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dc.contributor.authorTakizawa, Norio
dc.contributor.authorSmith, Tara C.
dc.contributor.authorNebl, Thomas
dc.contributor.authorCrowley, Jessica Lynn
dc.contributor.authorPalmieri, Stephen J.
dc.contributor.authorLifshitz, Lawrence M.
dc.contributor.authorEhrhardt, Anka G.
dc.contributor.authorHoffman, Laura M.
dc.contributor.authorBeckerle, Mary C.
dc.contributor.authorLuna, Elizabeth J.
dc.date2022-08-11T08:11:04.000
dc.date.accessioned2022-08-23T17:31:40Z
dc.date.available2022-08-23T17:31:40Z
dc.date.issued2006-08-02
dc.date.submitted2007-11-28
dc.identifier.citation<p>J Cell Biol. 2006 Jul 31;174(3):447-58. <a href="http://dx.doi.org/10.1083/jcb.200512051">Link to article on publisher's site</a></p>
dc.identifier.issn0021-9525 (Print)
dc.identifier.doi10.1083/jcb.200512051
dc.identifier.pmid16880273
dc.identifier.urihttp://hdl.handle.net/20.500.14038/50787
dc.description.abstractCell-substrate contacts, called focal adhesions (FAs), are dynamic in rapidly moving cells. We show that supervillin (SV)--a peripheral membrane protein that binds myosin II and F-actin in such cells--negatively regulates stress fibers, FAs, and cell-substrate adhesion. The major FA regulatory sequence within SV (SV342-571) binds to the LIM domains of two proteins in the zyxin family, thyroid receptor-interacting protein 6 (TRIP6) and lipoma-preferred partner (LPP), but not to zyxin itself. SV and TRIP6 colocalize within large FAs, where TRIP6 may help recruit SV. RNAi-mediated decreases in either protein increase cell adhesion to fibronectin. TRIP6 partially rescues SV effects on stress fibers and FAs, apparently by mislocating SV away from FAs. Thus, SV interactions with TRIP6 at FAs promote loss of FA structure and function. SV and TRIP6 binding partners suggest several specific mechanisms through which the SV-TRIP6 interaction may regulate FA maturation and/or disassembly.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16880273&dopt=Abstract">Link to article in PubMed</a></p>
dc.rightsPublisher PDF posted as allowed by the publisher's terms of use policy at: http://www.rupress.org/terms After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof.
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.subjectAdaptor Proteins, Signal Transducing
dc.subjectAnimals
dc.subjectCOS Cells
dc.subjectCattle
dc.subjectCells, Cultured
dc.subjectCercopithecus aethiops
dc.subjectDown-Regulation
dc.subjectFocal Adhesions
dc.subjectGreen Fluorescent Proteins
dc.subjectHumans
dc.subjectMembrane Proteins
dc.subjectMice
dc.subjectMicrofilament Proteins
dc.subjectMicrotubule-Associated Proteins
dc.subjectMyocytes, Smooth Muscle
dc.subjectNuclear Proteins
dc.subjectProtein Binding
dc.subjectRats
dc.subjectRegulatory Sequences, Nucleic Acid
dc.subjectTranscription Factors
dc.subjectCell Biology
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleSupervillin modulation of focal adhesions involving TRIP6/ZRP-1
dc.typeJournal Article
dc.source.journaltitleThe Journal of cell biology
dc.source.volume174
dc.source.issue3
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1310&amp;context=wfc_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/wfc_pp/311
dc.identifier.contextkey397401
refterms.dateFOA2022-08-23T17:31:41Z
html.description.abstract<p>Cell-substrate contacts, called focal adhesions (FAs), are dynamic in rapidly moving cells. We show that supervillin (SV)--a peripheral membrane protein that binds myosin II and F-actin in such cells--negatively regulates stress fibers, FAs, and cell-substrate adhesion. The major FA regulatory sequence within SV (SV342-571) binds to the LIM domains of two proteins in the zyxin family, thyroid receptor-interacting protein 6 (TRIP6) and lipoma-preferred partner (LPP), but not to zyxin itself. SV and TRIP6 colocalize within large FAs, where TRIP6 may help recruit SV. RNAi-mediated decreases in either protein increase cell adhesion to fibronectin. TRIP6 partially rescues SV effects on stress fibers and FAs, apparently by mislocating SV away from FAs. Thus, SV interactions with TRIP6 at FAs promote loss of FA structure and function. SV and TRIP6 binding partners suggest several specific mechanisms through which the SV-TRIP6 interaction may regulate FA maturation and/or disassembly.</p>
dc.identifier.submissionpathwfc_pp/311
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentDepartment of Physiology
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages447-58


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Publisher PDF posted as allowed by the publisher's terms of use policy at: http://www.rupress.org/terms After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof.
Except where otherwise noted, this item's license is described as Publisher PDF posted as allowed by the publisher's terms of use policy at: http://www.rupress.org/terms After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof.