Hypotonic stress induces fast, reversible degradation of the vimentin cytoskeleton via intracellular calcium release

Pan, Leiting; Ping, Zhang; Hu, Fang; Yan, Rui; He, Manni; Li, Wan; Xu, Jingyi; Xu, Ke

doi:10.1101/607416

Cited by 10 publications

(12 citation statements)

References 53 publications

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“…We treated cells with strong (75 mOsm) hypotonic shock for 5 min and then chemically fixed them for 2c-3D STORM. When we super-resolved clathrin and actin by 2c-3D STORM in these cells, the actin cytoskeleton remained intact (Pan et al, 2019) and associated with CCSs (Fig. S9 A -D).…”

Section: Actin Organization Adapts To Elevated Membrane Tension By Increasing Clathrin Coat Coveragementioning

confidence: 98%

Load adaptation of endocytic actin networks

Kaplan¹,

Sj²,

Chen³

et al. 2020

Preprint

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Clathrin-mediated endocytosis (CME) remains robust despite variations in plasma membrane tension. Actin assembly-mediated force generation becomes essential for CME under high membrane tension, but the underlying mechanisms are not understood. We investigated actin network ultrastructure at each stage of CME by super-resolution imaging. Actin and N-WASP spatial organization indicate that polymerization initiates at the base of clathrin-coated pits and that the actin network then grows away from the plasma membrane. Actin network organization is not tightly coupled to endocytic clathrin coat growth and deformation. Membrane tension-dependent changes in actin organization explain this uncoupling. Under elevated membrane tension, CME dynamics slow down and the actin network grows higher, resulting in greater coverage of the clathrin coat. This adaptive mechanism is especially crucial during the initial membrane curvature-generating stages of CME. Our findings reveal that adaptive force generation by the actin network ensures robust CME progression despite changes in plasma membrane tension.Highlights-Clathrin coat surface area and actin ultra-structure adapt to elevated membrane tension.-The actin network is nucleated at the base of the clathrin-coated pit and grows upward.-Actin ultra-structural organization is not tightly coupled to CME progression.-Actin force generation is required earlier in CME progression under elevated membrane tension.SummaryKaplan et al. revealed that actin assembly compensates for changes in plasma membrane tension by an adaptive force generating mechanism to ensure robust endocytosis. Under elevated membrane tension the network grows deeper, even in early endocytic stages, from the base upward.

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Section: Actin Organization Adapts To Elevated Membrane Tension By Increasing Clathrin Coat Coveragementioning

confidence: 98%

Load adaptation of endocytic actin networks

Kaplan¹,

Sj²,

Chen³

et al. 2020

Preprint

Self Cite

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“…The cytoskeleton is intimately linked to all processes regulating membrane tension, in particular cell volume regulation (5). For example, hypotonic shocks not only are responsible for increasing membrane tension (6,7) but also induce the degradation of vimentin (8) and a reorganization of actin filaments (9,10), without strongly affecting microtubules (8). The cytoskeleton regulates membrane tension by setting its value through active force generation and by establishing a membrane reservoir that buffers acute changes in tension (11).…”

Section: Plasma Membrane Tension | Cell Volume | Flipper-tr | Osmotic Shocks | Mechanobiologymentioning

confidence: 99%

Passive coupling of membrane tension and cell volume during active response of cells to osmosis

Roffay

Molinard

et al. 2021

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

112

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During osmotic changes of their environment, cells actively regulate their volume and plasma membrane tension that can passively change through osmosis. How tension and volume are coupled during osmotic adaptation remains unknown, as their quantitative characterization is lacking. Here, we performed dynamic membrane tension and cell volume measurements during osmotic shocks. During the first few seconds following the shock, cell volume varied to equilibrate osmotic pressures inside and outside the cell, and membrane tension dynamically followed these changes. A theoretical model based on the passive, reversible unfolding of the membrane as it detaches from the actin cortex during volume increase quantitatively describes our data. After the initial response, tension and volume recovered from hypoosmotic shocks but not from hyperosmotic shocks. Using a fluorescent membrane tension probe (fluorescent lipid tension reporter [Flipper-TR]), we investigated the coupling between tension and volume during these asymmetric recoveries. Caveolae depletion and pharmacological inhibition of ion transporters and channels, mTORCs, and the cytoskeleton all affected tension and volume responses. Treatments targeting mTORC2 and specific downstream effectors caused identical changes to both tension and volume responses, their coupling remaining the same. This supports that the coupling of tension and volume responses to osmotic shocks is primarily regulated by mTORC2.

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“…Relevant to this review are also glycosylation [ 36 ] and proteolysis. Vimentin proteolytic cleavage, either by endogenous proteases, like caspases during apoptosis [ 37 ] or calpain during hypotonic stress [ 38 ], or by proteases from pathogens, like the Moloney mouse sarcoma virus [ 39 ] or human immunodeficiency virus (HIV) [ 40 ], can provoke drastic rearrangements of the vimentin network with implications in pathogenesis.…”

Section: General Concepts On Vimentin Structure and Assemblymentioning

confidence: 99%

Vimentin as a Multifaceted Player and Potential Therapeutic Target in Viral Infections

Ramos

Stamatakis

Oeste

et al. 2020

IJMS

141

121

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Vimentin is an intermediate filament protein that plays key roles in integration of cytoskeletal functions, and therefore in basic cellular processes such as cell division and migration. Consequently, vimentin has complex implications in pathophysiology. Vimentin is required for a proper immune response, but it can also act as an autoantigen in autoimmune diseases or as a damage signal. Although vimentin is a predominantly cytoplasmic protein, it can also appear at extracellular locations, either in a secreted form or at the surface of numerous cell types, often in relation to cell activation, inflammation, injury or senescence. Cell surface targeting of vimentin appears to associate with the occurrence of certain posttranslational modifications, such as phosphorylation and/or oxidative damage. At the cell surface, vimentin can act as a receptor for bacterial and viral pathogens. Indeed, vimentin has been shown to play important roles in virus attachment and entry of severe acute respiratory syndrome-related coronavirus (SARS-CoV), dengue and encephalitis viruses, among others. Moreover, the presence of vimentin in specific virus-targeted cells and its induction by proinflammatory cytokines and tissue damage contribute to its implication in viral infection. Here, we recapitulate some of the pathophysiological implications of vimentin, including the involvement of cell surface vimentin in interaction with pathogens, with a special focus on its role as a cellular receptor or co-receptor for viruses. In addition, we provide a perspective on approaches to target vimentin, including antibodies or chemical agents that could modulate these interactions to potentially interfere with viral pathogenesis, which could be useful when multi-target antiviral strategies are needed.

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Hypotonic stress induces fast, reversible degradation of the vimentin cytoskeleton via intracellular calcium release

Cited by 10 publications

References 53 publications

Load adaptation of endocytic actin networks

Load adaptation of endocytic actin networks

Passive coupling of membrane tension and cell volume during active response of cells to osmosis

Vimentin as a Multifaceted Player and Potential Therapeutic Target in Viral Infections

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