Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/79981
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Phosphorylation of calmodulin: Functional implications |
Autor: | Benaim, Gustavo; Villalobo, Antonio CSIC ORCID | Fecha de publicación: | 2002 | Editor: | Wiley-Blackwell | Citación: | European Journal of Biochemistry 269(15): 3619-3631 (2002) | Resumen: | Calmodulin (CaM) is phosphorylated in vitro and in vivo by multiple protein-serine/threonine and protein-tyrosine kinases. Casein kinase II and myosin light-chain kinase are two of the well established protein-serine/threonine kinases implicated in this process. On the other hand, within the protein-tyrosine kinases involved in the phosphorylation of CaM are receptors with tyrosine kinase activity, such as the insulin receptor and the epidermal growth factor receptor, and nonreceptor protein-tyrosine kinases, such as several members of the Src family kinases, Janus kinase 2, and p38Syk. The phosphorylation of CaM brings important physiological consequences for the cell as the diverse phosphocalmodulin species have differential actions as compared to nonphosphorylated CaM when acting on different CaM-dependent systems. In this review we will summarize the progress made on this topic as the first report on phosphorylation of CaM was published almost two decades ago. We will emphasize the description of the phosphorylation events mediated by the different protein kinases not only in the test tube but in intact cells, the phosphorylation-mediated changes of CaM activity, its action on CaM-dependent systems, and the functional repercussion of these phosphorylation processes in the physiology of the cell. | Descripción: | Journal now known as FEBS Journal.-- Open Access content older than 1 year. | Versión del editor: | http://dx.doi.org/10.1046/j.1432-1033.2002.03038.x | URI: | http://hdl.handle.net/10261/79981 | DOI: | 10.1046/j.1432-1033.2002.03038.x | Identificadores: | doi: 10.1046/j.1432-1033.2002.03038.x issn: 0014-2956 e-issn: 1432-1033 |
Aparece en las colecciones: | (IIBM) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
Phosphorylation of calmodulin.pdf | 293,44 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
129
checked on 20-mar-2024
WEB OF SCIENCETM
Citations
121
checked on 28-feb-2024
Page view(s)
1.492
checked on 28-mar-2024
Download(s)
1.939
checked on 28-mar-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.