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dc.contributor.authorPereda, José M. de-
dc.date.accessioned2012-11-12T12:20:21Z-
dc.date.available2012-11-12T12:20:21Z-
dc.date.issued2006-
dc.identifierdoi: 10.1016/j.tcb.2006.05.004-
dc.identifierissn: 0962-8924-
dc.identifiere-issn: 1879-3088-
dc.identifier.citationTrends in Cell Biology 16(7): 376-383 (2006)-
dc.identifier.urihttp://hdl.handle.net/10261/60007-
dc.descriptionet al.-
dc.description.abstractHemidesmosomes are multiprotein adhesion complexes that promote epithelial stromal attachment in stratified and complex epithelia. Modulation of their function is of crucial importance in a variety of biological processes, such as differentiation and migration of keratinocytes during wound healing and carcinoma invasion, in which cells become detached from the substrate and acquire a motile phenotype. Although much is known about the signaling potential of the α6β4 integrin in carcinoma cells, the events that coordinate the disassembly of hemidesmosomes during differentiation and wound healing remain unclear. The binding of α6β4 to plectin has a central role in hemidesmosome assembly and it is becoming clear that disrupting this interaction is a crucial event in hemidesmosome disassembly. In addition, further insight into the functional interplay between α3β1 and α6β4 has contributed to our understanding of hemidesmosome disassembly and cell migration. © 2006 Elsevier Ltd. All rights reserved.-
dc.language.isoeng-
dc.publisherElsevier-
dc.rightsclosedAccess-
dc.titleCurrent insights into the formation and breakdown of hemidesmosomes-
dc.typeartículo-
dc.identifier.doi10.1016/j.tcb.2006.05.004-
dc.date.updated2012-11-12T12:20:21Z-
dc.description.versionPeer Reviewed-
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairetypeartículo-
item.grantfulltextnone-
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.languageiso639-1en-
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