{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/110778"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/110778","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Mechanism of E-cadherin dimerization at the plasma membrane","abstract":"Embargo set by: Seth Robbins for item 118623 Lift date: 2023-09-17T04:04:53Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","abstract_html":"Embargo set by: Seth Robbins for item 118623 Lift date: 2023-09-17T04:04:53Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","abstract_has_math":false,"creators":["Vu, Vinh"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Leckband, Deborah","Zhang, Kai","Das, Aditi","Breiher, Bill"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2021,"date_issued":"2021-09-17T04:03:59Z","date_published":"2021-09-17T04:03:59Z","updated_at":"2026-07-22T22:24:52Z","subjects":["cadherin, fluorescence, dimerization, oligomerization"],"languages":["en"],"rights":["Copy right 2021 Vinh Vu"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/2142/110778","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Leckband, Deborah","Zhang, Kai","Das, Aditi","Breiher, Bill"]},{"key":"dc:creator","label":"Author","values":["Vu, Vinh"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2021-09-17T04:03:59Z","2023-09-17T04:07:01Z","2021-03-26","2021-05"]},{"key":"dc:type","label":"Dc Type","values":["text","Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["cadherin, fluorescence, dimerization, oligomerization"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["Copy right 2021 Vinh Vu"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/110778"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Embargo set by: Seth Robbins for item 118623 Lift date: 2023-09-17T04:04:53Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Cadherins are essential intercellular adhesion proteins that regulate tissue cohesion and paracellular permeability by assembling dense adhesion plaques at cell-to-cell contacts. This thesis addresses two aspects of cadherin adhesion and force transduction. The first portion of this thesis addresses the mechanisms of E-cadherin dimerization at the plasma membrane and its impact on cadherin trans binding and on cadherin-mediated cell adhesion. Full-spectrum imaging fluorescence resonance energy transfer (FSI-FRET) measurements directly demonstrate that epithelial-cadherin (E-cadherin) forms constitutive lateral (cis) dimers at the plasma membrane. Studies further show that this requires the intracellular domain and binding to p120 catenin. Quantitative cell binding measurements and fluorescence imaging demonstrate that p120 catenin binding to the cadherin intracellular domain enhances the trans cadherin binding affinity, cell adhesion, and the assembly of macroscopic cadherin clusters at intercellular adhesions. Single-molecule tracking studies of engineered mutants of the E-cadherin ectodomain mutants on supported bilayers showed that the extracellular domain also clusters in the absence of the trans interaction or the intracellular domain, but the cis bonds between ectodomains are much weaker than those involving p120ctn. The second portion of this thesis described in Chapter 3 is on cadherin-based mechanotransduction and the role of homophilic vs heterophilic cadherin ligation on force transduction cascades. Studies demonstrate that cadherin force transduction requires homophilic cadherin ligation and cadherin association with specific receptor tyrosine kinases on the same cell. By contrast, heterophilic ligands fail to activate force transduction signaling. Studies further demonstrate that this mechano-selectivity regulates cadherin-dependent signaling cascades that reinforce cell adhesion strength and the extent of cell spreading on cadherin substrates. Overall, these studies provide novel insights into the assembly of cadherin adhesions, and the regulation of cadherin binding affinities, cell adhesion, and mechanotransduction.","Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2023-05-01","The student, Vinh Vu, accepted the attached license on 2021-03-12 at 13:56.","The student, Vinh Vu, submitted this Dissertation for approval on 2021-03-12 at 14:16.","This Dissertation was approved for publication on 2021-03-26 at 14:57.","DSpace SAF Submission Ingestion Package generated from Vireo submission #16194 on 2021-09-16 at 20:07:11","Made available in DSpace on 2021-09-17T04:03:59Z (GMT). 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This thesis addresses two aspects of cadherin adhesion and force transduction. The first portion of this thesis addresses the mechanisms of E-cadherin dimerization at the plasma membrane and its impact on cadherin trans binding and on cadherin-mediated cell adhesion. Full-spectrum imaging fluorescence resonance energy transfer (FSI-FRET) measurements directly demonstrate that epithelial-cadherin (E-cadherin) forms constitutive lateral (cis) dimers at the plasma membrane. Studies further show that this requires the intracellular domain and binding to p120 catenin. Quantitative cell binding measurements and fluorescence imaging demonstrate that p120 catenin binding to the cadherin intracellular domain enhances the trans cadherin binding affinity, cell adhesion, and the assembly of macroscopic cadherin clusters at intercellular adhesions. Single-molecule tracking studies of engineered mutants of the E-cadherin ectodomain mutants on supported bilayers showed that the extracellular domain also clusters in the absence of the trans interaction or the intracellular domain, but the cis bonds between ectodomains are much weaker than those involving p120ctn. The second portion of this thesis described in Chapter 3 is on cadherin-based mechanotransduction and the role of homophilic vs heterophilic cadherin ligation on force transduction cascades. Studies demonstrate that cadherin force transduction requires homophilic cadherin ligation and cadherin association with specific receptor tyrosine kinases on the same cell. By contrast, heterophilic ligands fail to activate force transduction signaling. Studies further demonstrate that this mechano-selectivity regulates cadherin-dependent signaling cascades that reinforce cell adhesion strength and the extent of cell spreading on cadherin substrates. Overall, these studies provide novel insights into the assembly of cadherin adhesions, and the regulation of cadherin binding affinities, cell adhesion, and mechanotransduction.","Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2023-05-01","The student, Vinh Vu, accepted the attached license on 2021-03-12 at 13:56.","The student, Vinh Vu, submitted this Dissertation for approval on 2021-03-12 at 14:16.","This Dissertation was approved for publication on 2021-03-26 at 14:57.","DSpace SAF Submission Ingestion Package generated from Vireo submission #16194 on 2021-09-16 at 20:07:11","Made available in DSpace on 2021-09-17T04:03:59Z (GMT). No. of bitstreams: 2 VU-DISSERTATION-2021.pdf: 3583057 bytes, checksum: eb3b047721b114334e4c6617b66c9bb9 (MD5) LICENSE.txt: 4204 bytes, checksum: 1b22850a7b1e7d317053a6f693825afd (MD5) Previous issue date: 2021-03-26","Embargo set by: Seth Robbins for item 118623 Lift date: 2023-09-17T04:07:01Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Author requested closed access (OA after 2yrs) in Vireo ETD system","Limited"],"dc:format":["application/pdf"],"dc:identifier":["http://hdl.handle.net/2142/110778"],"dc:language":["en"],"dc:rights":["Copy right 2021 Vinh Vu"],"dc:subject":["cadherin, fluorescence, dimerization, oligomerization"],"dc:title":["Mechanism of E-cadherin dimerization at the plasma membrane"],"dc:type":["text","Thesis"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:24:52Z"}