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

En cours de chargement...
Vignette d'image
Date
1998-12-25
Auteurs
Seshaiah, Partha
Coulombe, Pierre A.
Direction de publication
Direction de recherche
Titre de la revue
ISSN de la revue
Titre du volume
Éditeur
American Society of Biological Chemists
Projets de recherche
Structures organisationnelles
Numéro de revue
Résumé
Keratins (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.
Description
Revue
Journal of biological chemistry, Vol. 273 (52), 5176–35184 (1998)
DOI
10.1074/jbc.273.52.35176
URL vers la version publiée
Mots-clés
Citation
Type de document
article de recherche