The type I keratin 19 possesses distinct and context-dependent assembly properties

DC FieldValueLanguage
dc.contributor.authorFradette, Julie-
dc.contributor.authorGermain, Lucie-
dc.contributor.authorSeshaiah, Partha-
dc.contributor.authorCoulombe, Pierre A.-
dc.date.accessioned2018-01-23T19:44:50Z-
dc.date.available2018-01-23T19:44:50Z-
dc.date.issued1998-12-25-
dc.identifier.issn0021-9258fr
dc.identifier.urihttp://hdl.handle.net/20.500.11794/16575-
dc.description.abstractKeratins (K), the cytoplasmic intermediate filament (IF) proteins of epithelial cells, are encoded by a multigene family and expressed in a tissue- and differentiation-specific manner. In human skin, keratinocytes of the basal layer of epidermis and the outer root sheath of hair follicles express K5 and K14 as their main keratins. A small subpopulation of basal cells exhibiting stem-cell like characteristics express, in addition, K19. At 40 kDa, this keratin is the smallest IF protein due to an exceptionally short carboxyl-terminal domain. We examined the assembly properties of K19 and contrasted them to K14 in vitro and in vivo. Relative to K5-K14, we find that K5-K19 form less stable tetramers that polymerize into shorter and narrower IFs in vitro. When transiently co-expressed in cultured baby hamster kidney cells, the K5 and K19 combination fails to form a filamentous array, whereas the K5-K14 and K8-K19 ones readily do so. Transient expression of K19 in the epithelial cell lines T51B-Ni and A431 results in its integration into the endogenous keratin network with minimal if any perturbation. Collectively, these results indicate that K19 possesses assembly properties that are distinct from those of K14 and suggest that it may impart unique properties to the basal cells expressing it in skin epithelia.fr
dc.languageengfr
dc.publisherAmerican Society of Biological Chemistsfr
dc.titleThe type I keratin 19 possesses distinct and context-dependent assembly propertiesfr
dc.typeCOAR1_1::Texte::Périodique::Revue::Contribution à un journal::Article::Article de recherchefr
dcterms.bibliographicCitationJournal of biological chemistry, Vol. 273 (52), 5176–35184 (1998)fr
dc.identifier.doi10.1074/jbc.273.52.35176fr
dc.identifier.pubmed9857055fr
dc.subject.rvmKératinefr
dc.subject.rvmKératinocytesfr
rioxxterms.versionVersion of Recordfr
rioxxterms.version_of_recordhttps://doi.org/10.1074/jbc.273.52.35176fr
rioxxterms.project.funder_nameNational Science Foundationfr
rioxxterms.project.funder_nameNational Institutes of Healthfr
rioxxterms.project.funder_nameMedical Research Council Canadafr
bul.rights.periodeEmbargo12 moisfr
dc.audience.peerreviewOuifr
Collection:Articles publiés dans des revues avec comité de lecture

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