Active Cytoskeletal Composites Display Emergent Tunable Contractility and Restructuring

Active Cytoskeletal Composites Display Emergent Tunable Contractility and Restructuring | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Article Active Cytoskeletal Composites Display Emergent Tunable Contractility and Restructuring Gloria Lee, Gregor Leech, Pancy Lwin, Jonathan Michel, Christopher Currie, and 5 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-463018/v1 This work is licensed under a CC BY 4.0 License Status: Published Journal Publication published 01 Jan, 2021 Read the published version in Soft Matter → Version 1 posted You are reading this latest preprint version Abstract The cytoskeleton is a model active matter system that controls diverse cellular processes from division to motility. While both active actomyosin dynamics and actin-microtubule interactions are key to the cytoskeleton’s versatility and adaptability, an understanding of their interplay is lacking. Here, we couple microscale experiments with mechanistic modeling to elucidate how connectivity, rigidity, and force-generation affect emergent material properties in in vitro composites of actin, tubulin, and myosin. We use time-resolved differential dynamic microscopy and spatial image autocorrelation to show that ballistic contraction occurs in composites with sufficient flexibility and motor density, but that a critical fraction of microtubules is necessary to sustain controlled dynamics. Our active double-network models reveal that percolated actomyosin networks are essential for contraction, but that networks with comparable actin and microtubule densities can uniquely resist mechanical stresses while simultaneously supporting substantial restructuring. Our findings provide a much-needed blueprint for designing cytoskeleton-inspired materials that couple tunability with resilience and adaptability. Biomaterials Polymer Science Cytoskeletal Composites Contraction Restructuring adaptability Figures Figure 1 Figure 2 Figure 3 Figure 4 Figure 5 Figure 6 Full Text Additional Declarations There is NO Competing Interest. Supplementary Files Supp.Info.LeeNMSI210425.pdf Supplementary Information Cite Share Download PDF Status: Published Journal Publication published 01 Jan, 2021 Read the published version in Soft Matter → Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. 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Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-463018","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Article","associatedPublications":[],"authors":[{"id":23428924,"identity":"c1475eb4-0dd1-427d-9ecb-e305b17563e7","order_by":0,"name":"Gloria Lee","email":"","orcid":"https://orcid.org/0000-0002-0761-9127","institution":"University of San Diego","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Gloria","middleName":"","lastName":"Lee","suffix":""},{"id":23428925,"identity":"8cd74fa2-68b9-40d8-86d2-cae605cf6c1f","order_by":1,"name":"Gregor Leech","email":"","orcid":"","institution":"University of San Diego","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Gregor","middleName":"","lastName":"Leech","suffix":""},{"id":23428926,"identity":"8a8b8f3d-024d-405a-b197-af5388143753","order_by":2,"name":"Pancy Lwin","email":"","orcid":"","institution":"Rochester Institute of Technology","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Pancy","middleName":"","lastName":"Lwin","suffix":""},{"id":23428927,"identity":"377a9530-e646-45c7-b7ff-1bdaf48b3e46","order_by":3,"name":"Jonathan Michel","email":"","orcid":"","institution":"Rochester Institute of Technology","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Jonathan","middleName":"","lastName":"Michel","suffix":""},{"id":23428928,"identity":"cb61863d-81a0-434d-ad07-5eb886524e35","order_by":4,"name":"Christopher Currie","email":"","orcid":"","institution":"University of San Diego","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Christopher","middleName":"","lastName":"Currie","suffix":""},{"id":23428929,"identity":"64dc3de1-0b0c-4899-968a-c8ab01465694","order_by":5,"name":"Michael Rust","email":"","orcid":"","institution":"University of Chicago","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Michael","middleName":"","lastName":"Rust","suffix":""},{"id":23428930,"identity":"997891f6-a133-4f48-912d-7f6a30fcefd9","order_by":6,"name":"Jennifer