Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase

8 pages, 9 figures.-- Now known as FEBS Journal: Open Access content older than 1 year.

Detalles Bibliográficos
Autores: Benguria, Alberto, Hernández-Perera, Octavio, Martínez-Pastor, María Teresa, Sacks, David B., Villalobo, Antonio
Tipo de recurso: artículo
Fecha de publicación:1994
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/23937
Acceso en línea:http://hdl.handle.net/10261/23937
Access Level:acceso abierto
id ES_188c7c6b4cf0dae222c7bc2ec977c8da
oai_identifier_str oai:digital.csic.es:10261/23937
network_acronym_str ES
network_name_str España
repository_id_str
spelling Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinaseBenguria, AlbertoHernández-Perera, OctavioMartínez-Pastor, María TeresaSacks, David B.Villalobo, Antonio8 pages, 9 figures.-- Now known as FEBS Journal: Open Access content older than 1 year.An epidermal-growth-factor(EGF)-receptor preparation isolated by calmodulin-affinity chromatography from rat liver plasma membranes is able to phosphorylate calmodulin. Calmodulin phosphorylation was enhanced 3–8-fold by EGF, was dependent on the presence of a polycation or basic protein and was inhibited by micromolar concentrations of Ca2+. Phosphate incorporation into calmodulin occurs predominantly on tyrosine residues. Partial proteolysis of phosphocalmodulin by thrombin identifies Tyr99, located in the third calcium-binding domain of calmodulin, as the phosphorylated residue. Stoichiometric measurements show a 32P/calmodulin molar ratio of approximately 1 when optimal phosphorylation conditions are used.This work was supported in part by Research Grants to A. V. from the Comisión Interministerial de Ciencia y Tecnología (SAF392/93), and from the Secretaria de Educación de la Comunidad de Madrid (366/92). A. B. is the recipient of a predoctoral fellowship from the Departamento de Educación, Universidades e Investigación del Gobierno Vasco, 0. H.-P. is the recipient of a predoctoral fellowships from the Cabildo Insular de Gran Canaria, Fundacion Universitaria de Las Palmas, and from the Funducidn Científica de la Asociación Española Contra el Cancer, and M. T. M.-P. is the recepient of an undergraduate traineeship from the Consejo Superior de Investigaciones Cientipcas. Work at D. B. S. lab was supported by Research Grant DK43682 from the National Institutes of Health. USA.Peer reviewedWiley-Blackwell201020101994info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_65011080618 bytesapplication/pdfhttp://hdl.handle.net/10261/23937reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1111/j.1432-1033.1994.00909.xinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/239372026-05-22T06:33:51Z
dc.title.none.fl_str_mv Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase
title Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase
spellingShingle Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase
Benguria, Alberto
title_short Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase
title_full Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase
title_fullStr Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase
title_full_unstemmed Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase
title_sort Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase
dc.creator.none.fl_str_mv Benguria, Alberto
Hernández-Perera, Octavio
Martínez-Pastor, María Teresa
Sacks, David B.
Villalobo, Antonio
author Benguria, Alberto
author_facet Benguria, Alberto
Hernández-Perera, Octavio
Martínez-Pastor, María Teresa
Sacks, David B.
Villalobo, Antonio
author_role author
author2 Hernández-Perera, Octavio
Martínez-Pastor, María Teresa
Sacks, David B.
Villalobo, Antonio
author2_role author
author
author
author
description 8 pages, 9 figures.-- Now known as FEBS Journal: Open Access content older than 1 year.
publishDate 1994
dc.date.none.fl_str_mv 1994
2010
2010
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/23937
url http://hdl.handle.net/10261/23937
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1111/j.1432-1033.1994.00909.x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 1080618 bytes
application/pdf
dc.publisher.none.fl_str_mv Wiley-Blackwell
publisher.none.fl_str_mv Wiley-Blackwell
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869403992313823232
score 15,811543