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dc.contributor.authorNeelam, Srujana
dc.contributor.authorChancellor, T J.
dc.contributor.authorLi, Yuan
dc.contributor.authorNickerson, Jeffrey A.
dc.contributor.authorRoux, Kyle J.
dc.contributor.authorDickinson, Richard B.
dc.contributor.authorLele, Tanmay P.
dc.date2022-08-11T08:08:03.000
dc.date.accessioned2022-08-23T15:40:50Z
dc.date.available2022-08-23T15:40:50Z
dc.date.issued2015-05-05
dc.date.submitted2015-10-13
dc.identifier.citationProc Natl Acad Sci U S A. 2015 May 5;112(18):5720-5. doi: 10.1073/pnas.1502111112. Epub 2015 Apr 21. <a href="http://dx.doi.org/10.1073/pnas.1502111112">Link to article on publisher's site</a>.
dc.identifier.issn0027-8424 (Linking)
dc.identifier.doi10.1073/pnas.1502111112
dc.identifier.pmid25901323
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26489
dc.description.abstractHow cells maintain nuclear shape and position against various intracellular and extracellular forces is not well understood, although defects in nuclear mechanical homeostasis are associated with a variety of human diseases. We estimated the force required to displace and deform the nucleus in adherent living cells with a technique to locally pull the nuclear surface. A minimum pulling force of a few nanonewtons--far greater than typical intracellular motor forces--was required to significantly displace and deform the nucleus. Upon force removal, the original shape and position were restored quickly within a few seconds. This stiff, elastic response required the presence of vimentin, lamin A/C, and SUN (Sad1p, UNC-84)-domain protein linkages, but not F-actin or microtubules. Although F-actin and microtubules are known to exert mechanical forces on the nuclear surface through molecular motor activity, we conclude that the intermediate filament networks maintain nuclear mechanical homeostasis against localized forces.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=25901323&dopt=Abstract">Link to Article in PubMed</a>
dc.rights<p>Publisher PDF posted as allowed by the publisher's author rights policy at http://www.pnas.org/site/aboutpnas/authorfaq.xhtml.</p>
dc.subjectActins
dc.subjectAnimals
dc.subjectCell Adhesion
dc.subjectCell Line, Tumor
dc.subjectCell Membrane
dc.subjectCell Nucleus
dc.subjectCell Survival
dc.subjectCytoskeleton
dc.subjectElasticity
dc.subjectFibroblasts
dc.subject*Gene Expression Regulation
dc.subjectGreen Fluorescent Proteins
dc.subject*Homeostasis
dc.subjectHumans
dc.subjectMice
dc.subjectMicromanipulation
dc.subjectMicroscopy, Fluorescence
dc.subjectMicrotubules
dc.subjectNIH 3T3 Cells
dc.subjectNuclear Envelope
dc.subjectRNA, Small Interfering
dc.subjectcytoskeleton
dc.subjectnuclear forces
dc.subjectnuclear mechanics
dc.subjectnuclear positioning
dc.subjectnuclear shape
dc.subjectCell Biology
dc.titleDirect force probe reveals the mechanics of nuclear homeostasis in the mammalian cell
dc.typeArticle
dc.source.journaltitleProceedings of the National Academy of Sciences of the United States of America
dc.source.volume112
dc.source.issue18
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1172&amp;context=cellbiology_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cellbiology_pp/173
dc.identifier.contextkey7709840
refterms.dateFOA2022-08-23T15:40:50Z
html.description.abstract<p>How cells maintain nuclear shape and position against various intracellular and extracellular forces is not well understood, although defects in nuclear mechanical homeostasis are associated with a variety of human diseases. We estimated the force required to displace and deform the nucleus in adherent living cells with a technique to locally pull the nuclear surface. A minimum pulling force of a few nanonewtons--far greater than typical intracellular motor forces--was required to significantly displace and deform the nucleus. Upon force removal, the original shape and position were restored quickly within a few seconds. This stiff, elastic response required the presence of vimentin, lamin A/C, and SUN (Sad1p, UNC-84)-domain protein linkages, but not F-actin or microtubules. Although F-actin and microtubules are known to exert mechanical forces on the nuclear surface through molecular motor activity, we conclude that the intermediate filament networks maintain nuclear mechanical homeostasis against localized forces.</p>
dc.identifier.submissionpathcellbiology_pp/173
dc.contributor.departmentDepartment of Cell and Developmental Biology
dc.source.pages5720-5


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