ena/VASP and formins with fascin appears crucial for uniform elongation of all filaments in actin bundles in filopodia [ 215 , 301 , 302 ]. Some formins (that exist as dimers [ 303 ]) and Ena/VASP proteins (that exist as tetramers [ 302 ]) contribute to bundles formation as they have multiple actin-binding sites, a property common in all actin-bundling proteins. In addition, these proteins can translocate from the barbed ends to the side of actin filaments, which aids their crosslinking activity [ 304 , 305 , 306 ].…”

Section: Assembly and Disassembly Of Actin Bundlesmentioning

confidence: 99%

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Actin Bundles Dynamics and Architecture

2023

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Cells use the actin cytoskeleton for many of their functions, including their division, adhesion, mechanosensing, endo- and phagocytosis, migration, and invasion. Actin bundles are the main constituent of actin-rich structures involved in these processes. An ever-increasing number of proteins that crosslink actin into bundles or regulate their morphology is being identified in cells. With recent advances in high-resolution microscopy and imaging techniques, the complex process of bundles formation and the multiple forms of physiological bundles are beginning to be better understood. Here, we review the physiochemical and biological properties of four families of highly conserved and abundant actin-bundling proteins, namely, α-actinin, fimbrin/plastin, fascin, and espin. We describe the similarities and differences between these proteins, their role in the formation of physiological actin bundles, and their properties—both related and unrelated to their bundling abilities. We also review some aspects of the general mechanism of actin bundles formation, which are known from the available information on the activity of the key actin partners involved in this process.

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Benefits and challenges of reconstituting the actin cortex

Waechtler,

Jayasankar,

Morin

et al. 2024

Cytoskeleton

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The cell's ability to change shape is a central feature in many cellular processes, including cytokinesis, motility, migration, and tissue formation. The cell constructs a network of contractile proteins underneath the cell membrane to form the cortex, and the reorganization of these components directly contributes to cellular shape changes. The desire to mimic these cell shape changes to aid in the creation of a synthetic cell has been increasing. Therefore, membrane‐based reconstitution experiments have flourished, furthering our understanding of the minimal components the cell uses throughout these processes. Although biochemical approaches increased our understanding of actin, myosin II, and actin‐associated proteins, using membrane‐based reconstituted systems has further expanded our understanding of actin structures and functions because membrane–cortex interactions can be analyzed. In this review, we highlight the recent developments in membrane‐based reconstitution techniques. We examine the current findings on the minimal components needed to recapitulate distinct actin structures and functions and how they relate to the cortex's impact on cellular mechanical properties. We also explore how co‐processing of computational models with wet‐lab experiments enhances our understanding of these properties. Finally, we emphasize the benefits and challenges inherent to membrane‐based, reconstitution assays, ranging from the advantage of precise control over the system to the difficulty of integrating these findings into the complex cellular environment.

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VASP localization to lipid bilayers induces polymerization driven actin bundle formation

Cited by 6 publications

References 67 publications

VASP phase separation with priming proteins of fast endophilin mediated endocytosis modulates actin polymerization

VASP phase separation with priming proteins of fast endophilin mediated endocytosis modulates actin polymerization

Actin Bundles Dynamics and Architecture

Benefits and challenges of reconstituting the actin cortex

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