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Article: Spatial-temporal reorganization of activated integrins

TitleSpatial-temporal reorganization of activated integrins
Authors
KeywordsTumor metastasis
Actin polymerization
Synergy receptor
Supported lipid membrane
RGD peptide
Integrin
Src family kinase
Issue Date2012
Citation
Cell Adhesion and Migration, 2012, v. 6, n. 3, p. 280-284 How to Cite?
AbstractIntegrin receptors play important roles in cell adhesion and tumor metastasis. The coupling of mechanical sensing and biochemical ligation is known to collectively regulate the activation of integrin receptors. Recently, oligomerization of activated integrins has been considered as the primordial signature of cytoskeletal remodeling and the initiation of various downstream signals, such as focal and fibrillar adhesions. However, spatio-temporal reorganization of activated integrins and associated proteins remains poorly understood. Here, we summarized the recent discovery of sequential biophysical events of integrin activation during early adhesion formation. Using the cyclic Arg-Gly-Asp (RGD) peptide as a mobile ligand on supported lipid membranes, a series of previously unreported events were observed following integrin avb3 clustering and cell spreading, including a long-range lateral translocation of the integrin clusters. With initial clustering, localized actin polymerization occurred in a Src family kinase dependent manner. Clustering of liganded integrins recruits various adaptor proteins and serves as a reaction core for mechanobiological activities. In addition, there are future possibilities to investigate the role of other synergetic interactions with the activated integrin receptors. © 2012 Landes Bioscience.
Persistent Identifierhttp://hdl.handle.net/10722/202153
ISSN
2015 Impact Factor: 3.306
2015 SCImago Journal Rankings: 1.843
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYu, Chenghan-
dc.contributor.authorLuo, Weiwei-
dc.contributor.authorSheetz, Michael P.-
dc.date.accessioned2014-08-22T02:57:44Z-
dc.date.available2014-08-22T02:57:44Z-
dc.date.issued2012-
dc.identifier.citationCell Adhesion and Migration, 2012, v. 6, n. 3, p. 280-284-
dc.identifier.issn1933-6918-
dc.identifier.urihttp://hdl.handle.net/10722/202153-
dc.description.abstractIntegrin receptors play important roles in cell adhesion and tumor metastasis. The coupling of mechanical sensing and biochemical ligation is known to collectively regulate the activation of integrin receptors. Recently, oligomerization of activated integrins has been considered as the primordial signature of cytoskeletal remodeling and the initiation of various downstream signals, such as focal and fibrillar adhesions. However, spatio-temporal reorganization of activated integrins and associated proteins remains poorly understood. Here, we summarized the recent discovery of sequential biophysical events of integrin activation during early adhesion formation. Using the cyclic Arg-Gly-Asp (RGD) peptide as a mobile ligand on supported lipid membranes, a series of previously unreported events were observed following integrin avb3 clustering and cell spreading, including a long-range lateral translocation of the integrin clusters. With initial clustering, localized actin polymerization occurred in a Src family kinase dependent manner. Clustering of liganded integrins recruits various adaptor proteins and serves as a reaction core for mechanobiological activities. In addition, there are future possibilities to investigate the role of other synergetic interactions with the activated integrin receptors. © 2012 Landes Bioscience.-
dc.languageeng-
dc.relation.ispartofCell Adhesion and Migration-
dc.subjectTumor metastasis-
dc.subjectActin polymerization-
dc.subjectSynergy receptor-
dc.subjectSupported lipid membrane-
dc.subjectRGD peptide-
dc.subjectIntegrin-
dc.subjectSrc family kinase-
dc.titleSpatial-temporal reorganization of activated integrins-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.4161/cam.20753-
dc.identifier.pmid22863737-
dc.identifier.scopuseid_2-s2.0-84864920732-
dc.identifier.volume6-
dc.identifier.issue3-
dc.identifier.spage280-
dc.identifier.epage284-
dc.identifier.eissn1933-6926-
dc.identifier.isiWOS:000307868700016-

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