dc.creator | Muñiz Guinea, Manuel | es |
dc.creator | Alonso, Manuel | es |
dc.creator | Hidalgo Jiménez, Josefina | es |
dc.creator | Velasco López, Ángel | es |
dc.date.accessioned | 2016-05-03T11:52:53Z | |
dc.date.available | 2016-05-03T11:52:53Z | |
dc.date.issued | 1996 | |
dc.identifier.citation | Muñiz Guinea, M., Alonso, M., Hidalgo Jiménez, J. y Velasco López, Á. (1996). A Regulatory Role for cAMP-dependent Protein Kinase in Protein Traffic along the Exocytic Route. The Journal of Biological Chemistry, 271 (48), 30935. | |
dc.identifier.issn | 1083-351X | es |
dc.identifier.uri | http://hdl.handle.net/11441/40673 | |
dc.description.abstract | The influence of protein kinase A activity on transport
of newly synthesized vesicular stomatitis virus G glycoprotein
along the exocytic pathway was examined.
Transport of vesicular stomatitis virus G glycoprotein to
the cell surface was inhibited by N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide
(H-89), a
selective inhibitor of protein kinase A. This block occurred
at the exit of the Golgi complex, whereas transport
through the Golgi compartments or from the endoplasmic
reticulum to the Golgi was decreased in the
presence of H-89. As judged by immunofluorescence endoplasmic
reticulum to Golgi transport was accelerated
in cells incubated with activators of protein kinase A
such as isobutylmethylxanthine (IBMX) or forskolin
(FK). Treatment with IBMX and FK also increased transport
from the trans-Golgi network to the cell surface.
During incubation with IBMX and FK, the organization
of the Golgi complex was altered showing intercisternae
fusion and miscompartmentalization of resident proteins.
These structural changes affected both the kinetics
of acquisition of endoglycosidase H resistance and
transport activities. These data support a differential
regulatory role for protein kinase A in different transport
steps along the exocytic pathway. In particular,
transport from the trans-Golgi network to the cell surface
was dependent on protein kinase A activity. In
addition, the results suggest the involvement of this
enzyme on the maintenance of the Golgi complex
organization. | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | The American Society for Biochemistry and Molecular Biology | es |
dc.relation.ispartof | The Journal of Biological Chemistry, 271 (48), 30935. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | A Regulatory Role for cAMP-dependent Protein Kinase in Protein Traffic along the Exocytic Route | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Biología Celular | es |
dc.relation.publisherversion | http://www.jbc.org/content/271/48/30935.full.pdf+html | es |
idus.format.extent | 8 | es |
dc.journaltitle | The Journal of Biological Chemistry | |
dc.publication.volumen | 271 | |
dc.publication.issue | 48 | |
dc.publication.initialPage | 30935 | |
dc.identifier.idus | https://idus.us.es/xmlui/handle/11441/40673 | |