English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/23953
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Protein kinase C V3 domain mutants with differential sensitivities to m-calpain are not resistant to phorbol-ester-induced down-regulation

AuthorsJunco, María; Webster, Catherine; Crawford, Catherine; Boscá, Lisardo ; Parker, Peter J.
Issue Date1-Jul-1994
PublisherBlackwell Publishing
CitationThe Febs Journal 223(1): 259-263 (1994)
AbstractDistinct linker sequences were introduced into the protease-sensitive V3 domain of protein kinase C-α and the mutant proteins were expressed in COS-1 cells. Partially purified preparations of these mutants were functionally similar to wild-type protein kinase C-α, however their susceptibility to m-calpain was quite distinct, with one mutant being insensitive to cleavage. The three mutants, after expression in COS-1 cells, were found to behave in a manner indistinguishable from wild-type protein kinase C-α with respect to subcellular distribution, acute responses to 12-O-tetradecanoyl-phorbol 13-acetate and 12-O-tetradecanoyl-phorbol-13-acetate-induced down-regulation. The data imply that down-regulation of protein kinase C-α is likely to involve a general degradative process rather than cleavage by a site-specific protease.
Description5 páginas, 5 figures.
Publisher version (URL)http://dx.doi.org/10.1111/j.1432-1033.1994.tb18990.x
URIhttp://hdl.handle.net/10261/23953
DOI10.1111/j.1432-1033.1994.tb18990.x
ISSN0014-2956
Appears in Collections:(IIBM) Artículos
Files in This Item:
File Description SizeFormat 
wiley.pdf548,82 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.