Ross","email":"","orcid":"","institution":"Syracuse University","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Jennifer","middleName":"","lastName":"Ross","suffix":""},{"id":23428931,"identity":"603c06c8-5a16-4387-bc1c-20a104b0cbec","order_by":7,"name":"Ryan McGorty","email":"","orcid":"https://orcid.org/0000-0002-6577-060X","institution":"University of San Diego","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Ryan","middleName":"","lastName":"McGorty","suffix":""},{"id":23428932,"identity":"15ab421c-bce1-4d28-b8ee-164f66bea5d9","order_by":8,"name":"Moumita Das","email":"","orcid":"","institution":"Rochester Institute of Technology","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Moumita","middleName":"","lastName":"Das","suffix":""},{"id":23428933,"identity":"8adc1b8b-7b21-4c4e-a333-e23f204b486c","order_by":9,"name":"Rae Robertson-Anderson","email":"data:image/png;base64,iVBORw0KGgoAAAANSUhEUgAAAZAAAAAyAQMAAABI0h/eAAAABlBMVEX///8AAABVwtN+AAAACXBIWXMAAA7EAAAOxAGVKw4bAAAA80lEQVRIiWNgGAWjYJACCTDJ3gAk2CBsBh6itPAcIFmLRAJICwNhLebtZw/e+LinTs5c8vnDzwVlFnLy7g2MD9624dYicyYv2XLGs8PGlrNzjKVnnJMwNjxzgNlwLh4tEgw5ZtI8Bw4kbridwyDN2yaRuHFGAhuQgUcL/xsz6T8H6hI33Dz++DdQSz1QC/tvvFokgLYwHGBO3HCDwQxkS4K8RAIbM34tb4wtew4cNjY4k2NmzXNOwnADz8FmyTnn8Dksx/DGjwN1cgbHjz++zVNWJy/f3nzww5sy3FowgcEBxgZS1AOBPKkaRsEoGAWjYNgDAFBnTjtwN4XsAAAAAElFTkSuQmCC","orcid":"https://orcid.org/0000-0003-4475-4667","institution":"University of San Diego","correspondingAuthor":true,"submittingAuthor":false,"prefix":"","firstName":"Rae","middleName":"","lastName":"Robertson-Anderson","suffix":""}],"badges":[],"createdAt":"2021-04-25 21:25:29","currentVersionCode":1,"declarations":"","doi":"10.21203/rs.3.rs-463018/v1","doiUrl":"https://doi.org/10.21203/rs.3.rs-463018/v1","draftVersion":[],"editorialEvents":[{"content":"https://doi.org/10.1039/D1SM01083B","type":"published","date":"2021-01-01T12:08:44+00:00"}],"editorialNote":"","failedWorkflow":false,"files":[{"id":8870488,"identity":"a8933933-4466-490f-ba4e-7c450a01ec06","added_by":"auto","created_at":"2021-05-06 17:14:31","extension":"png","order_by":1,"title":"Figure 1","display":"","copyAsset":false,"role":"figure","size":535366,"visible":true,"origin":"","legend":"Tuning the composition of active cytoskeleton composites. (A) 256×128 pixel (212×106 μm) two-color confocal microscopy images show how composites of actin filaments (magenta) and microtubules (green) are rearranged via myosin II motor activity (Movie S1). In each panel, images taken at the beginning (left, before) and end (right, after) of the 45-min myosin activation are shown. Panels are ordered by increasing myosin concentration (cM, blue) going from left to right and increasing molar fraction of actin (ΦA, red) going from top to bottom. The colors outlining each panel match the color coding used in subsequent figures. Scale bar pertains to all images. Panels in the top-left and bottom-right do not have data. (B) Deformation of a simulated active biopolymer double-network for parameters shown in (A). Simulations show how double-networks made of an actomyosin network (magenta) and a microtubule network (green) deform for varying concentrations of myosin and actin. As in (A), panels are ordered by increasing myosin concentration (cM, blue) from left to right and increasing actin fraction (ΦA, red) going from top to bottom. Simulation box size is 24 ×20 μm for all images.","description":"","filename":"Fig1.png","url":"https://assets-eu.researchsquare.com/files/rs-463018/v1/6c8c1acf28a3aae73320720c.png"},{"id":8870615,"identity":"c4902aad-7126-4358-a536-fe2b930831ff","added_by":"auto","created_at":"2021-05-06 17:20:31","extension":"png","order_by":2,"title":"Figure 2","display":"","copyAsset":false,"role":"figure","size":521465,"visible":true,"origin":"","legend":"Differential dynamic microscopy shows that composite contraction dynamics can be independently tuned by the actin fraction and myosin concentration. (A) Representative image structure functions 𝐷(𝑞,𝛥𝑡) of varying active composites, normalized by the corresponding initial value 𝐷0, at wavenumber 𝑞 = 1.481 μm-1. DDM is performed separately on microtubule (top, open symbols) and