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Titolo:
FUNCTIONAL-ANALYSIS OF DESMOPLAKIN DOMAINS - SPECIFICATION OF THE INTERACTION WITH KERATIN VERSUS VIMENTIN INTERMEDIATE FILAMENT NETWORKS
Autore:
STAPPENBECK TS; BORNSLAEGER EA; CORCORAN CM; LUU HH; VIRATA MLA; GREEN KJ;
Indirizzi:
NORTHWESTERN UNIV,SCH MED,DEPT PATHOL CHICAGO IL 60611 NORTHWESTERN UNIV,SCH MED,ROBERT H LURIE CANC CTR CHICAGO IL 60611 NORTHWESTERN UNIV,SCH MED,DEPT DERMATOL CHICAGO IL 60611
Titolo Testata:
The Journal of cell biology
fascicolo: 3, volume: 123, anno: 1993,
pagine: 691 - 705
SICI:
0021-9525(1993)123:3<691:FODD-S>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
BULLOUS PEMPHIGOID ANTIGEN; DESMOSOMAL PLAQUE PROTEINS; KIDNEY EPITHELIAL-CELLS; CYTOPLASMIC DOMAIN; PLASMA-MEMBRANE; ORGANIZATION; EXPRESSION; PLECTIN; FAMILY; CDNAS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
51
Recensione:
Indirizzi per estratti:
Citazione:
T.S. Stappenbeck et al., "FUNCTIONAL-ANALYSIS OF DESMOPLAKIN DOMAINS - SPECIFICATION OF THE INTERACTION WITH KERATIN VERSUS VIMENTIN INTERMEDIATE FILAMENT NETWORKS", The Journal of cell biology, 123(3), 1993, pp. 691-705

Abstract

We previously demonstrated that truncated desmoplakin I (DP I) molecules containing the carboxyl terminus specifically coalign with and disrupt both keratin and vimentin intermediate filament (IF) networks when overexpressed in tissue culture cells (Stappenbeck, T. S., and K. J. Green. J. Cell Biol. 116:1197-1209). These experiments suggested thatthe DP carboxyl-terminal domain is involved either directly or indirectly in linking IF with the desmosome. Using a similar approach, we have now investigated the behavior of ectopically expressed full-length DP I in cultured cells. In addition, we have further dissected the functional sequences in the carboxyl terminus of DP I that facilitate theinteraction with IF networks. Transient transfection of a clone encoding full-length DP I into COS-7 cells produced protein that appeared in some cells to associate with desmosomes and in others to coalign with and disrupt IF Deletion of the carboxyl terminus from this clone resulted in protein that still appeared capable of associating with desmosomes but not interacting with IF networks. As the amino terminus appeared to be dispensable for IF interaction, we made finer deletions in the carboxyl terminus of DP based on blocks of sequence similarity with the related molecules bullous pemphigoid antigen and plectin. We found a sequence at the very carboxyl terminus of DP that was necessary for coalignment with and disruption of keratin IF but not vimentin IF. Furthermore, the coalignment of specific DP proteins along keratin IF but not vimentin IF was correlated with resistance to extraction by Triton. The striking uncoupling resulting from the deletion of specific DP sequences suggests that the carboxyl terminus of DP interacts differentially with keratin and vimentin IF networks.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 01:00:30