Please use this identifier to cite or link to this item: https://doi.org/10.1091/mbc.E10-08-0661
DC FieldValue
dc.titleFilamin depletion blocks endoplasmic spreading and destabilizes force-bearing adhesions
dc.contributor.authorLynch, C.D.
dc.contributor.authorGauthier, N.C.
dc.contributor.authorBiais, N.
dc.contributor.authorLazar, A.M.
dc.contributor.authorRoca-Cusachs, P.
dc.contributor.authorYu, C.-H.
dc.contributor.authorSheetz, M.P.
dc.date.accessioned2014-10-27T08:28:31Z
dc.date.available2014-10-27T08:28:31Z
dc.date.issued2011-04-15
dc.identifier.citationLynch, C.D., Gauthier, N.C., Biais, N., Lazar, A.M., Roca-Cusachs, P., Yu, C.-H., Sheetz, M.P. (2011-04-15). Filamin depletion blocks endoplasmic spreading and destabilizes force-bearing adhesions. Molecular Biology of the Cell 22 (8) : 1263-1273. ScholarBank@NUS Repository. https://doi.org/10.1091/mbc.E10-08-0661
dc.identifier.issn10591524
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100681
dc.description.abstractCell motility is an essential process that depends on a coherent, cross-linked actin cytoskeleton that physically coordinates the actions of numerous structural and signaling molecules. The actin cross-linking protein, filamin (Fln), has been implicated in the support of three-dimensional cortical actin networks capable of both maintaining cellular integrity and withstanding large forces. Although numerous studies have examined cells lacking one of the multiple Fln isoforms, compensatory mechanisms can mask novel phenotypes only observable by further Fln depletion. Indeed, shRNA-mediated knockdown of FlnA in FlnB-/- mouse embryonic fibroblasts (MEFs) causes a novel endoplasmic spreading deficiency as detected by endoplasmic reticulum markers. Microtubule (MT) extension rates are also decreased but not by peripheral actin flow, because this is also decreased in the Fln-depleted system. Additionally, Fln-depleted MEFs exhibit decreased adhesion stability that appears in increased ruffling of the cell edge, reduced adhesion size, transient traction forces, and decreased stress fibers. FlnA-/- MEFs, but not FlnB-/- MEFs, also show a moderate defect in endoplasm spreading, characterized by initial extension followed by abrupt retractions and stress fiber fracture. FlnA localizes to actin linkages surrounding the endoplasm, adhesions, and stress fibers. Thus we suggest that Flns have a major role in the maintenance of actin-based mechanical linkages that enable endoplasmic spreading and MT extension as well as sustained traction forces and mature focal adhesions. © 2011.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1091/mbc.E10-08-0661
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1091/mbc.E10-08-0661
dc.description.sourcetitleMolecular Biology of the Cell
dc.description.volume22
dc.description.issue8
dc.description.page1263-1273
dc.description.codenMBCEE
dc.identifier.isiut000289558600012
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

51
checked on May 20, 2022

WEB OF SCIENCETM
Citations

50
checked on May 12, 2022

Page view(s)

121
checked on May 12, 2022

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.