actin (bottom, filled symbols) time-series channels. The lag-time dependence for all curves is largely indistinguishable when comparing actin and microtubule channels. For the actin channel, image structure functions of composites with lower myosin concentrations cM (cyan left pointing triangles) and lower actin fractions ΦA (pink upwards pointing triangles) do not reach plateaus, while those of composites with higher myosin concentrations and actin fractions reach decorrelation plateaus at varying lag times (purple squares, green stars, blue right pointing triangles, orange circles, red downwards pointing triangles). (B) Average characteristic decay time 𝜏 vs wavenumber 𝑞 for both actin (filled symbols) and microtubule (open symbols) channels for each condition that reached a plateau in (A). All curves follow 𝜏 ~ 𝑞−1 scaling for 𝑞 = 1 – 3 μm-1, indicating ballistic motion. Symbol colors and shapes correspond to legends in (A). (C) Average contraction velocities k extracted from fitting 𝜏(𝑞) curves in (B) to 𝜏=(𝑘𝑞)−1. Error bars in (B) and (C) represent the standard error of values across all time-series.","description":"","filename":"Fig2.png","url":"https://assets-eu.researchsquare.com/files/rs-463018/v1/34dd2a9b3492aa18b978d978.png"},{"id":8870590,"identity":"b24cc5ca-6893-44ea-9996-570ea35b6bcf","added_by":"auto","created_at":"2021-05-06 17:17:31","extension":"png","order_by":3,"title":"Figure 3","display":"","copyAsset":false,"role":"figure","size":416679,"visible":true,"origin":"","legend":"Spatial image autocorrelation analysis reveals that myosin activity increases correlation lengths in a tunable manner independent of measured velocities. (A) Average autocorrelation curves 𝑔(𝑟) for the microtubule channel for all composite formulations at the beginning (left, t = 0 min, dark shades) and end (right, t = 42 mins, light shades) of the experimental window. The inset shows example fits of 𝑔(𝑟) curves to 𝑔(𝑟)=𝐴𝑒−𝑟𝜆 at the initial and final times for the (ΦA, cM) = (0.75, 0.12) composite. (B) Average correlation lengths for actin (closed symbols) and microtubule (open symbols) channels for each composite formulation determined from exponential fits (see inset in A) to the corresponding autocorrelation curves. Data is divided into composites that exhibit minimal restructuring (left) versus substantial restructuring (right). Error bars in (B) and (C) represent the standard error of values across all replicates.","description":"","filename":"Fig3.png","url":"https://assets-eu.researchsquare.com/files/rs-463018/v1/482471d59104ae785877d7a4.png"},{"id":8870617,"identity":"cbe4d09e-b8cc-4eb3-ae0b-338c33723774","added_by":"auto","created_at":"2021-05-06 17:20:31","extension":"png","order_by":4,"title":"Figure 4","display":"","copyAsset":false,"role":"figure","size":323432,"visible":true,"origin":"","legend":"Active double-network modeling shows tunable restructuring and rigidity of myosin-driven actin-microtubule composites. (A) Heat maps for strains experienced by actin and microtubule networks in the active double-network model for the myosin concentrations and molar actin fractions shown in Fig. 1. Contractile strains are shown in shades of red and extensile strains are shown in shades of blue, with darker colors representing larger strains. White-colored regions represent negligibly small strains. The strain maps for the actin network and microtubule network for each condition are shown in the top and bottom of each panel, respectively. (B) Mechanical modulus 𝐺’ of a simulated active double-network for parameters shown in Fig. 1B. 𝐺’ is in simulation units corresponding to the microtubule stretching modulus (α1).","description":"","filename":"Fig4.png","url":"https://assets-eu.researchsquare.com/files/rs-463018/v1/2bce382a05dca3a0bead6500.png"},{"id":8870588,"identity":"fdee12ee-ef3a-4176-af82-b96d16baa9e1","added_by":"auto","created_at":"2021-05-06 17:17:31","extension":"png","order_by":5,"title":"Figure 5","display":"","copyAsset":false,"role":"figure","size":721325,"visible":true,"origin":"","legend":"Time-resolved differential dynamic microscopy shows higher actin fractions result in accelerating contraction dynamics. (A) Characteristic decay time 𝜏 vs wavenumber 𝑞 for actin (filled symbols, left) and microtubule (open symbols, right) channels for consecutive 6-min intervals during the 45 min activation time of a representative time-series. Curves follow 𝜏 ~ 𝑞−1 scaling, indicating ballistic motion. Varying colors and symbols correspond to different composite formulations and time intervals as depicted in the legend (lower right). 𝜏(𝑞) curves for the ΦA = 0.75 composite (red, downward-pointing triangles) are lower in magnitude and show substantially more time-dependence compared to both ΦA=0.5 composites. Both ΦA=0.5 composites also have overlapping 𝜏(𝑞) curves, indicating negligible dependence of time-resolved dynamics on the myosin concentration cM. (B) Contraction velocities for actin filaments (closed symbols) and microtubules (open symbols) for each 6-min interval of every analyzed time-series, extracted from fitting corresponding 𝜏(𝑞) curves. Error bars represent the standard error of values across all replicates. Symbol colors and shapes match Fig. 3 and correspond to (ΦA, cM) combinations shown in the legend.","description":"","filename":"Fig5.png","url":"https://assets-eu.researchsquare.com/files/rs-463018/v1/818e50b1e401dfe6566befee.png"},{"id":8870493,"identity":"f7fec419-2af0-4907-9e5e-5fa147d937ca","added_by":"auto","created_at":"2021-05-06 17:14:31","extension":"png","order_by":6,"title":"Figure 6","display":"","copyAsset":false,"role":"figure","size":281762,"visible":true,"origin":"","legend":"Cartoon phase diagram of active cytoskeleton composite dynamics mapped to the corresponding composite formulation (ΦA, cM) highlights tunability and desirable properties of active composites. (A) Comprehensive phase diagram showing how myosin-driven composite velocities (green, determined from DDM), restructuring (blue, determined via SIA), acceleration (yellow, determined from time-resolved DDM), and rigidity (pink, determined via double-network simulations) vary in formulation space (ΦA,cM). Darker shading of each color qualitatively indicates increasing metric values quantified within the separated figures in (B). Note that the panels in the bottom figures that lack numbers are those that we did not measure. The colors in those panels (top left, bottom right) are extrapolated based on the trends in our data. Velocities are averaged over both actin and microtubule channels as we observed similar dynamics for both filaments in all cases. Degree of restructuring is calculated by taking the difference in final and initial correlation length (Δ𝜆=𝜆𝑓𝑖𝑛𝑎𝑙−𝜆𝑖𝑛𝑖𝑡𝑖𝑎𝑙), and is reported separately for actin and microtubule channels because we observed instances of significant differences in Δ𝜆 for the two filaments. Acceleration is calculated by computing the average change in velocity over time for the final 21 min of each time-series. Rigidity is calculated by performing simulations under 0.005% shear to obtain the mechanical modulus 𝐺′, expressed in simulation units corresponding to the microtubule stretching modulus α1. Composites with ΦA=0.5 and sufficiently high cM exhibit coordinated contractile dynamics and rearrangement without destructive network acceleration or decorrelation of actin and microtubule restructuring.","description":"","filename":"Fig6.png","url":"https://assets-eu.researchsquare.com/files/rs-463018/v1/7d37ada4f426aeaedc2880fb.png"},{"id":15662990,"identity":"32f233f8-940e-450d-98b0-867027795a5a","added_by":"auto","created_at":"2021-11-18 12:08:58","extension":"pdf","order_by":0,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":1392164,"visible":true,"origin":"","legend":"","description":"","filename":"LeeNM210425.pdf","url":"https://assets-eu.researchsquare.com/files/rs-463018/v1_covered.pdf"},{"id":13629055,"identity":"33a54eef-6029-4288-9328-e83163a6d5e4","added_by":"auto","created_at":"2021-09-17 08:04:34","extension":"pdf","order_by":0,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":1386244,"visible":true,"origin":"","legend":"","description":"","filename":"LeeNM210425.pdf","url":"https://assets-eu.researchsquare.com/files/rs-463018/v1_covered.pdf"},{"id":8870684,"identity":"8501f1aa-77ce-457a-90f1-b3e5a73f4add","added_by":"auto","created_at":"2021-05-06 17:23:38","extension":"pdf","order_by":0,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":1063165,"visible":true,"origin":"","legend":"","description":"","filename":"LeeNM210425.pdf","url":"https://assets-eu.researchsquare.com/files/rs-463018/v1_stamped.pdf"},{"id":8870616,"identity":"13516ecc-6bb2-4428-bc14-566afc1a6fb7","added_by":"auto","created_at":"2021-05-06 17:20:31","extension":"pdf","order_by":1,"title":"","display":"","copyAsset":false,"role":"supplement","size":613981,"visible":true,"origin":"","legend":"Supplementary Information","description":"","filename":"Supp.Info.LeeNMSI210425.pdf","url":"https://assets-eu.researchsquare.com/files/rs-463018/v1/6ba2d21a7d8c4dad6d68777c.pdf"}],"financialInterests":"There is \u003cb\u003eNO\u003c/b\u003e Competing Interest.","formattedTitle":"Active Cytoskeletal Composites Display Emergent Tunable Contractility and Restructuring","fulltext":[{"header":"Full Text","content":"This preprint is available for \u003ca href='/article/rs-463018/latest.pdf' target='_blank'\u003edownload as a PDF\u003c/a\u003e."}],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":false,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":true,"hideJournal":false,"highlight":"","institution":"","isAcceptedByJournal":true,"isAuthorSuppliedPdf":true,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":false,"isPdfUpToDate":true,"isWithdrawnOrRetracted":false,"journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true},"keywords":"Cytoskeletal Composites, Contraction, Restructuring, adaptability","lastPublishedDoi":"10.21203/rs.3.rs-463018/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-463018/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"The cytoskeleton is a model active matter system that controls diverse cellular processes from division to motility. While both active actomyosin dynamics and actin-microtubule interactions are key to the cytoskeleton’s versatility and adaptability, an understanding of their interplay is lacking. Here, we couple microscale experiments with mechanistic modeling to elucidate how connectivity, rigidity, and force-generation affect emergent material properties in in vitro composites of actin, tubulin, and myosin. We use time-resolved differential dynamic microscopy and spatial image autocorrelation to show that ballistic contraction occurs in composites with sufficient flexibility and motor density, but that a critical fraction of microtubules is necessary to sustain controlled dynamics. Our active double-network models reveal that percolated actomyosin networks are essential for contraction, but that networks with comparable actin and microtubule densities can uniquely resist mechanical stresses while simultaneously supporting substantial restructuring. Our findings provide a much-needed blueprint for designing cytoskeleton-inspired materials that couple tunability with resilience and adaptability.","manuscriptTitle":"Active Cytoskeletal Composites Display Emergent Tunable Contractility and Restructuring","msid":"","msnumber":"","nonDraftVersions":[{"code":1,"date":"2021-05-06 17:14:29","doi":"10.21203/rs.3.rs-463018/v1","editorialEvents":[{"type":"communityComments","content":0}],"status":"published","journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true}}],"origin":"","ownerIdentity":"d4e7607f-10da-41d6-9d83-c5534c44d047","owner":[],"postedDate":"May 6th, 2021","published":true,"recentEditorialEvents":[],"rejectedJournal":[],"revision":"","amendment":"","status":"published-in-journal","subjectAreas":[{"id":4141813,"name":"Biomaterials"},{"id":4141814,"name":"Polymer Science"}],"tags":[],"updatedAt":"2021-11-18T12:08:44+00:00","versionOfRecord":{"articleIdentity":"rs-463018","link":"https://doi.org/10.1039/D1SM01083B","journal":{"identity":"soft-matter","isVorOnly":true,"title":"Soft Matter"},"publishedOn":"2021-01-01 12:08:44","publishedOnDateReadable":"January 1st, 2021"},"versionCreatedAt":"2021-05-06 17:14:29","video":"","vorDoi":"10.1039/D1SM01083B","vorDoiUrl":"https://doi.org/10.1039/D1SM01083B","workflowStages":[]},"version":"v1","identity":"rs-463018","journalConfig":"researchsquare"},"__N_SSP":true},"page":"/article/[identity]/[[...version]]","query":{"redirect":"/article/rs-463018","identity":"rs-463018","version":["v1"]},"buildId":"cBFmMYwuxLRRLfASyISRj","isFallback":false,"isExperimentalCompile":false,"dynamicIds":[84888],"gssp":true,"scriptLoader":[]}